CD42a is a single-chain membrane glycoprotein that forms a noncovalent complex with CD42b. CD42b, also known as glycoprotein Ib a (GPIb a) is a membrane glycoprotein that is composed of a and b chains. The CD42b b chain is also designated CD42c, and is expressed on platelets and megakaryocytes. CD42a and CD42b are also present on platelets and mega-karyocytes, and the complex is a major component of the platelet surface. The complex acts as a receptor for von Willebrand's factor and as a von Willebrand's factor-dependent adhesion receptor.
Background References
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Post-translational Modification
Glycocalicin is the product of a proteolytic cleavage/shedding, catalyzed by ADAM17, which releases most of the extracellular domain. Binding sites for vWF and thrombin are in this part of the protein.
ICC staining CD42b in Jurkat cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
Immunohistochemical analysis of paraffin-embedded human spleen tissue with Rabbit anti-CD42b antibody (ER1803-26) at 1/1,000 dilution.
The section was pre-treated using heat mediated antigen retrieval with Tris-EDTA buffer (pH 9.0) for 20 minutes. The tissues were blocked in 1% BSA for 20 minutes at room temperature, washed with ddH2O and PBS, and then probed with the primary antibody (ER1803-26) at 1/1,000 dilution for 1 hour at room temperature. The detection was performed using an HRP conjugated compact polymer system. DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.
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