The vertical distribution of subseafloor archaeal communities is regarded as primarily managed by in situ situations in sediments similar to the availability of electron acceptors and donors, though sharp group shifts have additionally been noticed at lithological boundaries suggesting that at the very least a subset of vertically stratified Archaea kind a long-term genetic document of coinciding environmental situations that occurred at the time of sediment deposition. To substantiate this chance, we carried out a extremely resolved 16S rRNA gene survey of vertically stratified archaeal communities paired with paleo-oceanographic proxies in a sedimentary document from the northern Red Sea spanning the final glacial-interglacial cycle (i.e., marine isotope levels 1-6; MIS1-6).
Our outcomes present a powerful vital correlation between subseafloor archaeal communities and drastic paleodepositional changes related to glacial low vs. interglacial excessive stands (ANOSIM; R = .73; p = .001) and solely a reasonably robust correlation with lithological changes. Bathyarchaeota, Lokiarchaeota, MBGA, and DHVEG-1 had been the most ample recognized archaeal teams. Whether they represented historic cell traces from the time of deposition or migrated to the particular sedimentary horizons after deposition stays speculative. However, we present that the majority of sedimentary archaeal tetraether membrane lipids had been of allochthonous origin and never produced in situ.
Slow post-burial progress below energy-limited situations would clarify why the downcore distribution of these dominant archaeal teams nonetheless not directly reflect changes in the paleodepositional atmosphere that prevailed throughout the analyzed marine isotope levels. In addition, archaea seeded from the overlying water column similar to Thaumarchaeota and group II and III Euryarchaeota, which had been probably not have been capable of subsist after burial, had been recognized from a decrease abundance of preserved sedimentary DNA signatures, and represented direct markers of paleoenvironmental changes in the Red Sea spanning the final six marine isotope levels.
Harnessing paleo-environmental modeling and genetic information to foretell intraspecific genetic construction
Spatially express simulations of gene circulation inside advanced landscapes might assist forecast the responses of populations to international and anthropological changes. Simulating how previous local weather change formed intraspecific genetic variation can present a validation of fashions in anticipation of their use to foretell future changes. We overview simulation fashions that present inferences on inhabitants genetic construction. Existing simulation fashions usually combine advanced demographic and genetic processes however are much less centered on the panorama dynamics. In distinction to earlier approaches integrating detailed demographic and genetic processes and solely secondarily panorama dynamics, we current a mannequin primarily based on parsimonious organic mechanisms combining habitat suitability and mobile processes, relevant to advanced landscapes.
The simulation mannequin takes as enter (a) the species dispersal capacities as the principal organic parameter, (b) the species habitat suitability, and (c) the panorama construction, modulating dispersal. Our mannequin emphasizes the position of panorama options and their temporal dynamics in producing genetic differentiation amongst populations inside species. We illustrate our mannequin on caribou/reindeer populations sampled throughout the total species distribution vary in the Northern Hemisphere. We present that simulations over the previous 21 kyr predict a inhabitants genetic construction that matches empirical information. This strategy taking a look at the affect of historic panorama dynamics on intraspecific construction can be utilized to forecast inhabitants construction below local weather change eventualities and consider how species vary shifts may induce erosion of genetic variation inside species.
Bermudagrass (Cynodon dactylon Pers.) is a crucial warm-season perennial used extensively for turf, forage, soil conservation and remediation worldwide. However, restricted genomic info has hindered the software of molecular instruments in the direction of understanding genome evolution and in breeding new cultivars. We genotype a first-generation selfed inhabitants derived from the tetraploid (4x = 36) ‘A12359’ utilizing genotyping-by-sequencing. A high-density genetic map of 18 linkage teams (LGs) is constructed with 3,544 markers. Comparative genomic analyses reveal that every of 9 homeologous LG pairs of C. dactylon corresponds to at least one of the first 9 chromosomes of Oropetium thomaeum.
Phylotranscriptomics in Cucurbitaceae Reveal Multiple Whole-Genome Duplications and Key Morphological and Molecular Innovations
The capacity of climbing crops to develop upward alongside others to succeed in the cover for photosynthesis is hypothesized as a key innovation in flowering crops. Most members of the Cucurbitaceae, a household containing ∼1000 species and lots of necessary crops, are climbers and have attribute tendrils and pepo fruits. Here, we current 127 newly sequenced transcriptomes and genomes together with different datasets for a complete of 136 cucurbits representing all tribes to ascertain a strong Cucurbitaceae phylogeny containing eight extremely resolved main clades.
We analyzed whole-genome duplication, diversification dynamics, and ancestral morphologies, and located that after early genome duplication occasion(s), a burst of diversification and morphological improvements in flower, fruit, and root characters occurred below the local weather optimum in the Early Eocene. Species radiation throughout the Mid-Eocene Climatic Optimum additionally coincided with a number of morphological changes shared by 80% of cucurbits. We discovered that the cucurbit-specific tendril identification gene TEN originated from a paleo-polyploidization occasion at the origin of the household.
Mouse anti VEGFR-1/Flt-1 (#EIC) (human) |
101-M26 |
Angio Proteomie |
100ug |
EUR 297.6 |
Mouse anti VEGFR-1/Flt-1 (#EWF) (human) |
101-M28 |
Angio Proteomie |
100ug |
EUR 297.6 |
Mouse anti VEGFR-1/Flt-1 (#EWI) (human) |
101-M30 |
Angio Proteomie |
100ug |
EUR 297.6 |
anti- VEGFR-1/FLT-1 antibody |
FNab09393 |
FN Test |
100µg |
EUR 606.3 |
|
Description: Antibody raised against VEGFR-1/FLT-1 |
Anti-Human VEGFR-1/Flt-1 Antibody |
102-PA20 |
ReliaTech |
200 µg |
EUR 173.25 |
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. |
Anti-Human VEGFR-1/Flt-1 Antibody |
102-PABi20 |
ReliaTech |
50 µg |
EUR 157.5 |
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. |
Anti-Human VEGFR-1/Flt-1 Antibody |
101-MBi24 |
ReliaTech |
50 µg |
EUR 246.75 |
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. |
Anti-Human VEGFR-1/Flt-1 Antibody |
101-MBi30 |
ReliaTech |
50 µg |
EUR 189 |
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. |
Mouse anti VEGFR-3/Flt-4 (#1) (human) |
101-M36 |
Angio Proteomie |
100ug |
EUR 297.6 |
Mouse anti VEGFR-1/Flt-1-Biotin (#EWF) (human) |
101-MBi28 |
Angio Proteomie |
50ug |
EUR 297.6 |
VEGFR-1/FLT-1 antibody |
E39-09393 |
EnoGene |
100ug/100ul |
EUR 225 |
Description: Available in various conjugation types. |
VEGFR-1 / FLT-1 Antibody |
abx239393-100ug |
Abbexa |
100 ug |
EUR 577.2 |
|
Anti-Mouse VEGFR-1/Flt-1 Antibody |
103-M31 |
ReliaTech |
100 µg |
EUR 399 |
Description: Vascular Endothelial Growth Factor (VEGF or VEGF-A) family members are major mediators of vasculogenesis and angiogenesis. Specifically, biological activities attributed to VEGFs include: mitogenic activity on endothelial cells, increased permeability of endothelial cells to proteins, stimulation of monocyte migration across endothelial cells and angiogenic activity. Three VEGF family receptors have been described: Flt-1 (fms-like tyrosine kinase) also known as VEGF R1, KDR (kinase-insert domain-containing receptor) also known as Flk-1 and VEGF R2, and Flt-4 also known as VEGF R3. The three receptors contain seven extracellular immunoglobulin-like domains and share substantial sequence homology. In addition, neuropilin-1, a neuronal receptor, also acts as a co-receptor for VEGF when expressed on vascular endothelial cells, endothelial cell progenitors and monocytes. VEGF R1 is expressed primarily on endothelial cells but is also found on human peripheral blood monocytes. Through its endothelial mitogenic and hyperpermeability activities, VEGF influences a variety of immune functions related to wound healing and blood protein traffic across endothelial barriers. |
Mouse anti VEGFR-3/Flt-4-Biotin (#1) (human) |
101-MBi36 |
Angio Proteomie |
50ug |
EUR 297.6 |
Recombinant Human FLT-1/VEGFR-1 Protein |
RP01137 |
Abclonal |
50μg |
EUR 308.75 |
|
Anti-Human VEGFR-1/Flt-1 (Peptide), soluble Antibody |
102-PA21S |
ReliaTech |
100 µg |
EUR 126 |
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. |
Rabbit Anti-Human VEGFR-1 Flt-1 (Peptide), soluble |
102-PA21 |
Angio Proteomie |
100ug |
EUR 240 |
Active Recombinant Human FLT-1/VEGFR-1 Protein |
RP01188 |
Abclonal |
5 μg |
EUR 32.5 |
|
Human FLT-1/VEGFR-1 Control/blocking peptide #1 |
FLT11-P |
Alpha Diagnostics |
100 ug |
EUR 196.8 |
Anti-Hu/Mo VEGFR-1/Flt-1, Antagonistic Antibody |
mV1004.1m-h-m |
ReliaTech |
100 µg |
EUR 645.75 |
Description: Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The antibody will bind near the ligand binding site of the receptor and has antagonistic activity by blocking the binding of natural ligands. |
Biotinylated Recombinant Human FLT-1/VEGFR-1 Protein |
RP02100 |
Abclonal |
500μg |
EUR 2843.75 |
|
Rabbit Anti-human FLT-1/VEGFR-1 IgG #1, aff pure |
FLT11-A |
Alpha Diagnostics |
100 ul |
EUR 578.4 |
Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein |
S01-011 |
ReliaTech |
5 µg |
EUR 73.5 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D5), soluble Recombinant Protein |
S01-012 |
ReliaTech |
20 µg |
EUR 157.5 |
Description: Recombinat human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-5 (sVEGFR-1(D5)) is a 70 kDa protein containing amino acid residues. The baculovirus generated, recombinant human sVEGFR-1 is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 5 extracellular domains, which contain all the information necessary for high affinity ligand binding. The receptor monomers have a mass of approximately 70 kDa. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVE supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein |
S01-013 |
ReliaTech |
5 µg |
EUR 103.95 |
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D4), soluble Recombinant Protein |
S01-014 |
ReliaTech |
20 µg |
EUR 199.5 |
Description: Recombinant Human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-4 (sVEGFR-1(D4)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 4 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 55 kDa containing 457 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein |
S01-015 |
ReliaTech |
5 µg |
EUR 103.95 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (D3), soluble Recombinant Protein |
S01-016 |
ReliaTech |
20 µg |
EUR 199.5 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein |
S01-009 |
ReliaTech |
5 µg |
EUR 73.5 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor precursor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Human VEGFR-1/Flt-1 (native), soluble Recombinant Protein |
S01-010 |
ReliaTech |
20 µg |
EUR 157.5 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1) is the naturally occurring form and was cloned from total RNA of human umbilical vein endothelial cells. The recombinant mature sVEGFR-1 is a glycosylated monomeric protein with a mass of approximately 96 kDa. The soluble receptor protein consists of the first 6 extracellular domains (Met1-His688) containing the unique 31 amino acids residues at the C-terminus. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly, a naturally occurring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis binding VEGF with the same affinity as the full-length receptor. |
Anti-Human VEGFR-3/FLT-4 Antibody |
102-PA22 |
ReliaTech |
200 µg |
EUR 147 |
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (FIT1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelia cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system. |
Anti-Human VEGFR-3/FLT-4 Antibody |
102-PABi22 |
ReliaTech |
50 µg |
EUR 157.5 |
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (FIT1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelia cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system. |
Anti-Human VEGFR-3/FLT-4 Antibody |
101-M37 |
ReliaTech |
100 µg |
EUR 199.5 |
Description: VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk 1) and VEGFR-3 (FLT-4) belong to the class III subfamily of receptor tyrosine kinases (RTKs). All three receptors contain seven immunoglobulin-like repeats in their extracellular domains and kinase insert domains in their intracellular regions. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. These receptors play essential roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The VEGFR-3 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 24 aa residue signal peptide. Mature VEGFR-3 is composed of a 751 aa residue extracellular domain, a 22 aa residue transmembrane domain and a 482 aa residue cytoplasmic domain. Both VEGF-C and VEGF-D have been shown to bind and activate VEGF R3 (Flt-4). The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stage of development. It is important for lymphangiogenesis. |
Anti-Human VEGFR-3/FLT-4 Antibody |
101-M38 |
ReliaTech |
100 µg |
EUR 399 |
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (Flt1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides which remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelial cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system. |
Anti-Human VEGFR-3/FLT-4 Antibody |
101-M870 |
ReliaTech |
100 µg |
EUR 399 |
Description: Receptor tyrosine Kinase VEGFR-3, also known as FLT4, together with VEGFR1 (Flt1) and VEGFR2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides which remain linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelial cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system. |
Human VEGFR-1/Flt-1 (D3)-His, soluble Recombinant Protein |
S01-080 |
ReliaTech |
50 µg |
EUR 378 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 domain D1-3 (sVEGFR-1(D3)) is produced as a non-chimeric protein in a monomeric form. The soluble receptor protein contains only the first 3 extracellular domains, which contain all the information necessary for binding of VEGF. The receptor monomers have a mass of approximately 45 kDa containing 352 amino acid residues. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes, dendritic cells and on trophoblast cells. The flt-1 gene was first described in 1990. The receptor contains seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular splited tyrosine kinase domain. Compared to VEGFR-2 the Flt-1 receptor has a higher affinity for VEGF but a weaker signaling activity. VEGFR-1 thus leads not to proliferation of endothelial cells, but mediates signals for differentiation. Interestingly a naturally occuring soluble variant of VEGFR-1 (sVEGFR-1) was found in HUVEC supernatants in 1996, which is generated by alternative splicing of the flt-1 mRNA. The biological functions of sVEGFR-1 still are not clear, but it seems to be an endogenous regulator of angiogenesis, binding VEGF with the same affinity as the full-length receptor. |
Mouse Monoclonal Anti-human FLT-1/VEGFR-1 IgG, aff pure |
FLT12-M |
Alpha Diagnostics |
100 ug |
EUR 578.4 |
Mouse Monoclonal Anti-human FLT-1/VEGFR-1 IgG, aff pure |
FLT14-M |
Alpha Diagnostics |
100 ug |
EUR 578.4 |
Anti-Mouse VEGFR-3/FLT-4 Antibody |
103-M36 |
ReliaTech |
100 µg |
EUR 246.75 |
Description: VEGFR-3, also known as FLT4, is a member of the Tyr protein kinase family. The extracellular portion of VEGFR-3 contains 7 immunoglobulin (Ig)-like domains and the cytoplasmic portion contains a protein kinase domain. FLT4 regulates angiogenesis and lymphangiogenesis, its ligands are VEGF-C and D and its binding is mediated by the 2nd and 3rd Ig-like domains of FLT4. During fetal development VEGFR-3 is expressed on endothelial cells, however, in the adult mice, the vascular endothelial cells lose VEGFR-3 expression, but the lymphatic endothelium expresses it constitutively. In addition, VEGFR-3 expression can be induced in tumors with active angiogenesis. |
Anti-Mouse VEGFR-3/FLT-4 Antibody |
103-M38 |
ReliaTech |
100 µg |
EUR 399 |
Description: Receptor tyrosine kinase VEGFR-3, also known as Flt-4, together with VEGFR-1 (Flt-1) and VEGFR-2 (KDR/Flk-1), are the receptors for vascular endothelial growth factors (VEGF). The VEGFR family belongs to the class II subfamily of receptor tyrosine kinases (RTKs), containing a large extracellular region which is composed of seven Ig-like domains (D1–D7), a single transmembrane (TM) helix and cytoplasmic region with a tyrosine kinase activity. In VEGFR-3, the fifth Ig homology domain is proteolytically cleaved which results in polypeptides remaining linked by two disulfide bonds. VEGFR-3 is widely expressed on all endothelial cells in early embryogenesis, while, in adult tissues, VEGFR-3 expression disappears from the vascular endothelial cells and is observed only on the lymphatic endothelium. VEGF-C and VEGF-D activation of VEGFR-3 plays an important role in the formation of the lymphatic vessel system. |
Human VEGFR-3 / Flt-4 GENLISA ELISA |
KBH0215 |
Krishgen |
1 x 96 wells |
EUR 286 |
Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein |
SFC-005 |
ReliaTech |
10 µg |
EUR 57.75 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1(D7)/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1(D7)/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein |
SFC-006 |
ReliaTech |
50 µg |
EUR 168 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1(D7)) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1(D7)/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1(D7)/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Rabbit Anti-Mouse FLT-1/VEGFR-1 (279-299aa) IgG, aff pure |
FLT15-A |
Alpha Diagnostics |
100 ul |
EUR 578.4 |
Human VEGFR-3/FLT-4/Fc Chimera, soluble |
SFC-010 |
Angio Proteomie |
50ug |
EUR 378 |
Rabbit Anti-Mouse FLT-4/VEGFR-3 IgG #1, aff pure |
FLT41-A |
Alpha Diagnostics |
100 ug |
EUR 578.4 |
Active Recombinant Human VEGFR-3/FLT-4 Protein |
RP00123 |
Abclonal |
10 μg |
EUR 175.5 |
|
Human VEGFR-3/FLT-4, soluble Recombinant Protein |
S01-017 |
ReliaTech |
10 µg |
EUR 103.95 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis. |
Human VEGFR-3/FLT-4, soluble Recombinant Protein |
S01-017S |
ReliaTech |
5 µg |
EUR 63 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis. |
Human VEGFR-3/FLT-4, soluble Recombinant Protein |
S01-018 |
ReliaTech |
50 µg |
EUR 210 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3/FLT-4) was fused with a carboxy-terminal 6X histidine-tag. The recombinant mature sVEGFR-3/FLT-4 is a glycosylated monomeric protein. The sVEGFR-3/FLT-4 monomers have a mass of approximately 120 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23 aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751 aa residue extracellular domain, a 22 aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The Flt-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial a latter stages of development. It is important for lymphangiogenesis. |
FLT-1/VEGFR1 Human, Antibody |
GWB-BE9645 |
GenWay Biotech |
0.1 mg |
Ask for price |
Rat Monoclonal anti-Mouse VEGFR-3 (FLT-4) Antibody |
xAP-0836 |
Angio Proteomie |
100ug |
EUR 280 |
Mouse FLT-4/VEGFR-3 Control/blocking peptide #1 |
FLT41-P |
Alpha Diagnostics |
100 ug |
EUR 196.8 |
Human FLT-4/VEGFR-3 control/blocking peptide #2 |
FLT42-P |
Alpha Diagnostics |
100 ug |
EUR 196.8 |
Rabbit Anti-Human FLT-4/VEGFR-3 IgG #2, aff pure |
FLT42-A |
Alpha Diagnostics |
100 ug |
EUR 578.4 |
Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein |
SFC-M05 |
ReliaTech |
10 µg |
EUR 57.75 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1D1-7) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1D1-7/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1D1-7/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signalling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble Recombinant Protein |
SFC-M06 |
ReliaTech |
50 µg |
EUR 168 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-1 (sVEGFR-1D1-7) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-1D1-7/Fc is a disulfide-linked homodimeric protein. The sVEGFR-1D1-7/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Thr751), which contain all the information necessary for high affinity ligand binding. Endothelial cells express three different vascular endothelial growth factor (VEGF) receptors, belonging to the family of receptor tyrosine kinases (RTKs). They are named VEGFR-1 (Flt-1), VEGFR-2 (KDR/Flk-1), and VEGFR-3 (Flt-4). Their expression is almost exclusively restricted to endothelial cells, but VEGFR-1 can also be found on monocytes. All VEGF-receptors have seven immunoglobulin-like extracellular domains, a single transmembrane region and an intracellular split tyrosine kinase domain. VEGFR-2 has a lower affinity for VEGF than the Flt-1 receptor, but a higher signaling activity. Mitogenic activity in endothelial cells is mainly mediated by VEGFR-2 leading to their proliferation. Differential splicing of the flt-1 gene leads to the formation of a secreted, soluble variant of VEGFR-1 (sVEGFR-1). No naturally occurring, secreted forms of VEGFR-2 have so far been reported. The binding of VEGF165 to VEGFR-2 is dependent on heparin. |
Human VEGFR1/Flt-1 ELISA KIT |
E42EH-249 |
EnoGene |
96T/48T |
Ask for price |
Human VEGFR-1/Flt1 ELISA Kit |
EHV0045 |
Abclonal |
96Tests |
EUR 625.2 |
Human VEGFR-3/FLT-4/Fc Chimera, soluble Recombinant Protein |
SFC-009 |
ReliaTech |
10 µg |
EUR 73.5 |
Description: Recombinant human soluble Vascular Endothelial Growth Factor Receptor-3 (sVEGFR-3) was fused with the Fc part of human IgG1. The recombinant mature sVEGFR-3/Fc is a disulfide-linked homodimeric protein. The sVEGFR-3/Fc monomers have a mass of approximately 130 kDa. The soluble receptor protein consists of all 7 extracellular domains (Met1-Glu774). All three VEGF receptors belong to the class III subfamily of receptor tyrosine kinases (RTKs) characterised by the seven immunoglobulin-like loops in the extracellular domain. The expression of VEGFR-1 to -3 is almost exclusively restricted to hematopoietic precursor cells, vascular and lymphatic endothelial cells and to the monocyte/macrophage lineage. They play key roles in vasculogenesis, hematopoiesis, angiogenesis and lymphangiogenesis. The VEGFR-3/FLT-4 cDNA encodes a 1298 amino acid (aa) residue precursor protein with a 23aa residue signal peptide. Mature VEGFR-3/FLT-4 is composed of a 751aa residue extracellular domain, a 22aa transmembrane domain and a 482aa residue cytoplasmic domain. Both VEGF family members VEGF-C and VEGF-D have been shown to bind and activate VEGFR-3/FLT-4. The FLT-4 gene is widely expressed in the early embryo but becomes restricted to the lymphatic endothelial at latter stages of development. It is important for lymphangiogenesis. |
VEGFR-1/Flt1/ Rat VEGFR- 1/ Flt1 ELISA Kit |
ELA-E0147r |
Lifescience Market |
96 Tests |
EUR 1063.2 |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC940659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF594 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC940659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF594 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNCH0658-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), Horseradish Peroxidase conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNCH0658-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), Horseradish Peroxidase conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNCH0659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), Horseradish Peroxidase conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNCH0659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), Horseradish Peroxidase conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNUM0659-50 |
Biotium |
50uL |
EUR 474 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), 1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNC700658-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF770 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNC700658-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF770 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC700659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF770 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC700659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF770 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNC810658-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF680R conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNC810658-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF680R conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC810659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF680R conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC810659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF680R conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC880659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF488A conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC880659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF488A conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNC800658-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF680 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNC800658-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF680 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC800659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF680 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC800659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF680 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNC550658-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF555 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNC550658-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF555 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC550659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF555 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC550659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF555 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNC430658-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF543 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNC430658-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF543 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC430659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF543 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC430659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF543 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNC610658-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF660R conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNC610658-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF660R conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC610659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF660R conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC610659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF660R conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC470659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF647 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC470659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF647 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC680659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF568 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC680659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF568 conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNC050658-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF405M conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNC050658-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), CF405M conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC050659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF405M conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC050659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF405M conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC040659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF405S conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC040659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF405S conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC400659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF640R conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNC400659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), CF640R conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNCA0658-250 |
Biotium |
250uL |
EUR 459.6 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), APC conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNCA0659-250 |
Biotium |
250uL |
EUR 459.6 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), APC conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNCAP0658-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), Alkaline Phosphatase conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNCAP0658-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), Alkaline Phosphatase conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNCAP0659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), Alkaline Phosphatase conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNCAP0659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), Alkaline Phosphatase conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNCB0659-100 |
Biotium |
100uL |
EUR 238.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), Biotin conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNCB0659-500 |
Biotium |
500uL |
EUR 652.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), Biotin conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNCP0658-250 |
Biotium |
250uL |
EUR 459.6 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), PerCP conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNCP0659-250 |
Biotium |
250uL |
EUR 459.6 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), PerCP conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/658) Antibody |
BNCR0658-250 |
Biotium |
250uL |
EUR 459.6 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/658), RPE conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNCR0659-250 |
Biotium |
250uL |
EUR 459.6 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), RPE conjugate, Concentration: 0.1mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNUB0659-100 |
Biotium |
100uL |
EUR 250.8 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), Concentration: 0.2mg/mL |
VEGFR1 / Flt-1(FLT1/659) Antibody |
BNUB0659-500 |
Biotium |
500uL |
EUR 549.6 |
Description: Primary antibody against VEGFR1 / Flt-1(FLT1/659), Concentration: 0.2mg/mL |
Recombinant human VEGFR1/Flt-1 Protein, His Tag |
E40KMP1308 |
EnoGene |
20ug |
EUR 495 |
FLT-1/VEGFR1 Antibody (IHC Gold) |
E36PA577 |
EnoGene |
100ul |
EUR 225 |
Description: Available in various conjugation types. |
Recombinant Human VEGFR1/FLT-1 Protein, Avi His Tag |
E40KMP2138 |
EnoGene |
20ug |
EUR 495 |
Mouse Anti-Human Flt-1/VEGFR1 monoclonal antibody, clone JID688 |
CABT-L2814-100uL500uL |
Creative Diagnostics |
100 uL, 500 uL |
EUR 602.4 |
Mouse Anti-Human Flt-1/VEGFR1 monoclonal antibody, clone JID688 |
CABT-L2814 |
Creative Diagnostics |
100 µl, 500 µl |
Ask for price |
|
Description: Mouse |
Human Vascuar endothelial cell growth factor receptor 3(VEGFR-3,Flt-4) Elisa Kit |
EK712433 |
AFG Bioscience LLC |
96 Wells |
EUR 0.26 |
Human Vascuar endothelial cell growth factor receptor 3,VEGFR-3/Flt-4 ELISA Kit |
EKC40132-48T |
Biomatik Corporation |
48T |
EUR 474.04 |
Human Vascuar endothelial cell growth factor receptor 3,VEGFR-3/Flt-4 ELISA Kit |
EKC40132-5x96T |
Biomatik Corporation |
5x96T |
EUR 3216.7 |
Human Vascuar endothelial cell growth factor receptor 3,VEGFR-3/Flt-4 ELISA Kit |
EKC40132-96T |
Biomatik Corporation |
96T |
EUR 677.2 |
Human Vascuar endothelial cell growth factor receptor 3, VEGFR-3/Flt-4 ELISA Kit |
CSB-E04765h-24T |
Cusabio |
1 plate of 24 wells |
EUR 198 |
|
Description: Quantitative sandwich ELISA kit for measuring Human Vascuar endothelial cell growth factor receptor 3, VEGFR-3/Flt-4 in samples from serum, plasma, tissue homogenates. A new trial version of the kit, which allows you to test the kit in your application at a reasonable price. |
Human Vascuar endothelial cell growth factor receptor 3, VEGFR-3/Flt-4 ELISA Kit |
1-CSB-E04765h |
Cusabio |
-
Ask for price
-
Ask for price
-
Ask for price
|
- 1 plate of 96 wells
- 10 plates of 96 wells each
- 5 plates of 96 wells each
|
|
Description: Quantitative sandwich ELISA kit for measuring Human Vascuar endothelial cell growth factor receptor 3, VEGFR-3/Flt-4 in samples from serum, plasma, tissue homogenates. Now available in a cost efficient pack of 5 plates of 96 wells each, conveniently packed along with the other reagents in 5 separate kits. |
Human Vascuar endothelial cell growth factor receptor 3 (VEGFR-3/Flt-4) ELISA Kit |
RK12064 |
Abclonal |
96T |
EUR 280 |
VEGFR-1 |
E8RT1651 |
EnoGene |
100ul |
EUR 275 |
Description: Available in various conjugation types. |
Human Vascuoar endothelial cell growth factor receptor 3,VEGFR-3/Flt-4 ELISA Kit |
201-12-0216 |
SunredBio |
96 tests |
EUR 528 |
|
Description: A quantitative ELISA kit for measuring Human in samples from biological fluids. |
Human Vascuoar endothelial cell growth factor receptor 3(VEGFR-3/Flt-4)ELISA Kit |
GA-E0232HM-48T |
GenAsia Biotech |
48T |
EUR 346.8 |
Human Vascuoar endothelial cell growth factor receptor 3(VEGFR-3/Flt-4)ELISA Kit |
GA-E0232HM-96T |
GenAsia Biotech |
96T |
EUR 559.2 |
Human Vascuoar endothelial cell growth factor receptor 3(VEGFR-3/Flt-4)ELISA Kit |
QY-E00703 |
Qayee Biotechnology |
96T |
EUR 433.2 |
Human Vascuoar endothelial cell growth factor receptor 3,VEGFR-3/Flt-4 ELISA Kit |
YLA1379HU-48T |
Shanghai YL Biotech |
48T |
Ask for price |
Human Vascuoar endothelial cell growth factor receptor 3,VEGFR-3/Flt-4 ELISA Kit |
YLA1379HU-96T |
Shanghai YL Biotech |
96T |
Ask for price |
Rat VEGFR-1/Flt1 ELISA Kit |
ERV0045 |
Abclonal |
96Tests |
EUR 625.2 |
VEGFR-1 (Human, polyclonal, antagonistic) |
pV1004R-h |
Angio Proteomie |
100ug |
EUR 561 |
Mouse VEGFR1/Flt-1 ELISA KIT |
E42EM-191 |
EnoGene |
96T/48T |
Ask for price |
VEGFR1 / Flt-1(FLT1/658), 1mg/mL |
BNUM0658-50 |
Biotium |
50uL |
EUR 396 |
Description: Primary and secondary antibodies for multiple methodologyimmunostaining detection application |
VEGFR1 / Flt-1(FLT1/658), 0.2mg/mL |
BNUB0658-100 |
Biotium |
100uL |
EUR 225 |
Description: Primary and secondary antibodies for multiple methodologyimmunostaining detection application |
VEGFR1 / Flt-1(FLT1/658), 0.2mg/mL |
BNUB0658-500 |
Biotium |
500uL |
EUR 485 |
Description: Primary and secondary antibodies for multiple methodologyimmunostaining detection application |
Goat VEGFR-1/Flt1 ELISA Kit |
EGTV0045 |
Abclonal |
96Tests |
EUR 625.2 |
Human VEGFR3/Flt-4 ELISA Kit |
EK5791 |
SAB |
96 tests |
EUR 599 |
|
Mouse VEGFR-1/Flt1 ELISA Kit |
EMV0045 |
Abclonal |
96Tests |
EUR 625.2 |
VEGFR-1 Antibody |
48347-100ul |
SAB |
100ul |
EUR 399.6 |
VEGFR-1 Antibody |
48347-50ul |
SAB |
50ul |
EUR 286.8 |
Rabbit VEGFR-1/Flt1 ELISA Kit |
ERTV0045 |
Abclonal |
96Tests |
EUR 625.2 |
Canine VEGFR-1/Flt1 ELISA Kit |
ECV0045 |
Abclonal |
96Tests |
EUR 625.2 |
Bovine VEGFR-1/Flt1 ELISA Kit |
EBV0045 |
Abclonal |
96Tests |
EUR 625.2 |
Porcine VEGFR-1/Flt1 ELISA Kit |
EPV0045 |
Abclonal |
96Tests |
EUR 625.2 |
Anserini VEGFR-1/Flt1 ELISA Kit |
EAV0045 |
Abclonal |
96Tests |
EUR 625.2 |
VEGFR-1 (Human, monoclonal, agonistic) |
mV1004m-h |
Angio Proteomie |
100ug |
EUR 467.5 |
Biotinylated Recombinant Human VEGFR1/FLT-1 Protein, Avi His Tag |
E40KMP2104 |
EnoGene |
20ug |
EUR 495 |
Our outcomes help the speculation that cucurbit permutations had been in all probability pushed by elevated genetic variety following polyploidizations and by trait morphological improvements below paleo-climate upheavals. Our examine gives a phylogenetic framework and new insights into morphological and genomic changes underlying the adaptive evolution of Cucurbitaceae.