Rat GP1BB Protein

Glycoprotein Ib (platelet), beta polypeptide Protein Datasheet

GP1BB Protein Product Information

• Synonym: GP1BB
• Protein Construction: A DNA sequence encoding the rat GP1BB (Q9JJM7) (Met1-Cys147) was expressed, fused with the Fc region of human IgG1 at the C-terminus.
• Source: Rat
• Expression Host: Human Cells

GP1BB Protein QC Testing

• Purity: > 85% 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: Pro 27
• Molecular Mass: The recombinant rat GP1BB/Fc is a disulfide-linked homodimer. The reduced monomer comprises 359 amino acids and has a predicted molecular mass of 40.1 kDa. The apparent molecular mass of the protein is approximately 63 kDa in SDS-PAGE under reducing conditions.
• 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: GP1BB protein

GP1BB 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.

GP1BB Protein Description

GP1BB, also known as CD42C, is the beta chain of platelet glycoprotein Ib (GPIb). GPIb is a heterodimeric transmembrane protein. GPIb is part of the GPIb-V-IX system that constitutes the receptor for von Willebrand factor, and mediates platelet adhesion in the arterial circulation. It consists of a disulfide-linked 140 kD alpha chain and 22 kD beta chain. GPIb alpha chain provides the VWF binding site, and GP1BB contributes to surface expression of the receptor and participates in transmembrane signaling through phosphorylation of its intracellular domain.

References

1. Andrews RK. et al., 1990, Biochemistry. 28 (21): 8317-26.
2. Clemetson KJ. 2007, Thromb Haemost. 98 (1): 63-8.
3. Kunishima S. et al., 2003, Int J Hematol. 76 (4): 319-27.