Recombinant Human CD42b/GPIb alpha Protein, CF
Recombinant Human CD42b/GPIb alpha Protein, CF Summary
His17-Leu505, with a C-terminal 6-His tag
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in sterile PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Background: CD42b/GPIb alpha
Platelet glycoprotein Ib alpha chain (GPIb alpha ), also known as CD42b alpha, is a 145 kDa type I transmembrane protein that is a member of the leucine‑rich repeat (LRR) family of ligand binding proteins (1‑3). It is expressed by platelets as the ligand‑binding subunit of the platelet GPIb‑IX‑V complex (4). Human GPIb alpha contains a 16 amino acid (aa) signal sequence, a 489 aa extracellular domain (ECD), a 21‑aa transmembrane domain, and a 100 aa cytoplasmic region. The ECD contains 8 LRRs, with # 2, 3 and 4 having been demonstrated to regulate shear‑dependent adhesion to von Willebrand factor (vWF) (5, 6). The LRRs are followed by a thrombin‑binding anionic region that includes three sulfated tyrosines, a sialomucin domain with N‑ and O‑linked carbohydrates, and two cysteines near the membrane that allow dimerization with GP1b alpha beta (1‑6). Four human isoforms with 1 to 4 repeats of aa 398‑411 within the sialomucin domain of mature GPIb alpha are known to exist but have unknown significance (7). The ECD of human GPIb alpha shares 48‑51% aa identity with mouse, rat, bovine and canine GPIb alpha. The metalloproteinase TACE/ADAM17 constitutively and inducibly cleaves GPIb alpha, between Gly 480 and Val 481. This releases a soluble form called glycocalicin that circulates at ~2 μg/mL (8, 9). GPIb alpha binding to ligands such as thrombin, kininogen, and coagulation factors XI and XII helps to initiate platelet activation and coordinate the coagulation cascade (1, 10‑12). Binding of GPIb alpha to vWF or thrombospondin in the plasma or matrix, vWF or P‑selectin on endothelial cells, or the integrin alpha M beta 2 (MAC‑1) on myeloid cells, controls response to vascular injury (1, 13). Bernard‑Soulier syndrome and platelet‑type von Willebrand disease are platelet function disorders that can be caused by mutations in GPIb alpha (1, 14).
- Andrews, R.K. et al. (2007) Arterioscler. Thromb. Vasc. Biol. 27:1511.
- Lopez, J.A. et al. (1987) Proc. Natl. Acad. Sci. USA 84:5615.
- Wenger, R.H. et al. (1988) Biochem. Biophys. Res. Commun. 156:389.
- Luo, S-Z. et al. (2007) Blood 109:603.
- Uff, S. et al. (2002) J. Biol. Chem. 277:35657.
- Shen, Y. et al. (2006) J. Biol. Chem. 281:26419.
- Ishida, F. et al. (1995) Blood 86:1356.
- Gardiner, E.E. et al. (2007) J. Thromb. Haemost. 5:1530.
- Beer, J.H. et al. (1994) Blood 83:691.
- Adam, F. et al. (2003) Eur. J. Biochem. 270:2959.
- Baglia, F.A. et al. (2004) J. Biol. Chem. 279:49323.
- Bradford, H.N. et al. (2000) J. Biol. Chem. 275:22756.
- Wang, Y. et al. (2005) Circulation 112:2993.
- Othman, M. et al. (2005) Blood 105:4330.
Citation for Recombinant Human CD42b/GPIb alpha Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
Redox control of beta2-glycoprotein I-von Willebrand factor interaction by thioredoxin-1.
Authors: Passam FH, Rahgozar S, Qi M, Raftery MJ, Wong JW, Tanaka K, Ioannou Y, Zhang JY, Gemmell R, Qi JC, Giannakopoulos B, Hughes WE, Hogg PJ, Krilis SA
J. Thromb. Haemost., 2010;8(8):1754-62.
Sample Types: Buffer
Applications: Binding Assay
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