ITGA2B encodes integrin alpha chain 2b. Integrins are heterodimeric integral membrane proteins composed of an alpha chain and a beta chain. Alpha chain 2b undergoes post-translational cleavage to yield disulfide-linked light and heavy chains that join with beta 3 to form a fibronectin receptor expressed in platelets that plays a crucial role in coagulation. Mutations that interfere with this role result in thrombasthenia. In addition to adhesion, integrins are known to participate in cell-surface mediated signalling.
This gene encodes the alpha subunit of a transmembrane receptor for collagens and related proteins. The encoded protein forms a heterodimer with a beta subunit and mediates the adhesion of platelets and other cell types to the extracellular matrix. Loss of the encoded protein is associated with bleeding disorder platelet-type 9. Antibodies against this protein are found in several immune disorders, including neonatal alloimmune thrombocytopenia. This gene is located adjacent to a related alpha subunit gene. Alternative splicing results in multiple transcript variants.
ITGA3,also named as MSK18,CD49c,GAPB3 and FRP-2,belongs to the integrin alpha chain family. It is a receptor for fibronectin,laminin,collagen,epiligrin,thrombospondin and CSPG4. ITGA3 may mediate with LGALS3 the stimulation by CSPG4 of endothelial cells migration. ITGA3 is highly concentrated in epithelial cells where it strongly adheres to Laminin-5 and Laminin-5 induced rapid adhesion can be blocked by antibodies against the alpha-3 integrin subunit. It can be cleaved into heavy chain(840aa) and light chain(176aa). This antibody can recognize the heavy chain.
ITGA6 Antibody detects endogenous levels of total ITGA6.
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