Recombinant Human VEGF 145 (aa 27-171) Protein, CF

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human VEGF 145 (aa 27-171) Protein, CF Summary

• Details of Functionality: Measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells. Conn, G. et al. (1990) Proc. Natl. Acad. Sci. USA 87:1323. The ED₅₀ for this effect is 12-60 ng/mL.
• Source: E. coli-derived human VEGF protein
  Ala27-Arg171, with an N-terminal Met
• Accession #: NP_001191313
• N-terminal Sequence: Met-Ala27 & Pro28
• Structure / Form: Disulfide-linked homodimer
• Protein/Peptide Type: Recombinant Proteins
• Gene: VEGFA
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• Theoretical MW: 17 kDa (monomer).
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
• SDS-PAGE: 20 kDa, reducing conditions

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in HCl.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by silver stain
• Reconstitution Instructions: Reconstitute at 100 μg/mL in 4 mM HCl.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human VEGF 145 (aa 27-171) Protein, CF

• MVCD1
• VAS
• vascular endothelial growth factor A
• Vascular permeability factor
• Vasculotropin
• VEGF
• VEGFA
• VEGF-A
• VEGFMGC70609
• VPF
• VPFvascular endothelial growth factor

Background

Vascular endothelial growth factor (VEGF or VEGFA), also known as vascular permeability factor (VPF), is a potent mediator of both angiogenesis and vasculogenesis in the fetus and adult (1-3). It is a member of the PDGF family of proteins that is characterized by the presence of eight conserved cysteine residues that form a cystine knot structure (4). Humans express multiple alternatively spliced isoforms of VEGF that are 111, 121, 145, 165, 183, 189, and 206 amino acids (aa) in length (4, 5, 6). Isoforms other than VEGF₁₁₁ and 121 contain basic heparin binding regions and are not freely diffusible (4, 5). VEGF₁₆₅ appears to be the most abundant and potent isoform, followed by VEGF₁₂₁ and VEGF₁₈₉ (3-5). VEGF₁₄₅ expression is relatively low, and is found mainly in female and male reproductive tissues, carcinomas of the female reproductive system, and other solid tumors (5, 7, 8). Expression of mouse VEGF₁₄₄, the rodent ortholog to human VEGF₁₄₅, is particularly enhanced by metabolic stress, such as that encountered during sustained exercise or starvation (8, 9). Human VEGF₁₄₅ shares 89% aa sequence identity with mouse and rat VEGF₁₄₄. VEGF₁₄₅ binds to the type I transmembrane receptor tyrosine kinase VEGF R2/KDR/Flk1 on endothelial cells. This receptor appears to be the primary mediator of VEGF angiogenic activity (3-5, 7). Unlike VEGF₁₆₅, VEGF₁₄₅ does not bind VEGF R1/Flt1 or VEGF R3/Flt-4 (4, 5, 7). VEGF₁₄₅ also binds the semaphorin receptor Neuropilin2 and promotes complex formation with VEGF R2, but unlike VEGF₁₆₅ and VEGF₁₂₁, it does not bind Neuropilin1 (10, 11). VEGF is required during embryogenesis to regulate the proliferation, migration, and survival of endothelial cells (3, 4, 7). In adults, VEGF acts mainly during wound healing and the female reproductive cycle (3). Pathologically, isoforms that include VEGF₁₄₅ are involved in tumor angiogenesis and vascular leakage (5, 12, 13).

1. Leung, D.W. et al. (1989) Science 246:1306.
2. Keck, P.J. et al. (1989) Science 246:1309.
3. Byrne, A.M. et al. (2005) J. Cell. Mol. Med. 9:777.
4. Robinson, C.J. and S.E. Stringer (2001) J. Cell. Sci. 114:853.
5. Woolard, J. et al. (2009) Microcirculation 16:572.
6. Mineur, P. et al. (2007) J. Cell Biol. 179:1261.
7. Poltorak, Z. et al. (1997) J. Biol. Chem. 272:7151.
8. Zhang, L. et al. (2002) Biochem. Biophys. Res. Commun. 292:860.
9. Ding, Y.H. et al. (2004) Curr. Neurovasc. Res. 1:411.
10. Pan, Q. et al. (2007) J. Biol. Chem. 282:24049.
11. Gluzman-Poltorak, Z. et al. (2000) J. Biol. Chem. 275:18040.
12. Weis, S.M. and D.A. Cheresh (2005) Nature 437:497.
13. Thurston, G. (2002) J. Anat. 200:575.

Publications for VEGF (7626-VE/CF)(1)

Publication using 7626-VE/CF

• Lecce , Laura, Lam , Yuen Tin, Lindsay , Laura A, Yuen , Sui Chin, Simpson , Philippa, Handelsman , David J, Ng , Martin K Aging impairs VEGF-mediated, androgen-dependent regulation of angiogenesis. Mol Endocrinol, 2014-07-24;28(9):1487-501. 2014-07-24 [PMID: 25058601] (Bioassay, Human)

FAQs for VEGF (7626-VE/CF). (Showing 1 - 1 of 1 FAQ).

1. Why is the molecular weight of VEGF different from the similar antibody, for some companies the the molecular weight is 40KD)?
   • I can't comment on another company's antibody because I don't have any information about their products. I can tell you that VEGF is expressed in a variety of isoforms and is subject to various post-translational modifications that influence its apparent molecular weight in an SDS-PAGE gel compared to the theoretical molecular weight.

Bioinformatics

• Gene Symbol: VEGFA
• Uniprot:
  • NP_001191313()