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Recombinant Mouse VEGF 120 Protein, CF

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Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse VEGF 120 Protein, CF Summary

Details of Functionality
Measured in a cell proliferation assay using HUVEC human umbilical vein endothelial cells. The ED50 for this effect is 1-4 ng/mL.
Source
E. coli-derived mouse VEGF protein
Ala27-Arg146 (Gly117Glu & Glu118Arg)
Accession #
N-terminal Sequence
Ala27
Structure / Form
Disulfide-linked homodimer
Protein/Peptide Type
Recombinant Proteins
Gene
Vegfa
Purity
>97%, 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
14 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.
Publications
Read Publications using
494-VE/CF in the following applications:

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 Acetonitrile and TFA.
Purity
>97%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 50 µg/mL in sterile PBS.

Notes

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

Alternate Names for Recombinant Mouse VEGF 120 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 a cysteine-knot structure formed by eight conserved cysteine residues (4). Alternately spliced isoforms of 121, 145, 165, 183, 189, and 206 amino acids (aa) have been identified in humans, with 120, 164 and 188 aa isoforms found in mouse (2, 4). VEGF120 and VEGF121 lack basic heparin-binding regions and are freely diffusible (4). Mouse embryos expressing only the VEGF120 isoform do not survive to term and show defects in skeletogenesis (5). Mouse VEGF120 shares 98% aa sequence identity with corresponding regions of rat, 89% with canine, feline, equine and porcine, and 87% with human, ovine 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 affinity is highest for binding to VEGF R1, VEGF R2 appears to be the primary mediator of VEGF angiogenic activity (3, 4). Human VEGF165 binds the semaphorin receptor, Neuropilin-1; VEGF121 binding has also been reported (6). 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 (7, 8). Circulating VEGF levels correlate with disease activity in autoimmune diseases such as rheumatoid arthritis, multiple sclerosis and systemic lupus erythematosus (9). VEGF is induced by hypoxia and cytokines such as IL‑1, IL-6, IL-8, oncostatin M and TNF-alpha (3, 4, 10).

  1. Breier, G. et al. (1992) Development 114:521.
  2. Shima, D.T. et al. (1996) J. Biol. Chem. 271:3877.
  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. Zelzer, E. et al. (2002) Development 129:1893.
  6. Pan, Q. et al. (2007) J. Biol. Chem. 282:24049.
  7. Weis, S.M. and D.A. Cheresh (2005) Nature 437:497.
  8. Thurston, G. (2002) J. Anat. 200:575.
  9. Carvalho, J.F. et al. (2007) J. Clin. Immunol. 27:246.
  10. Angelo, L.S. and R. Kurzrock (2007) Clin. Cancer Res. 13:2825.

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Publications for VEGF (494-VE/CF)(8)

We have publications tested in 3 confirmed species: Mouse, N/A, Porcine.

We have publications tested in 3 applications: Bioassay, In Vivo, Western Blot.


Filter By Application
Bioassay
(3)
In Vivo
(5)
Western Blot
(1)
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Mouse
(6)
N/A
(1)
Porcine
(1)
All Species
Showing Publications 1 - 8 of 8.
Publications using 494-VE/CF Applications Species
Y Ichiyama, R Matsumoto, S Obata, O Sawada, Y Saishin, M Kakinoki, T Sawada, M Ohji Assessment of mouse VEGF neutralization by ranibizumab and aflibercept PLoS ONE, 2022-12-21;17(12):e0278951. 2022-12-21 [PMID: 36542626] (Western Blot, N/A) Western Blot N/A
J Wang, W Song, R Yang, C Li, T Wu, XB Dong, B Zhou, X Guo, J Chen, Z Liu, QC Yu, W Li, J Fu, YA Zeng Endothelial Wnts control mammary epithelial patterning via fibroblast signaling Cell Reports, 2021-03-30;34(13):108897. 2021-03-30 [PMID: 33789106] (Bioassay, Mouse) Bioassay Mouse
Lin H, Shabbir A, Molnar M, Yang J, Marion S, Canty JM, Lee T Adenoviral expression of vascular endothelial growth factor splice variants differentially regulate bone marrow-derived mesenchymal stem cells. J. Cell. Physiol., 2008-08-01;216(2):458-68. 2008-08-01 [PMID: 18288639] (Bioassay, Porcine) Bioassay Porcine
Horst AK, Ito WD, Dabelstein J, Schumacher U, Sander H, Turbide C, Brummer J, Meinertz T, Beauchemin N, Wagener C Carcinoembryonic antigen-related cell adhesion molecule 1 modulates vascular remodeling in vitro and in vivo. J. Clin. Invest., 2006-05-04;116(6):1596-605. 2006-05-04 [PMID: 16680193] (In Vivo, Mouse) In Vivo Mouse
Niida S, Kondo T, Hiratsuka S, Hayashi S, Amizuka N, Noda T, Ikeda K, Shibuya M VEGF receptor 1 signaling is essential for osteoclast development and bone marrow formation in colony-stimulating factor 1-deficient mice. Proc. Natl. Acad. Sci. U.S.A., 2005-09-19;102(39):14016-21. 2005-09-19 [PMID: 16172397] (Bioassay, In Vivo, Mouse) Bioassay, In Vivo Mouse
Qian DZ, Wang X, Kachhap SK, Kato Y, Wei Y, Zhang L, Atadja P, Pili R The histone deacetylase inhibitor NVP-LAQ824 inhibits angiogenesis and has a greater antitumor effect in combination with the vascular endothelial growth factor receptor tyrosine kinase inhibitor PTK787/ZK222584. Cancer Res., 2004-09-15;64(18):6626-34. 2004-09-15 [PMID: 15374977] (In Vivo, Mouse) In Vivo Mouse
Usui T, Ishida S, Yamashiro K, Kaji Y, Poulaki V, Moore J, Moore T, Amano S, Horikawa Y, Dartt D, Golding M, Shima DT, Adamis AP VEGF164(165) as the pathological isoform: differential leukocyte and endothelial responses through VEGFR1 and VEGFR2. Invest. Ophthalmol. Vis. Sci., 2004-02-01;45(2):368-74. 2004-02-01 [PMID: 14744874] (In Vivo, Mouse) In Vivo Mouse
Banerjee K, Biswas PS, Kim B, Lee S, Rouse BT CXCR2-/- mice show enhanced susceptibility to herpetic stromal keratitis: a role for IL-6-induced neovascularization. J. Immunol., 2004-01-15;172(2):1237-45. 2004-01-15 [PMID: 14707102] (In Vivo, Mouse) In Vivo Mouse

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FAQs for VEGF (494-VE/CF). (Showing 1 - 1 of 1 FAQs).

  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.

Additional VEGF Products

Blogs on VEGF. Showing 1-10 of 23 blog posts - Show all blog posts.

Unlocking the Potential of Biosimilars in Immuno-Oncology
By Jennifer Jones, M.S.Biosimilar Antibodies: Imitation Meets InnovationIn the ever-evolving medical landscape, a new class of pharmaceuticals is emerging as a game-changer, poised to transform the way we approach...  Read full blog post.

Understanding ‘Y’ in Breast Cancer: Crucial Role of DNA/RNA-binding Protein YB-1 in the Development, Pre-Invasive, and Metastatic Phases
Jamshed Arslan, Pharm D, PhD In the United States, 1 in 8 women will be diagnosed with breast cancer in her lifetime.1 Despite the prevalence, cancer genesis is a mystery. The heterogeneity of cancers makes it diff...  Read full blog post.

Detecting HIF alpha and beyond: Best controls for hypoxia Western blot analysis
By Rosa Moreno, PhD. Detecting HIF alpha and beyond: Best controls for hypoxia Western blot analysisPhysiological low levels of oxygen induce normal hypoxic events across biological systems. This hypoxic state activ...  Read full blog post.

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.

Getting Physical: Link between Lipid Metabolism and Hypoxia Target Genes
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.

The application of CD31/Pecam-1 (MEC 7.46) in breast cancer research
CD31/PECAM-1, or platelet endothelial cell adhesion molecule 1, is a 130-kDa glycoprotein expressed on vascular and hematopoietic cells.  Depending on the cell type, CD31/PECAM-1 expression can be largely localized to cell junctions, playing a rol...  Read full blog post.

The dynamic use of a PCNA antibody in fish, porcine and primate species
Proliferating cell nuclear antigen (PCNA) plays a crucial role in nucleic acid metabolism as it pertains to DNA replication and repair.  Most noted for its activation of subunits of DNA polymerase, it has also been found to interact with cell-cycl...  Read full blog post.

Showing 1-10 of 23 blog posts - Show all blog posts.
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Bioinformatics

Gene Symbol Vegfa
Uniprot