Recombinant Human VEGF-B Protein, His Tag, 20 µg

Background
Vascular endothelial growth factor B (VEGFB) is also known as VEGF-related factor (VRF), is a secreted O-glycosylated protein, which belongs to the PDGF/VEGF growth factor family. VEGFB is expressed in all tissues except liver. Highest levels found in heart, skeletal muscle and pancreas. VEGFB is growth factor for endothelial cells. VEGF-B seems to play a role only in the maintenance of newly formed blood vessels during pathological conditions. VEGF-B also plays an important role on several types of neurons. It is important for the protection of neurons in the retina and the cerebral cortex during stroke and of motoneurons during motor neuron diseases such as amyotrophic lateral sclerosis.VEGF-B167 binds heparin and neuropilin-1 whereas the binding to neuropilin-1 of VEGF-B186 is regulated by proteolysis.

Source
Recombinant Human VEGF-B, His Tag (VE6-H5225) is expressed from human 293 cells (HEK293). It contains AA Pro 22 - Ala 207 (Accession # P49765-1). Predicted N-terminus: Pro 22

Molecular Characterization
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 20.3 kDa. The protein migrates as 15 kDa and 30-35 kDa under reducing (R) condition (SDS-PAGE).

Endotoxin
Less than 1.0 EU per μg of the rh VEGFB 186 by the LAL method.

Purity
>90% as determined by SDS-PAGE.

Formulation
Lyophilized from 0.22 μm filtered solution in PBS, pH7.4. Normally Mannitol or Trehalose are added as protectants before lyophilization.

Reconstitution
See Certificate of Analysis for reconstitution instructions and specific concentrations.

Storage
Avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
In lyophilized state for 1 year (4oC); After reconstitution under sterile conditions for 3 months (-70oC).

Bioactivity
Please refer to product data sheet.

References

(1) Olofsson B., et al., 1996, Proc. Natl. Acad. Sci. U.S.A. 93:2576-2581.
(2) Iyer S., et al., 2006, J. Mol. Biol. 359:76-85.
(3) Zhang F., et al., 2009, Proc. Natl. Acad. Sci. U.S.A. 106 (15): 6152–7.