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Recombinant Mouse VEGFA protein (His Tag)

Species

Mouse

Purity

>90 %, SDS-PAGE

Tag

His Tag

Activity

not tested

Cat no : Eg0277

Validation Data Gallery

  • Purity of Recombinant Mouse VEGFA was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

    Purity of Recombinant Mouse VEGFA was determined by SDS-PAGE. The protein was resolved in an SDS-PAGE in reducing (R) and non-reducing (NR) conditions and stained using Coomassie blue.

Product Information

Purity >90 %, SDS-PAGE
Endotoxin <0.1 EU/μg protein, LAL method
Activity 
Not tested
Expression HEK293-derived Mouse VEGFA protein Ala27-Arg190 (Accession# Q00731-2) with a His tag at the N-terminus.
GeneID 22339
Accession Q00731-2
PredictedSize 20.1 kDa
SDS-PAGE 22-26 kDa, reducing (R) conditions
Formulation Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization.
Reconstitution Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water.
Storage Conditions
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
  • Until expiry date, -20℃ to -80℃ as lyophilized proteins.
  • 3 months, -20℃ to -80℃ under sterile conditions after reconstitution.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature.

Background

VEGFA, also named as VEGF or VPF, belongs to the PDGF/VEGF growth factor family. It is a growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. VEGFA induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. It binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin. Defects in VEGFA are associated with microvascular complications of diabetes type 1 (MVCD1). Alternately spliced isoforms of 121, 145, 148, 165, 183, 189, and 206 amino acids (aa) have been identified in humans, with 120, 144, 164 and 188 aa isoforms found in rat and mouse.

References:

1. Conn, G. et al. (1990) J. Biol. Chem. 87:2628.
2. Ishii, H. et al. (2001) Arch. Oral Biol. 46:77.
3. Byrne, A.M. et al. (2005) J. Cell. Mol. Med. 9:777.
4. Robinson, C.J. and Stringer, S.E. (2001) J. Cell. Sci. 114:853.