Recombinant Human VEGF 165 Avi-tag Biotinylated Protein, CF

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2 μg/lane of Biotinylated Recombinant Human VEGF 165 Avi-tag (Catalog # AVI293) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® blue staining, showing ...read more
When Recombinant Human VEGFR1/Flt-1 Fc Chimera (Catalog # 321-FL) is immobilized at 1 µg/mL, Biotinylated Recombinant Human VEGF 165Avi-tag (Catlaog # AVI293) binds with an ED50 of 0.6-3.6 ng/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Human VEGF 165 Avi-tag Biotinylated Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human VEGFR1/Flt-1 Fc Chimera (Catalog # 321-FL) is immobilized at 1 µg/mL (100 µL/well), Recombinant Biotinylated Recombinant Human VEGF 165 Avi-tag (Catalog # AVI293) binds with an ED50 of 0.6-3.6 ng/mL.
Source
Human embryonic kidney cell, HEK293-derived human VEGF protein
Human VEGF 165
(Ala27-Arg191)
Accession # NP_001165097
Avi-tag 
N-terminusC-terminus
Accession #
N-terminal Sequence
Ala27
Structure / Form
Disulfide-linked homodimer, biotinylated via Avi-tag.
Protein/Peptide Type
Recombinant Proteins
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
21 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
20-28 kDa, under 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 with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 250 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 165 Avi-tag Biotinylated 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 VEGF-A), 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 that is characterized by the presence of eight conserved cysteine residues and a cystine knot structure (4). Humans express alternately spliced isoforms of 121, 145, 165, 183, 189, and 206 amino acids (aa) in length (4). VEGF165 appears to be the most abundant and potent isoform, followed by VEGF121 and VEGF189 (3, 4). Isoforms other than VEGF121 contain basic heparin-binding regions and are not freely diffusible (4). Human VEGF165 shares 88% aa sequence identity with corresponding regions of mouse and rat, 96% with porcine, 95% with canine, and 93% with feline, equine and bovine VEGF, respectively. VEGF binds the type I transmembrane receptor tyrosine kinases VEGF R1 (also called Flt-1) and VEGF R2 (Flk-1/KDR) on endothelial cells (4). Although VEGF affinity is highest for binding to VEGF R1, VEGF R2 appears to be the primary mediator of VEGF angiogenic activity (3, 4). VEGF165 binds the semaphorin receptor, Neuropilin-1 and promotes complex formation with VEGF R2 (5). VEGF is required during embryogenesis to regulate the proliferation, migration, and survival of endothelial cells (3, 4). In adults, VEGF functions mainly in wound healing and the female reproductive cycle (3). Pathologically, it is involved in tumor angiogenesis and vascular leakage (6, 7). Circulating VEGF levels correlate with disease activity in autoimmune diseases such as rheumatoid arthritis, multiple sclerosis and systemic lupus erythematosus (8). VEGF is induced by hypoxia and cytokines such as IL-1, IL-6, IL-8, oncostatin M and TNF-alpha (3, 4, 9).

  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. Pan, Q. et al. (2007) J. Biol. Chem. 282:24049.
  6. Weis, S.M. and D.A. Cheresh (2005) Nature 437:497.
  7. Thurston, G. (2002) J. Anat. 200:575.
  8. Carvalho, J.F. et al. (2007) J. Clin. Immunol. 27:246.
  9. Angelo, L.S. and R. Kurzrock (2007) Clin. Cancer Res. 13:2825.

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FAQs for VEGF (AVI293). (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.

Other Available Formats

Biotin AVI293

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Detecting HIF alpha and beyond: Best controls for hypoxia Western blot analysis
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Neurovascular signaling for repair enhances brain metastasis
By Jamshed Arslan, Pharm. D., PhD. Stroke    is a leading cause of mortality and morbidity worldwide. Cellular players – neurons, astrocytes, endothelial and stromal cells – involved in post-stroke repair t...  Read full blog post.

mTOR Signaling and the Tumor Microenvironment
By Yoskaly Lazo-Fernandez, PhD The mammalian target of rapamycin (mTOR) is a conserved serine/threonine kinase that, as a member of two distinct intracellular protein complexes, mTORC1 and mTORC2, regulates protein...  Read full blog post.

Chemotherapy-induced metastasis: An unexpected foe?
By Yoskaly Lazo-Fernandez, PhD IntroductionEvidence has accumulated recently indicating that common cancer therapies might stimulate metastasis in a significant number of cancer patients1. In fact, neoadjuvant che...  Read full blog post.

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By Jamshed Arslan Pharm.D. von Hippel-Lindau (VHL) disease is associated with tumors arising in multiple organs. Activation of hypoxia-inducible factor (HIF)-alpha underlies the VHL disease pathogenesis. In normoxia...  Read full blog post.

The role of HIF-2 alpha in the progression and therapy of clear cell renal cell carcinoma
HIF-2 alpha, also known as hypoxia-inducible factor 2, endothelial PAS domain protein-1, and member of PAS superfamily 2 is part of the HIF family of proteins.  The HIF family is composed of HIF-1, HIF-2 and HIF-3, where HIF-2 is a dimeric protein...  Read full blog post.

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The role of HIF-1 Alpha signaling in the retina under hypoxic conditions
Hypoxia inducible factor 1 (HIF-1) is a protein that plays an essential role in hypoxia, or low levels of cellular oxygen. HIF-1 is a heterodimeric protein that consists of a constitutively expressed beta subunit and oxygen related alpha subunit. ...  Read full blog post.

Using SCP3/SYCP3 Antibodies as Meiosis Markers in Gametogenesis and DNA Repair Studies
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