GP1BB Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | P13224 |
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Gene ID | 2812 |
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Other Names | Platelet glycoprotein Ib beta chain, GP-Ib beta, GPIb-beta, GPIbB, Antigen CD42b-beta, CD42c, GP1BB |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | GP1BB |
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Function | Gp-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to von Willebrand factor, which is already bound to the subendothelium. |
Cellular Location | Membrane; Single-pass type I membrane protein. |
Tissue Location | Expressed in heart and brain. |
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Provided below are standard protocols that you may find useful for product applications.
Background
GP1BB is a heterodimeric transmembrane protein consisting of a disulfide-linked 140 kD alpha chain and 22 kD beta chain. It is part of the GPIb-V-IX system that constitutes the receptor for von Willebrand factor (VWF), and mediates platelet adhesion in the arterial circulation. GPIb alpha chain provides the VWF binding site, and GPIb beta contributes to surface expression of the receptor and participates in transmembrane signaling through phosphorylation of its intracellular domain. Mutations in the GPIb beta subunit have been associated with Bernard-Soulier syndrome, velocardiofacial syndrome and giant platelet disorder. The 206 amino acid precursor of GPIb beta is synthesized from a 1.0 kb mRNA expressed in plateletes and megakaryocytes. A 411 amino acid protein arising from a longer, unspliced transcript in endothelial cells has been described.
References
Xu,X. Vox Sang. 97 (4), 330-337 (2009)Mo,X. J. Thromb. Haemost. 7 (9), 1533-1540 (2009)Hadjkacem,B. Ann. Hematol. 88 (5), 465-472 (2009)
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