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VLA-4 is a cell surface heterodimer in the integrin superfamily of adhesion receptors. Anti-VLA-4 antibodies inhibited cytolytic T cell activity, with inhibitory activity directed against the effector T cells rather than their targets. Thus, whereas other VLA receptors appear to mediate cell--matrix interactions, VLA-4 may have a cell--cell adhesion function. Alpha 4 stands apart from all other known integrin alpha subunit sequences because (i) alpha 4 has neither an inserted I-domain, nor a disulfide-linked C-terminal fragment, (ii) its sequence is the most unique and (iii) only alpha 4 has a potential protease cleavage site, near the middle of the coding region, which appears responsible for the characteristic 80,000 and 70,000 Mr fragments of alpha 4 (1). Unlike any other integrin alpha subunit, the intact (150 kDa) alpha 4 subunit of VLA-4 can sometimes be cleaved into two noncovalently associated fragments (80 and 70 kDa) (2). The VLA-4 integrins are indispensable for embryogenesis, haematopoiesis and immune responses, possibly because alpha4 regulates cellular functions differently from other integrins through its cytoplasmic tail (3).
![Flow Cytometry Integrin alpha 4/CD49d Antibody (7.2R) [Unconjugated]](http://images.novusbio.com/fullsize/antibody/Integrin_alpha_4_MAB1354_Flow_Cytometry_20528.jpg)
![Immunocytochemistry Integrin alpha 4/CD49d Antibody (7.2R) [Unconjugated]](http://images.novusbio.com/fullsize/antibody/Integrin_alpha_4_MAB1354_Immunocytochemistry_6565.jpg)
