Anti-Integrin alpha5beta1 Antibody

Integrin alpha-5 beta1 (UniProt: P08648/P05556); also known as CD49 antigen-like family member E, Fibronectin receptor subunit alpha/Fibronectin receptor subunit beta, VLA-5/ VLA-4 subunit beta, CD49e/CD29) is encoded by the ITGA5/ITGB1 (also known as FNRA/FNRB, MDF2, MSK12) gene (Gene ID: 3678/3688) in human. Integrins are heterodimeric integral membrane proteins composed of an a subunit and a b subunit that function in cell surface adhesion and signaling. Integrin a5 is expressed on thymocytes, T cells, monocytes, platelets, early B cells, and activated in B cells. Integrin a5 exhibits an increased expression in mesodermal progenitors and is shown to be prevalent in fetal cardiomyocytes. Its deletion is shown to cause mesodermal defects during embryogenesis in murine models. Membrane fractions obtained from fibroblasts of diabetic animals display significant reduction in integrin a5 levels. Integrin a5 is a single-pass type I membrane glycoprotein that is synthesized with a signal peptide (aa 1-41), which is subsequently cleaved off to generate the mature form that contains a heavy chain (aa 42-894) and a light chain (aa 895-1049). Structurally, it consists of an extracellular domain (aa 42-995), a transmembrane domain (aa 996-1021), and a cytoplasmic domain (aa 1022-1049). It contains four calcium binding sites (aa 480-488; 334-342; 401-409; and 465-473). When associated with b 1 subunit it can serve as a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands. Integrin b 1 is synthesized with a signal peptide (aa 1-20) that is subsequently cleaved off. The mature form has an extracellular domain (aa 21-728), a helical domain (aa 729-751) and a cytoplasmic region (aa 752-798). (Ref.: Almeida, ME et al., (2016). Mol. Cell. Biochem. 421(1-2); 19-28; Neiman, G., et al. (2019). Sci. Rep. 9; 18077; Su, Y., et al. (2016). Proc. Natl. Acad. Sci. USA. 113(27); E3872-E3881).