Application

Research CategoryApoptosis & Cancer

Research Sub CategoryApoptosis - Additional

Immunohistochemistry Analysis: A 1:50 dilution from a representative lot detected VEGF-B in human skeletal muscle myocytes and vascular tissue and cardiac myocytes in human heart.

Detect VEGF-B using this Anti-VEGF-B Antibody validated for use in western blotting & IHC (Paraffin).

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General description

VEGF-B, also known as Vascular endothelial growth factor B, VEGF-related factor, VRF, and encoded by the gene VEGFB/VRF, is an endothelial cell growth factor that has multiple splice variants and plays roles in angiogenesis but also in cardiac muscle function, coronary vascular development, chemotaxis of endothelial cells and mast cells, apoptosis regulation, platelet activation, cell division, wound healing and the activation of various signaling pathways. VEGFB is a secreted protein that stays associated with cells because of its ability to bind to heparin. VEGFB is expressed in all cells except for liver cells with the highest levels found in muscle and pancreatic cells. VEGFB levels in plasma are also being studied as a potential biomarker for ventricle damage after heart attacks. High levels of plasma VEGFB show little remodeling whereas patients with lower levels had significant ventricle remodeling, thus VEGFB may have clinical utility in the identification of patients at high risk of remodeling and therefore ventricle damage.

Immunogen

Epitope: Unknown

KLH-conjugated linear peptide corresponding to human VEGF-B.

Physical form

Affinity purified

Purified rabbit polyclonal in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Quality

Evaluated by Western Blotting in human skeletal muscle tissue lysate.

Western Blotting Analysis: 1.0 µg/mL of this antibody detected VEGF-B in 10 µg of human skeletal muscle tissue lysate.

Storage and Stability

Stable for 1 year at 2-8°C from date of receipt.

Target description

~40/32/25 kDa observed. The ~40kDa band observed is likely due to homo and/or hetero-dimers, the ~32kDa band observed is likely due to glycosylation, and the ~25kDa band is un-modified VEGF186 (Olofsson, B., et al. (1998). Proc Natl Acad Sci USA. 95(20):11709-11714).