Recombinant Human CD42b/GPIb alpha Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

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Recombinant Human CD42b/GPIb alpha Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. Recombinant Human CD42b/GPIb alpha is immobilized at 0.5 μg/mL (100 μL/well), the concentration of Recombinant Human vWF-A2 (Catalog # 2764-WF) that produces 50% optimal binding response is approximately 6-36 ng/mL in the presence of ristocetin.
Source
Mouse myeloma cell line, NS0-derived human CD42b/GPIb alpha protein
His17-Leu505, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
His17
Protein/Peptide Type
Recombinant Proteins
Gene
GP1BA
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Theoretical MW
54.7 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
95-120 kDa, reducing conditions
Publications
Read Publication using
4067-GP in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human CD42b/GPIb alpha Protein, CF

  • Antigen CD42b-alpha
  • BP1BA
  • BSS
  • CD42b antigen
  • CD42b
  • CD42b-alpha
  • glycoprotein Ib (platelet), alpha polypeptide
  • Glycoprotein Ibalpha
  • GP1B
  • GP1BA
  • GPIb alpha
  • GP-Ib alpha
  • GPIbA
  • GPIb-alpha
  • MGC34595
  • platelet glycoprotein Ib alpha chain
  • platelet membrane glycoprotein 1b-alpha subunit

Background

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).

  1. Andrews, R.K. et al. (2007) Arterioscler. Thromb. Vasc. Biol. 27:1511. 
  2. Lopez, J.A. et al. (1987) Proc. Natl. Acad. Sci. USA 84:5615.
  3. Wenger, R.H. et al. (1988) Biochem. Biophys. Res. Commun. 156:389. 
  4. Luo, S-Z. et al. (2007) Blood 109:603. 
  5. Uff, S. et al. (2002) J. Biol. Chem. 277:35657.
  6. Shen, Y. et al. (2006) J. Biol. Chem. 281:26419.
  7. Ishida, F. et al. (1995) Blood 86:1356.
  8. Gardiner, E.E. et al. (2007) J. Thromb. Haemost. 5:1530.
  9. Beer, J.H. et al. (1994) Blood 83:691.
  10. Adam, F. et al. (2003) Eur. J. Biochem. 270:2959.
  11. Baglia, F.A. et al. (2004) J. Biol. Chem. 279:49323.
  12. Bradford, H.N. et al. (2000) J. Biol. Chem. 275:22756.
  13. Wang, Y. et al. (2005) Circulation 112:2993.
  14. Othman, M. et al. (2005) Blood 105:4330.

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Publications for CD42b/GPIb alpha (4067-GP)(1)

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: Binding Assay.


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Bioinformatics

Gene Symbol GP1BA
Uniprot