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ELISAAntibody data
- Antibody Data
- Antigen structure
- References [4]
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- Product number
- 656 - Provider product page
- Provider
- YO Proteins AB
- Proper citation
- YO Proteins Cat#656, RRID:AB_10898414
- Product name
- Mouse anti-human CD42b (Platelet GPIb) monoclonal antibody, clone VM16d
- Antibody type
- Monoclonal
- Description
- The monoclonal antibody is directed against the CD42b antigen, platelet glycoprotein GPIb, that serves as a receptor for von Willebrand factor and as a high affinity thrombin receptor. The antigen is expressed on human platelets and megakaryocytes. The antigen is absent or present in very low levels on platelets of patients with the Bernard-Soulier syndrome. VM16d inhibits low conc. thrombin (<0.1 U/ml) induced platelet aggregation and decreases thrombin binding to platelets. F(ab')2 and F(ab') fragments are equally effective as whole intact antibodies. the VM16d-epitope is located within the 45 kDa N-terminal domain of GPIb alpha- chain. VM16d does not effect platelet interaction with von Willebrand factor, leading to the conclusion that the antibody reacts with or nearby the thrombin receptor site
- Host
- Mouse
- Conjugate
- Unconjugated
- Isotype
- IgG
- Vial size
- 1 ml
Submitted references Thrombin binding to GPIbalpha induces integrin alphaIIbbeta3 dependent platelet adhesion to fibrin in ex vivo flowing whole blood.
Thrombin binding to GPIbalpha induces platelet aggregation and fibrin clot retraction supported by resting alphaIIbbeta3 interaction with polymerized fibrin.
Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ibalpha. Identification of the sulfated tyrosine/anionic sequence Tyr-276-Glu-282 of glycoprotein Ibalpha as a binding site for von Willebrand factor and alpha-thrombin.
Characterization of an antiglycoprotein Ib monoclonal antibody that specifically inhibits platelet-thrombin interaction.
Dubois C, Reigner SC, Steiner B, Riederer MA
Thrombosis and haemostasis 2004 Feb;91(2):233-7
Thrombosis and haemostasis 2004 Feb;91(2):233-7
Thrombin binding to GPIbalpha induces platelet aggregation and fibrin clot retraction supported by resting alphaIIbbeta3 interaction with polymerized fibrin.
Dubois C, Steiner B, Kieffer N, Reigner SC
Thrombosis and haemostasis 2003 May;89(5):853-65
Thrombosis and haemostasis 2003 May;89(5):853-65
Mocarhagin, a novel cobra venom metalloproteinase, cleaves the platelet von Willebrand factor receptor glycoprotein Ibalpha. Identification of the sulfated tyrosine/anionic sequence Tyr-276-Glu-282 of glycoprotein Ibalpha as a binding site for von Willebrand factor and alpha-thrombin.
Ward CM, Andrews RK, Smith AI, Berndt MC
Biochemistry 1996 Apr 16;35(15):4929-38
Biochemistry 1996 Apr 16;35(15):4929-38
Characterization of an antiglycoprotein Ib monoclonal antibody that specifically inhibits platelet-thrombin interaction.
Mazurov AV, Vinogradov DV, Vlasik TN, Repin VS, Booth WJ, Berndt MC
Thrombosis research 1991 Jun 15;62(6):673-84
Thrombosis research 1991 Jun 15;62(6):673-84
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