Subseafloor Archaea reflect 139 kyrs of paleodepositional changes in the northern Red Sea

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

Mouse anti VEGFR-3/Flt-4 (#1) (human)
101-M36	Angio Proteomie	100ug	EUR 297.6

Mouse Anti-Human VEGFR-1/Flt-1
MBS690002-01mg	MyBiosource	0.1mg	EUR 430

Mouse Anti-Human VEGFR-1/Flt-1
MBS690002-5x01mg	MyBiosource	5x0.1mg	EUR 1645

Mouse Anti-Human VEGFR-1/Flt-1
MBS690109-005mg	MyBiosource	0.05mg	EUR 450

Mouse Anti-Human VEGFR-1/Flt-1
MBS690109-5x005mg	MyBiosource	5x0.05mg	EUR 1725

Mouse Anti-Human VEGFR-1/Flt-1
MBS690355-01mg	MyBiosource	0.1mg	EUR 450

Mouse Anti-Human VEGFR-1/Flt-1
MBS690355-5x01mg	MyBiosource	5x0.1mg	EUR 1725

Mouse Anti-Human VEGFR-1/Flt-1
MBS690361-01mg	MyBiosource	0.1mg	EUR 450

Mouse Anti-Human VEGFR-1/Flt-1
MBS690361-5x01mg	MyBiosource	5x0.1mg	EUR 1725

Mouse Anti-Human VEGFR-1/Flt-1
MBS690384-005mg	MyBiosource	0.05mg	EUR 430

Mouse Anti-Human VEGFR-1/Flt-1
MBS690384-5x005mg	MyBiosource	5x0.05mg	EUR 1645

Mouse Anti-Human VEGFR-1/Flt-1
MBS690483-005mg	MyBiosource	0.05mg	EUR 430

Mouse Anti-Human VEGFR-1/Flt-1
MBS690483-5x005mg	MyBiosource	5x0.05mg	EUR 1645

Mouse Anti-Human VEGFR-1/Flt-1
MBS690832-01mg	MyBiosource	0.1mg	EUR 430

Mouse Anti-Human VEGFR-1/Flt-1
MBS690832-5x01mg	MyBiosource	5x0.1mg	EUR 1645

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.

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- VEGFR-1/FLT-1 antibody
FNab09393	FN Test	100µg	EUR 606.3
Description: Antibody raised against VEGFR-1/FLT-1

Mouse anti VEGFR-1/Flt-1-Biotin (#EWF) (human)
101-MBi28	Angio Proteomie	50ug	EUR 297.6

Human VEGFR-1/Flt-1 (D5), soluble
MBS691664-002mg	MyBiosource	0.02mg	EUR 380

Human VEGFR-1/Flt-1 (D5), soluble
MBS691664-5x002mg	MyBiosource	5x0.02mg	EUR 1410

Human VEGFR-1/Flt-1 (D5), soluble
MBS691669-0005mg	MyBiosource	0.005mg	EUR 265

Human VEGFR-1/Flt-1 (D5), soluble
MBS691669-5x0005mg	MyBiosource	5x0.005mg	EUR 890

Human VEGFR-1/Flt-1 (D3), soluble
MBS691717-002mg	MyBiosource	0.02mg	EUR 450

Human VEGFR-1/Flt-1 (D3), soluble
MBS691717-5x002mg	MyBiosource	5x0.02mg	EUR 1725

Human VEGFR-1/Flt-1 (D4), soluble
MBS691847-0005mg	MyBiosource	0.005mg	EUR 310

Human VEGFR-1/Flt-1 (D4), soluble
MBS691847-5x0005mg	MyBiosource	5x0.005mg	EUR 1110

Human VEGFR-1/Flt-1 (D3), soluble
MBS692000-0005mg	MyBiosource	0.005mg	EUR 310

Human VEGFR-1/Flt-1 (D3), soluble
MBS692000-5x0005mg	MyBiosource	5x0.005mg	EUR 1110

Human VEGFR-1/Flt-1 (D4), soluble
MBS692119-002mg	MyBiosource	0.02mg	EUR 450

Human VEGFR-1/Flt-1 (D4), soluble
MBS692119-5x002mg	MyBiosource	5x0.02mg	EUR 1725

Human VEGFR-1/Flt-1 (native), soluble
MBS691505-0005mg	MyBiosource	0.005mg	EUR 265

Human VEGFR-1/Flt-1 (native), soluble
MBS691505-5x0005mg	MyBiosource	5x0.005mg	EUR 890

Human VEGFR-1/Flt-1 (native), soluble
MBS691991-002mg	MyBiosource	0.02mg	EUR 380

Human VEGFR-1/Flt-1 (native), soluble
MBS691991-5x002mg	MyBiosource	5x0.02mg	EUR 1410

Mouse anti VEGFR-3/Flt-4-Biotin (#1) (human)
101-MBi36	Angio Proteomie	50ug	EUR 297.6

VEGFR-1 / FLT-1 Antibody
abx239393-100ug	Abbexa	100 ug	EUR 577.2

VEGFR-1/FLT-1 antibody
CAF50629-100ug	Biomatik Corporation	100ug	EUR 312

VEGFR-1/FLT-1 antibody
E39-09393	EnoGene	100ug/100ul	EUR 225
Description: Available in various conjugation types.

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.

Recombinant Human FLT-1/VEGFR-1 Protein
RP01137	Abclonal	50μg	EUR 308.2

Recombinant Human FLT-1/VEGFR-1 Protein
RP01188	Abclonal	5 μg	EUR 49.6

Recombinant Human FLT-1/VEGFR-1 Protein
RP02099	Abclonal	100μg	EUR 205.47

Human VEGFR-1/Flt-1 (D3)-His, soluble
MBS692528-005mg	MyBiosource	0.05mg	EUR 725

Human VEGFR-1/Flt-1 (D3)-His, soluble
MBS692528-5x005mg	MyBiosource	5x0.05mg	EUR 2965

Rabbit anti VEGFR-3/Flt-4 (human)
102-PA22AG	Angio Proteomie	50ug	EUR 240

Rabbit anti VEGFR-3/Flt-4 (human)
102-PA22S	Angio Proteomie	100ug	EUR 240

Anti-Human VEGFR-3/FLT-4 (#1) Antibody
MBS4158541-01mg	MyBiosource	0.1mg	EUR 920

Anti-Human VEGFR-3/FLT-4 (#1) Antibody
MBS4158541-5x01mg	MyBiosource	5x0.1mg	EUR 3880

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

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691483-005mg	MyBiosource	0.05mg	EUR 395

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691483-5x005mg	MyBiosource	5x0.05mg	EUR 1490

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691782-001mg	MyBiosource	0.01mg	EUR 245

Human VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691782-5x001mg	MyBiosource	5x0.01mg	EUR 805

Human FLT-1/VEGFR-1 Control/blocking peptide #1
FLT11-P	Alpha Diagnostics	100 ug	EUR 196.8

Biotinylated Recombinant Human FLT-1/VEGFR-1 Protein
RP02100	Abclonal	500μg	EUR 421.56

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.

Anti-Human VEGFR-l/Flt-1 (#EWC) Antibody
MBS4158536-01mg	MyBiosource	0.1mg	EUR 920

Anti-Human VEGFR-l/Flt-1 (#EWC) Antibody
MBS4158536-5x01mg	MyBiosource	5x0.1mg	EUR 3880

Anti-Human VEGFR-l/Flt-1 (#EIC) Antibody
MBS4158537-01mg	MyBiosource	0.1mg	EUR 920

Anti-Human VEGFR-l/Flt-1 (#EIC) Antibody
MBS4158537-5x01mg	MyBiosource	5x0.1mg	EUR 3880

Anti-Human VEGFR-l/Flt-1 (#EWF) Antibody
MBS4158538-01mg	MyBiosource	0.1mg	EUR 920

Anti-Human VEGFR-l/Flt-1 (#EWF) Antibody
MBS4158538-5x01mg	MyBiosource	5x0.1mg	EUR 3880

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.

Rabbit Anti-human FLT-1/VEGFR-1 IgG #1, aff pure
FLT11-A	Alpha Diagnostics	100 ul	EUR 578.4

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.

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.

Human VEGFR-3/FLT-4, soluble
MBS691602-001mg	MyBiosource	0.01mg	EUR 310

Human VEGFR-3/FLT-4, soluble
MBS691602-5x001mg	MyBiosource	5x0.01mg	EUR 1110

Human VEGFR-3/FLT-4, soluble
MBS691970-005mg	MyBiosource	0.05mg	EUR 465

Human VEGFR-3/FLT-4, soluble
MBS691970-5x005mg	MyBiosource	5x0.05mg	EUR 1805

Human VEGFR-3/FLT-4, soluble
MBS692181-0005mg	MyBiosource	0.005mg	EUR 250

Human VEGFR-3/FLT-4, soluble
MBS692181-5x0005mg	MyBiosource	5x0.005mg	EUR 835

Anti-Human VEGFR-l/Flt-1 (#EWF) Biotin Antibody
MBS4158553-005mg	MyBiosource	0.05mg	EUR 920

Anti-Human VEGFR-l/Flt-1 (#EWF) Biotin Antibody
MBS4158553-5x005mg	MyBiosource	5x0.05mg	EUR 3880

Anti-Human VEGFR-3/FLT-4 (CL 1) Biotin Antibody
MBS4158555-005mg	MyBiosource	0.05mg	EUR 920

Anti-Human VEGFR-3/FLT-4 (CL 1) Biotin Antibody
MBS4158555-5x005mg	MyBiosource	5x0.05mg	EUR 3880

Mouse Anti-Human VEGFR-3/FLT-4
MBS690017-01mg	MyBiosource	0.1mg	EUR 450

Mouse Anti-Human VEGFR-3/FLT-4
MBS690017-5x01mg	MyBiosource	5x0.1mg	EUR 1725

Mouse Anti-Human VEGFR-3/FLT-4
MBS690153-01mg	MyBiosource	0.1mg	EUR 450

Mouse Anti-Human VEGFR-3/FLT-4
MBS690153-5x01mg	MyBiosource	5x0.1mg	EUR 1725

Mouse Anti-Human VEGFR-3/FLT-4
MBS690532-005mg	MyBiosource	0.05mg	EUR 450

Mouse Anti-Human VEGFR-3/FLT-4
MBS690532-5x005mg	MyBiosource	5x0.05mg	EUR 1725

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.

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.

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

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.

Human VEGFR-3/FLT-4 ELISA (total)
MBS691467-0096mg	MyBiosource	0.096mg	EUR 815

Human VEGFR-3/FLT-4 ELISA (total)
MBS691467-5x0096mg	MyBiosource	5x0.096mg	EUR 3625

Human VEGFR-3 / Flt-4 GENLISA ELISA
KBH0215	Krishgen	1 x 96 wells	EUR 286

Recombinant Human VEGFR-3/FLT-4 Protein
RP00123	Abclonal	10 μg	EUR 102.73

Recombinant Human VEGFR-3/FLT-4 Protein
RP01797	Abclonal	100μg	EUR 42.51

Rat Anti-Mouse VEGFR-3/FLT-4
MBS690799-01mg	MyBiosource	0.1mg	EUR 450

Rat Anti-Mouse VEGFR-3/FLT-4
MBS690799-5x01mg	MyBiosource	5x0.1mg	EUR 1725

VEGFR-3/Flt-4
JP27779	Demeditec Diagnostics	96	EUR 611

VEGFR-3/FLT-4
MBS692733-01mg	MyBiosource	0.1mg	EUR 725

VEGFR-3/FLT-4
MBS692733-5x01mg	MyBiosource	5x0.1mg	EUR 2965

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (AP)
MBS6443139-01mL	MyBiosource	0.1mL	EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (AP)
MBS6443139-5x01mL	MyBiosource	5x0.1mL	EUR 4120

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (APC)
MBS6443140-01mL	MyBiosource	0.1mL	EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (APC)
MBS6443140-5x01mL	MyBiosource	5x0.1mL	EUR 4120

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (HRP)
MBS6443143-01mL	MyBiosource	0.1mL	EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (HRP)
MBS6443143-5x01mL	MyBiosource	5x0.1mL	EUR 4120

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (PE)
MBS6443149-01mL	MyBiosource	0.1mL	EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (PE)
MBS6443149-5x01mL	MyBiosource	5x0.1mL	EUR 4120

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (FITC)
MBS6443142-01mL	MyBiosource	0.1mL	EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (FITC)
MBS6443142-5x01mL	MyBiosource	5x0.1mL	EUR 4120

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.

Rabbit Anti-Mouse FLT-1/VEGFR-1 (279-299aa) IgG, aff pure
FLT15-A	Alpha Diagnostics	100 ul	EUR 578.4

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (Biotin)
MBS6443141-01mL	MyBiosource	0.1mL	EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (Biotin)
MBS6443141-5x01mL	MyBiosource	5x0.1mL	EUR 4120

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (AP)
MBS6417421-01mL	MyBiosource	0.1mL	EUR 950

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (AP)
MBS6417421-5x01mL	MyBiosource	5x0.1mL	EUR 4120

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (APC)
MBS6417422-01mL	MyBiosource	0.1mL	EUR 950

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (APC)
MBS6417422-5x01mL	MyBiosource	5x0.1mL	EUR 4120

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (HRP)
MBS6417425-01mL	MyBiosource	0.1mL	EUR 950

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (HRP)
MBS6417425-5x01mL	MyBiosource	5x0.1mL	EUR 4120

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (PE)
MBS6417431-01mL	MyBiosource	0.1mL	EUR 950

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (PE)
MBS6417431-5x01mL	MyBiosource	5x0.1mL	EUR 4120

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (FITC)
MBS6417424-01mL	MyBiosource	0.1mL	EUR 950

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (FITC)
MBS6417424-5x01mL	MyBiosource	5x0.1mL	EUR 4120

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (Biotin)
MBS6417423-01mL	MyBiosource	0.1mL	EUR 950

FLT1 (FLT, FLT-1, VEGFR1, VEGFR-1, Vascular Endothelial Growth Factor Receptor 1) (Biotin)
MBS6417423-5x01mL	MyBiosource	5x0.1mL	EUR 4120

Human VEGFR-3/FLT-4/Fc Chimera, soluble
MBS691672-005mg	MyBiosource	0.05mg	EUR 430

Human VEGFR-3/FLT-4/Fc Chimera, soluble
MBS691672-5x005mg	MyBiosource	5x0.05mg	EUR 1645

Human VEGFR-3/FLT-4/Fc Chimera, soluble
MBS691800-001mg	MyBiosource	0.01mg	EUR 265

Human VEGFR-3/FLT-4/Fc Chimera, soluble
MBS691800-5x001mg	MyBiosource	5x0.01mg	EUR 890

Human VEGFR-3/FLT-4/Fc Chimera, soluble
SFC-010	Angio Proteomie	50ug	EUR 378

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (MaxLight 405)
MBS6443144-01mL	MyBiosource	0.1mL	EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (MaxLight 405)
MBS6443144-5x01mL	MyBiosource	5x0.1mL	EUR 4120

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (MaxLight 490)
MBS6443145-01mL	MyBiosource	0.1mL	EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (MaxLight 490)
MBS6443145-5x01mL	MyBiosource	5x0.1mL	EUR 4120

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (MaxLight 550)
MBS6443146-01mL	MyBiosource	0.1mL	EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (MaxLight 550)
MBS6443146-5x01mL	MyBiosource	5x0.1mL	EUR 4120

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (MaxLight 650)
MBS6443147-01mL	MyBiosource	0.1mL	EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (MaxLight 650)
MBS6443147-5x01mL	MyBiosource	5x0.1mL	EUR 4120

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (MaxLight 750)
MBS6443148-01mL	MyBiosource	0.1mL	EUR 950

VEGFR1 (Vascular Endothelial Growth Factor Receptor 1, FLT, FLT-1, VEGFR1, VEGFR-1) (MaxLight 750)
MBS6443148-5x01mL	MyBiosource	5x0.1mL	EUR 4120

Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691499-005mg	MyBiosource	0.05mg	EUR 395

Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691499-5x005mg	MyBiosource	5x0.05mg	EUR 1490

Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691661-001mg	MyBiosource	0.01mg	EUR 245

Mouse VEGFR-1/Flt-1(D7)-Fc Chimera, soluble
MBS691661-5x001mg	MyBiosource	5x0.01mg	EUR 805

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

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.