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Specifications
- Pack type:Vial
- Conjugation:Unconjugated
- Protein Function:Cytokine
- Protein/Peptide Type:Recombinant
- Source:E. coli
- Species:Human
- Size:50 µg
- Tag sequence:MGHHHHHHSGSEF
- Storage Conditions:–20 °C
- Endotoxin Content:<1.0 EU per 1 μg (determined by the LAL method)
- Gene ID:7422
- Reconstitution Instructions:Reconstitute in 10 mM PBS (pH 7.4) to a concentration of 0.1 - 1.0 mg/ml. Do not vortex.
- Endotoxin-free:N
- Carrier-Free:Y
- Protease-free:N
- Animal-Free:Y
- Protein Synonyms:Vascular Endothelial Growth Factor 165
- UniProtKB:P15692
- Protein/Peptide Name:VEGF165
- Purity:95 - 100%
- Molecular Weight:20 kDa
- Sequence:Pro28~Arg191
- Endotoxin Level:Low
- Concentration:0.2 mg/ml
- Formulation:Lyophilized from PBS, pH 7.4, containing 0.01% SKL, 5% Trehalose.
- Nuclease-free:N
- Shipping Temperature:4 °C
- Tested Applications:Positive control, Immunogen, SDS-PAGE, Western blot.
- Cat. No.:MSPP-RPB696HU1
Specifications
About this item
This is a VEGF165 recombinant protein (prokaryotic), Human is sequencing from Pro28~Arg191 with 95 - 100% purity. Lyophilized from PBS, pH 7.4, containing 0.01% SKL, 5% Trehalose with 0.2 mg/ml.
- High quality, purity, reproducibility and effectiveness
- Offers customized buffers and tag options
- 100% quality and service satisfaction guarantee
VEGF165 is an angiogenic cytokine that also regulates vascular permeability.The neuropilin-1 (np1) receptor binds the 165 amino-acid form of VEGF165 and functions as an enhancer that potentiates VEGF165 signaling via the VEGFR-2 tyrosine-kinase receptor. A VEGF165 mutant (VEGF165KF) that binds to neuropilins but displays a much lower affinity toward VEGFR-1 and VEGFR-2. VEGF165KF failed to induce VEGFR-2 phosphorylation in cells lacking neuropilins. However, in the presence of np1, VEGF165KF bound weakly to VEGFR-2, induced VEGFR-2 phosphorylation, and activated ERK1/2. Interestingly, VEGF165KF did not promote formation of VEGFR-2/np1 complexes nor did high concentrations of VEGF165KF inhibit VEGF165 induced formation of such complexes, suggesting that VEGF165 does not stabilize VEGFR-2/np1 complexes by forming bridges spanning VEGFR-2 and np1.