Rat PDGFRB / PDGFR-1 Protein (His Tag)

Platelet derived growth factor receptor, beta polypeptide Protein Datasheet

PDGFRB / PDGFR-1 Protein Product Information

• Synonym: PDGFRB, Pdgfr, Pdgfr1
• Protein Construction: A DNA sequence encoding the rat PDGFRB(Q05030)(Met1-Lys530) was expressed, fused with a polyhistidine tag at the C-terminus.
• Source: Rat
• Expression Host: Human Cells

PDGFRB / PDGFR-1 Protein QC Testing

• Purity: > 95 % as determined by SDS-PAGE
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Leu 32
• Molecular Mass: The recombinant rat PDGFRB comprises 510 amino acids and predicts a molecular mass of 57.6 kDa. The apparent molecular mass of the recombinant protein is approximately 92 kDa in SDS-PAGE under reducing conditions due to glycosylation.
• Formulation: Lyophilized from sterile PBS, pH7.4.
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: PDGFRB / PDGFR-1 protein

PDGFRB / PDGFR-1 Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

PDGFRB / PDGFR-1 Protein Description

Beta-type platelet-derived growth factor receptor, also known as CD140b, PDGFRB, PDGF-R-beta, PDGF receptor-β, is a member of the protein kinase superfamily and CSF-1/PDGF receptor subfamily. The PDGF family consists of PDGF-A, -B, -C and -D, which form either homo- or heterodimers (PDGF-AA, -AB, -BB, -CC, -DD). The four PDGFs are inactive in their monomeric forms. The PDGFs bind to the protein tyrosine kinase receptors PDGF receptor-α and -β. These two receptor isoforms dimerize upon binding the PDGF dimer, leading to three possible receptor combinations, namely -αα, -ββ and -αβ. The extracellular region of the PDGF receptor-β consists of five immunoglobulin-like domains while the intracellular part is a tyrosine kinase domain. The ligand-binding sites of PDGF receptor-α and -β are located to the three first immunoglobulin-like domains. PDGF-CC specifically interacts with PDGFR-αα and -αβ, but not with –ββ, and thereby resembles PDGF-AB. PDGF-DD binds to PDGFR-ββ with high affinity, and to PDGFR-αβ to a much lower extent and is regarded as PDGFR-ββ specific. PDGF-AA binds only to PDGFR-αα, while PDGF-BB is the only PDGF that can bind all three receptor combinations with high affinity.

References

1. Chi, KD. et al., 1997, Oncogene 15: 1051-7.
2. Arcaro, A. et al., 2000, Mol. Cell. Biol. 20: 3817-30.
3. Bergsten, E. et al., 2001, Nat. Cell Biol. 3: 512-16.
4. Zhang, Z. et al., 2004, Protein Sci. 13: 2819-24.
5. Morerio, C. et al., 2004, Cancer Res. 64: 2649-51.