Human CD42b/GPIb alpha Antibody Summary
His17-Leu505
Accession # P07359
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Detection of Human CD42b/GPIb alpha by Western Blot. Western blot shows lysates of human platelets. PVDF membrane was probed with 1 µg/mL of Sheep Anti-Human CD42b/GPIb a Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4067) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). A specific band was detected for CD42b/GPIb a at approximately 135 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
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Detection of Human CD42b/GPIb alpha in Human Whole Blood CD41+Platelets by Flow Cytometry. Human whole blood CD41+platelets were stained with Sheep Anti-Human CD42b/GPIb a Polyclonal Antibody (Catalog # AF4067) followed by NL637-conjugated anti sheep antibody (Catalog # NL011) and Human CD41 FITC-conjugated Monoclonal Antibody. Quadrant markers were set based on control antibody staining (Catalog # 5-001-A).
Reconstitution Calculator
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
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 Gly480 and Val481. 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.
Product Datasheets
Citations for Human CD42b/GPIb alpha Antibody
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.
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Cleavage by MMP‐13 renders VWF unable to bind to collagen but increases its platelet reactivity
Authors: Joanna‐Marie Howes, Vera Knäuper, Jean‐Daniel Malcor, Richard W. Farndale
Journal of Thrombosis and Haemostasis
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Atroxlysin-III, A Metalloproteinase from the Venom of the Peruvian Pit Viper Snake Bothrops atrox (Jerg�n) Induces Glycoprotein VI Shedding and Impairs Platelet Function
Authors: LS Oliveira, MI Estevão-Co, VG Alvarenga, DE Vivas-Ruiz, A Yarleque, AM Lima, A Cavaco, JA Eble, EF Sanchez
Molecules, 2019-09-26;24(19):.
Species: Human
Sample Types: Platelets
Applications: Western Blot -
The collagen-binding integrin alpha2beta1 is a novel interaction partner of the Trimeresurus flavoviridis venom protein flavocetin-A.
Authors: Arlinghaus F, Eble J
J Biol Chem, 2012-11-30;288(2):947-55.
Species: Human
Sample Types: Cell Lysates
Applications: Western Blot
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