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ActiveMax® Recombinant Human VEGF165, Tag Free, (HPLC-verified, MALS verified), 5 x 200µg  

ActiveMax® Recombinant Human VEGF165, Tag Free, (HPLC-verified, MALS verified), 5 x 200µg

ActiveMax® Recombinant Human VEGF165, Ala 27 - Arg 191, was produced in human 293 cells (HEK293), Tag free, (HPLC-verified, MALS verified)

Synonyms: Vascular endothelial growth factor A-165, VEGF-A165 cytokine, Vascular permeability factor, VPF-165

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Availability: within 7 days

2 090,00 €

VEGF165 is the most abundant splice variant of VEGF-A [1,2]. 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 [1]. VEGF gene expression is induced by hypoxia, inflammatory cytokines and oncogenes [1,2]. VEGF165 binds to heparan sulfate and is retained on the cell surface and in the extracellular matrix [2,3]. VEGF165 binds to the receptor tyrosine kinases, VEGFR1 and VEGFR2 [1]. VEGF165 is the only splice variant that binds to co-receptors NRP-1 and NRP-2 [1-3] that function to enhance VEGFR2 signaling [1]. Binding of VEGF165 to VEGFR1 and VEGFR2 leads to activation of the PI3K/AKT, p38 MAPK, FAK and paxillin [1]. VEGF plays a key role in tumor angiogenesis in many cancers [2].

Recombinant ActiveMax® Human VEGF165, Tag Free (MALS verified) (VE5-H4210) is expressed from human 293 cells (HEK293). It contains AA Ala 27 - Arg 191 (Accession # P15692-4).
Predicted N-terminus: Ala 27

Molecular Characterization
This protein carries no "tag". The protein has a calculated MW of 19.2 kDa. As a result of glycosylation, the protein migrates as 24 kDa (monomer) under reducing (R) condition, and 43-50 kDa (homodimer) under non-reducing (NR) condition (SDS-PAGE).

Less than 1.0 EU per μg of the ActiveMax® Human VEGF165 by the LAL method.

>98% as determined by SDS-PAGE.
>95% as determined by SEC-MALS.

Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally Trehalose is added as protectant before lyophilization.
Contact us for customized product form or formulation.

See Certificate of Analysis for details of reconstitution instruction and specific concentration.

Avoid repeated freeze-thaw cycles. No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C-8°C); After reconstitution under sterile conditions for 1 month (4°C-8°C) or 3 months (-20°C to -70°C).

Please refer to product data sheet.