This protein carries a polyhistidine tag at the N-terminus. The protein has a calculated MW of 20 kDa (monomer). As a result of glycosylation, the protein migrates as 25 kDa (monomer) under reducing (R) condition, and 43-50 kDa (homodimer) under non-reducing (NR) condition (SDS-PAGE).
VEGF
Spezies: Schwein
Wirt: Escherichia coli (E. coli)
Recombinant
> 95 % as determined by reducing SDS-PAGE.
Beschränkungen
Nur für Forschungszwecke einsetzbar
Format
Lyophilized
Buffer
PBS, pH 7.4
Handhabung
Please avoid repeated freeze-thaw cycles.
Lagerung
-20 °C
Informationen zur Lagerung
No activity loss was observed after storage at: In lyophilized state for 1 year (4 °C), After reconstitution under sterile conditions for 3 months (-70 °C).
Kerros, Tripathi, Zha, Mehrens, Sergeeva, Philips, Qiao, Peters, Katayama, Sukhumalchandra, Ruisaard, Perakis, St John, Lu, Mittendorf, Clise-Dwyer, Herrmann, Alatrash, Toniatti, Hanash, Ma, Molldrem: "Neuropilin-1 mediates neutrophil elastase uptake and cross-presentation in breast cancer cells." in: The Journal of biological chemistry, Vol. 292, Issue 24, pp. 10295-10305, (2017) (PubMed).
VEGF165 is the most abundant splice variant of VEGF-A. VEGF165 is produced by a number of cells including endothelial cells, macrophages and T cells. VEGF165 is involved in angiogenesis, vascular endothelial cell survival, growth, migration and vascular permeability. VEGF gene expression is induced by hypoxia, inflammatory cytokines and oncogenes. VEGF165 binds to heparan sulfate and is retained on the cell surface and in the extracellular matrix. VEGF165 binds to the receptor tyrosine kinases, VEGFR1 and VEGFR2. VEGF165 is the only splice variant that binds to co-receptors NRP-1 and NRP-2 that function to enhance VEGFR2 signaling. Binding of VEGF165 to VEGFR1 and VEGFR2 leads to activation of the PI3K/AKT, p38 MAPK, FAK and paxillin. VEGF plays a key role in tumor angiogenesis in many cancers.