Recombinant Human VEGF (165aa) (E. coli)



DescriptionVEGF is a homodimeric glycoprotein that is actively involved in angiogenesis, vasculogenesis and endothelial cell growth. Owing to alternative splicing of the mRNA, VEGF occurs in several molecular variants of 121, 162, 145, 148, 165, 183, 189 and 206 amino acids. The various isoforms of VEGF differ in biological properties such as; (a) the receptors they recognize and (b) their interaction with heparan sulfate proteoglycans. VEGF-121 and VEGF-165 are soluble secreted forms of the factor while VEGF-189 and VEGF-206 are mostly bound to heparin-containing proteoglycans in the cell surface or in the basement membrane. VEGF-165 is the most common variant in most tissues and one with heparin binding properties. Recombinant VEGF-165aa is a non-glycosylated, disulfide linked homodimer.
FamilyVEGF/PGDF/Pleiotrophin Family
AliasesVascular endothelial growth factor A, VEGF-A, Vascular permeability factor, VPF, VEGFA, VEGF-165aa
Recombinant Human Vascular Endothelial Growth Factor 165AA (VEGFA)
Gene SymbolVEGFA
Gene ID7422
Accession NumberP15692
SourceE. coli
SpeciesHuman (H. sapiens)
AppearanceLyophilized Powder
Molecular Weight19 kDa
Endotoxin Level<1.0 EU/µg of recombinant protein as determined by the LAL method
Purity>95% as determined by SDS-PAGE
FormulationLyophilized from 0.2 μm filtered solution in sodium phosphate and NaCl (pH 6.5)
FunctionThe ED50 as determined by the dose-dependent proliferation of human umbilical vein endothelial cells was found to be <0.1ng/ml.
ReconstitutionA quick spin of the vial followed by reconstitution in distilled water to a concentration no less than 0.1 mg/mL. This solution can then be diluted into other buffers.
StorageThe lyophilized protein is stable for at least one year from date of receipt at -70°C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8°C for one month, or at -20°C for six months, with a carrier protein without detectable lo
UsageFor research use only. Not for diagnostic or therapeutic use.

How are endotoxin levels measured?
1. For estimating the endotoxin levels; we use the LAL (Limulus Amebocyte Lysate) method: The lysate from horseshoe crab amebocytes clots in the presence of very low endotoxin. This reaction is the basis of the Limulus amebocyte lysate (LAL) assay which was approved by the FDA in 1970. · Endotoxin is generally measured in Endotoxin Units per milliliter (EU/mL). · For recombinant proteins: EU is reported per microgram of protein. · One EU = 0.1-0.2 ng endotoxin/µg of protein. · At abm, we do the LAL chromogenic assays that can detect down to 0.01 EU/ml.
With regard to the BSA levels in some Growth Factors and Cytokines, can you please provide an explanation as to why they are so high?
The amount of BSA, as part of the formulation of a protein, can vary considerably depending on how much BSA was deemed optimum/necessary for protein stability in combination with /in-lieu of - other possible additives. The aforementioned formulations are somewhat analogous to the “carrier” versions of many formulations from “R and D systems” that have as high as 50 µg of BSA per µg of the recombinant protein product. If, needed or desired, abm scientists can substitute BSA for other stabilizing additives for most formulations.
Are your Escherichia coli sourced growth factors: 1) Human derived materials free? 2) Recombinant proteins free?
Yes, all of abm's growth factors made in Escherichia coli using recombinant technology contain no human derived-products or other recombinant proteins. In the rare cases of BSA presence, this will be mentioned in the product's formulation.

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