Platelet membrane glycoprotein Ib (GPIba) is comprised of an a and b subunit linked by disulfide bonds. GPIba (also known as CD42b) is a 135 kDa membrane protein subunit that binds a variety of adhesive and procoagulant ligands, including von Willebrand factor. Cleavage of GPIba by the “sheddase” ADAM17 releases the ectodomain glycocalicin into plasma. ADAM17 cleaves GPIba at Gly464-Val465.

GPIba General References

  1. E.E. Gardiner, D. Karunakaran, Y. Shen, J.F. Arthur, R.K. Andrews, M.C. Berndt. Controlled shedding of platelet glycoprotein (GP)VI and GPIb-IX-V by ADAM family metalloproteinases. (2007). J Thromb Haemost; 5(7):1530–1537
  2. R.W. Colman. Major platelet Glycoproteins: Platelet Glycoprotein Ib-IX-V (2006). Hemostasis and Thrombosis: Basic Principles and Clinical Practice. Philadelphia, PA: Lippincott Williams & Wilkins.
  3. R. Li, J. Emsley. The Organizing Principle of Platelet Glycoprotein Ib-IX-V Complex. (2013). J Thromb Haemost. 11(4): 605–614.

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    Catalog # Specificity Isotype ELISA Blotting Data Sheet and Pricing Add To Cart
  • GMA-340 Shedding cleavage site of GPIba IgG1 Binds immobilized human platelet GPIba and synthetic peptide. Blots under reduced and non-reduced conditions. View Add To Cart