Products > Recombinant Proteins > Cytokines & Growth Factors

Categories

Human VEGF165

DatasheetFiguresReference

Order Form

Slide this table

Cat-Nr.300-075
Size5 µg
Price99 €
SourceE. coli
Formulationlyophilized
Purity Confirmation> 95% by SDS-PAGE
Length [aa]165
Molecular Weight38.2 kDa
N Terminal SequenceAPMAEGG
Endotoxin Levels< 0.1 ng per µg of human VEGF165
Biological ActivityThe ED50 for stimulation of cell proliferation in human umbilical vein endothelial cells by VEGF165 has been determined to be in the range of 1-5 ng/ml.
Species ReactivityHuman
Buffer50mM acetic acid
ReconstitutionThe lyophilized VEGF165 should be reconstituted in 50 mM acetic acid to a concentration not lower than 50 µg/ml. For long term storage we recommend to add at least 0.1% human or bovine serum albumin.
Stability and StorageLyophilized samples are stable for greater than six months at -20°C to -70°C. Reconstituted VEGF165 should be stored in working aliquots at -20°C.
Synonymsvascular endothelial growth factor A; VEGFA; VPF; VEGF; MVCD1
DescriptionHuman Vascular Endothelial Growth Factor VEGF165, a 23 kDa protein consisting of 165 amino acid residues, is produced as a homodimer. VEGF is a polypeptide growth factor and a member of the platelet-derived growth factor family. It is a specific mitogen for vascular endothelial cells and a strong angiogenic factor in vivo. Two high-affinity tyrosine kinase receptors for VEGF165 have been identified, VEGFR-1 (FLT-1), and VEGFR-2 (KDR). Consistent with the endothelial cell-specific action of VEGF165, expression of both receptor genes has been found predominantly but not exclusively on endothelial cells. Expression of VEGFR-1 was also found on human monocytes, neutrophils (PMNs), bovine brain pericytes and villous and extra villous trophoblast. In addition to its action as a mitogen it is a potent vascular permeability factor (VPF) in vivo. VEGF165 is also a chemo attractant molecule for monocytes and endothelial cells. 5 different proteins are generated by differential splicing: VEGF121, VEGF145, VEGF165, VEGF189 and VEGF206. The most abundant form is VEGF165. Whereas VEGF121 and VEGF165 are secreted proteins, VEGF145, VEGF189 and VEGF206 are strongly cell-associated. The isoforms VEGF145, VEGF165 and VEGF189 bind to heparin with high affinity. VEGF165 is apparently a homo-dimer, but preparations of VEGF165 show some heterogeneity on SDS gels, depending on the secretion of different glycosylation patterns. All dimeric forms have similar biological activities but their bioavailability is very different. There is good evidence that different cells and tissues express different VEGF isoforms. The other members of this increasing growth factor family are VEGF-B, -C, -D and -E. Another member is the Placenta growth factor PlGF.
Protein SequenceAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQENPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR
Uniprot IDP15692
Protein RefSeqNP_001020537.2
mRNA RefSeqNM_001025366.2

Figures

Figure 1.
SDS-PAGE analysis of recombinant human VEGF165. Samples were loaded in 15% SDS-polyacrylamide gel under non-reducing condition and stained with Coomassie blue.
Figure 2.
VEGF165-induced proliferation of HUVE cells. HUVECs were stimulated with increasing amounts of human VEGF165.

Reference

  1. Eph-ephrin signaling couples endothelial cell sorting and arterial specification. J. Stewen et al., Nat Commun. 2024; 15: 2539.
  2. Arsenic Trioxide Decreases Lymphangiogenesis by Inducing Apoptotic Pathways and Inhibition of Important Endothelial Cell Receptors. I. Hrgovic et al., Curr Issues Mol Biol. 2024 Jan; 46(1): 67–80.
  3. SUCNR1 Is Expressed in Human Placenta and Mediates Angiogenesis: Significance in Gestational Diabetes. R. Atallah et al., Int J Mol Sci. 2021 Nov; 22(21): 12048.
  4. Transforming growth factor‐β1 signalling triggers vascular endothelial growth factor resistance and monocyte dysfunction in type 2 diabetes mellitus. L.‐M. Makowski et al., J Cell Mol Med. 2021 Jun; 25(11): 5316–5325.
  5. Outgrowth, proliferation, viability, angiogenesis and phenotype of primary human endothelial cells in different purchasable endothelial culture media: feed wisely. B. Leopold et al., Histochem Cell Biol. 2019; 152(5): 377–390.
  6. Apelin+ Endothelial Niche Cells Control Hematopoiesis and Mediate Vascular Regeneration after Myeloablative Injury. Qi Chen et al., Cell Stem Cell. 2019 Dec 5; 25(6): 768–783.e6.
  7. BMP-2 induces human mononuclear cell chemotaxis and adhesion and modulates monocyte-to-macrophage differentiation. E. Pardali et al., J Cell Mol Med. 2018 Nov;22(11):5429-5438.
  8. Hypoxia Impairs Initial Outgrowth of Endothelial Colony Forming Cells and Reduces Their Proliferative and Sprouting Potential.  Tasev D et al., Front Med (Lausanne). 2018 Dec 20;5:356.
  9. Blood Outgrowth and Proliferation of Endothelial Colony Forming Cells are Related to Markers of Disease Severity in Patients with Pulmonary Arterial Hypertension. Smits J et al., Int J Mol Sci. 2018 Nov 27;19(12). pii: E3763.
  10. Pericytes regulate VEGF-induced endothelial sprouting through VEGFR1. H. M. Eilken et al., Nat Commun. 2017; 8: 1574.
  11. CD34 expression modulates tube-forming capacity and barrier properties of peripheral blood-derived endothelial colony-forming cells (ECFCs). D. Tasev et al., Angiogenesis. 2016; 19: 325–338.
  12. Endothelial Cells Derived from Non-malignant Tissues Are of Limited Value as Models for Brain Tumor Vasculature. Lohr J et al., Anticancer Res. 2015 May;35(5):2681-90.
  13. Long-Term Expansion in Platelet Lysate Increases Growth of Peripheral Blood-Derived Endothelial-Colony Forming Cells and Their Growth Factor-Induced Sprouting Capacity. D. Tasev et al., PLoS One. 2015; 10(6): e0129935.
  14. The inhibition of tyrosine kinase receptor signalling in leiomyosarcoma cells using the small molecule kinase inhibitor PTK787/ZK222584 (Vatalanib®). A. K.A. Gaumann et al., Int J Oncol. 2014 Dec; 45(6): 2267–2277.
  15. Improved Anchorage of Ti6Al4V Orthopaedic Bone Implants through Oligonucleotide Mediated Immobilization of BMP-2 in Osteoporotic Rats. J. V. Wölfle et al., PLoS One. 2014; 9(1): e86151.
  16. Spatial regulation of VEGF receptor endocytosis in angiogenesis. M. Nakayama et al., Nat Cell Biol.2 13 Mar; 15(3): 249–260.
  17. Fbxw7 Controls Angiogenesis by Regulating Endothelial Notch Activity. N. Izumi et al., PLoS One. 2012; 7(7): e41116.
  18. The Antiangiogenic 16K Prolactin Impairs Functional Tumor Neovascularization by Inhibiting Vessel Maturation. Ngoc-Quynh-Nhu Nguyen et al., PLoS One. 2011; 6(11): e27318.
  19. MicroRNA-21 Exhibits Antiangiogenic Function by Targeting RhoB Expression in Endothelial Cells. C. Sabatel et al., PLoS One. 2011; 6(2): e16979.
  20. Autocrine activity of soluble Flt-1 controls endothelial cell function and angiogenesis. S. Ahmad et al., Vasc Cell. 2011; 3: 15.
  21. Feed-forward Signaling by Membrane-bound Ligand Receptor Circuit: THE CASE OF NOTCH DELTA-LIKE 4 LIGAND IN ENDOTHELIAL CELLS. V. Caolo et al., J Biol Chem. 2010 Dec 24; 285(52): 40681–40689.
  22. Impaired Collateral Recruitment and Outward Remodeling in Experimental Diabetes. J. M. van Golde et al., Diabetes. 2008 Oct; 57(10): 2818–2823.
  23. Elevated placental soluble vascular endothelial growth factor receptor-1 inhibits angiogenesis in preeclampsia. S. Ahmad and A. Ahmed Circ Res. 2004 Oct 29;95(9):884-91.
  24. Collagen type 1 retards tube formation by human microvascular endothelial cells in a fibrin matrix. Kroon, M.E. et al., Angiogenesis (2002) 5: 257.
Order Form
Back to overview

All prices plus VAT + possible delivery charges

© 2024 ReliaTech. All Rights Reserved – VEGF165 (300-075)