VEGF (165) IS stands for vascular endothelial growth factor 165 aa "Improved Sequence". Human VEGF (165) IS is a recombinant protein optimized for use in cell culture, differentiation studies, and functional assays.

Data and images for Human VEGF (165) IS

Figures

Figure 1

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SDS-PAGE of Human VEGF (165) IS, premium grade under non-reduced (NR) and reduced (R) conditions.

Figure 1

SDS-PAGE of Human VEGF (165) IS, premium grade under non-reduced (NR) and reduced (R) conditions.

Specifications for Human VEGF (165) IS

Overview

VEGF (165) IS stands for vascular endothelial growth factor 165 aa "Improved Sequence". Human VEGF (165) IS is a recombinant protein optimized for use in cell culture, differentiation studies, and functional assays.

Applications

Human VEGF (165) IS may be used for a variety of applications, including:
  • Proliferation of endothelial cells.
  • Promotion of endothelial cell migration.
  • Chemo-attractant function, inducing migration of monocytes and osteoblasts.
  • Increasing the release of von Willebrand factor from endothelial cells and metallo-proteinases activity.

Detailed product information

Background information

Vascular endothelial growth factor (VEGF), a disulfide-linked homodimer also known as VEGF-A, belongs to the platelet-derived growth factor superfamily. VEGF is secreted by vascular smooth muscle cells upon hypoxic conditions and promotes angiogenesis and vasculogenesis, vascular permeability, and inhibition of apoptosis, through the binding to two cell surface receptors, VEGFR1 (Flt-1) and VEGFR2 (KDR/Flk-1), and other co-receptors, which are expressed mainly on endothelial cells and immune cells. VEGFR2 mediates almost all observed endothelial responses to VEGF, while neuropilin-1 acts as co-receptor for the VEGF 165 isoform and enhances its binding to VEGFR2 and its biological activity. The VEGF/VEGFR system supports initiation of inflammation, inducing migration of monocytes and macrophages, but also acts on neurons and kidney epithelial cells. Moreover, VEGF contributes to tumor growth and metastasis formation, and is crucial during embryonic development and wound healing. Alteration in VEGF/VEGFR pathways have been associated with diseases, such as cancer, age-related macular degeneration, preeclampsia, rheumatoid arthritis, and neuronal disorders, such as amyotrophic lateral sclerosis. Several isoforms are generated as a result of alternative splicing, including the soluble isoforms VEGF 121 aa and VEGF 165 aa in human, and a VEGF 164 aa isoform in mouse.

Biological activity

  • Proliferation of human umbilical vein endothelial cells (NIBSC 02/286)
  • research grade: ≥ 3×
    10
    5
    U/mg
  • premium grade: ≥ 5×
    10
    5
    U/mg
  • We measure the biological activity of each batch of MACS Premium-Grade Cytokines and state the results in the Certificate of Analysis (CoA). Based on the lot-specific activity, exact doses of active cytokine can be applied to cell culture experiments. This allows for reproducible cell culture conditions without the need for time-consuming lot-to-lot testing.

Quality description

Research-grade
cytokines are suitable for a wide variety of cell culture applications. They are sterile-filtered prior to lyophilization. Generally, endotoxin levels are <0.1 ng/μg (<1 EU/μg), and purities are >95%. The biological activity is tested in appropriate bioassays.
Premium-grade
cytokines offer the convenience of high and well-defined biological activities and allow exact unit dosing for demanding applications. The biological activity is determined after lyophilization and reconstitution, and normalized to WHO/NIBSC standards whenever available. In general, endotoxin levels are <0.01 ng/μg (<0.1 EU/μg), and purities are >97%. Lot-specific activities are stated in the Certificate of Analysis (www. miltenyibiotec.com/certificates).

Resources for Human VEGF (165) IS

Documents and Protocols

Certificates

Please follow this
link
to search for Certificates of Analysis (CoA) by lot number.

References for Human VEGF (165) IS

Publications

  1. Conn, G. et al. (1990) Purification of a glycoprotein vascular endothelial cell mitogen from a rat glioma-derived cell line. Proc. Natl. Acad. Sci. U.S.A. 87(4): 1323-1327
  2. Jayaraman, A. et al. (2018) Untargeted metabolomics reveals distinct metabolic reprogramming in endothelial cells co-cultured with CSC and non-CSC prostate cancer cell subpopulations. PLoS One 13(2): e0192175
  3. Masumoto, H. et al. (2016) The myocardial regenerative potential of three-dimensional engineered cardiac tissues composed of multiple human iPS cell-derived cardiovascular cell lineages. Sci Rep 6: 29933
  4. Nakane, T. et al. (2017) Impact of Cell Composition and Geometry on Human Induced Pluripotent Stem Cells-Derived Engineered Cardiac Tissue. Sci Rep 7: 45641
  5. Lamanuzzi, A. et al. (2018) Inhibition of mTOR complex 2 restrains tumor angiogenesis in multiple myeloma. Oncotarget. 9(29): 20563-20577
  6. Rao, L. et al. (2018)
    Targeting angiogenesis in multiple myeloma by the VEGF and HGF blocking DARPin
    ®
    protein MP0250: a preclinical study.
    Oncotarget. 9(17): 13366-13381
  7. Tiemeier, G. L et al. (2019) Closing the Mitochondrial Permeability Transition Pore in hiPSC-Derived Endothelial Cells Induces Glycocalyx Formation and Functional Maturation. Stem Cell Reports 13(5): 803-816
  8. Beez, C. M. et al. (2019) Cardiac Extracellular Vesicles (EVs) Released in the Presence or Absence of Inflammatory Cues Support Angiogenesis in Different Manners. Int J Mol Sci 20(24): 6363
  9. Manocha, E. et al. (2021) Avian Reovirus P17 Suppresses Angiogenesis by Promoting DPP4 Secretion. Cells 10(2): 259
  10. van IJzendoorn, D. G. P. et al. (2020) Vascular Tumor Recapitulated in Endothelial Cells from hiPSCs Engineered to Express the SERPINE1-FOSB Translocation. Cell Rep Med. 1(9): 100153
  11. Zeinali, S. et al. (2021) Remodeling of an in vitro microvessel exposed to cyclic mechanical stretch. APL Bioeng 5(2): 026102

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