Anti-Integrin beta-1 Antibody, clone 102DF5 clone 102DF5, from mouse

Integrin beta-1 (UniProt: P05556; also known as Fibronectin receptor subunit beta, Glycoprotein IIa, GPIIA, VLA-4 subunit beta, CD29) is encoded by the ITGB1 (also known as FNRB, MDF2, MSK12) gene (Gene ID: 3688) in human. Integrins are heterodimeric integral membrane proteins composed of an alpha subunit and a beta subunit that function in cell surface adhesion and signaling. Integrin beta-1 is a single-pass type I membrane protein that can associate with one of the multiple alpha subunits to serve as a receptor for fibronectin and other extracellular matrix proteins. Integrin beta-1 integrin recognizes the sequence R-G-D in a wide array of ligands. Five isoforms of integrin beta-1 have been reported that are produced by alternative splicing. Integrin beta-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). Isoform 1 of integrin beta-1 is widely expressed and other isoforms are generally co-expressed with a more restricted distribution. Isoform 2 is expressed in skin, liver, skeletal muscle, cardiac muscle, placenta, umbilical vein endothelial cells, neuroblastoma cells, lymphoma cells, hepatoma cells and astrocytoma cells. Isoform 3 and isoform 4 are expressed in muscle, kidney, liver, placenta, cervical epithelium, umbilical vein endothelial cells, fibroblast cells, embryonal kidney cells, platelets and several blood cell lines. Isoform 4 is selectively expressed in peripheral T-cells and isoform 5 is expressed specifically in striated muscle (skeletal and cardiac muscle). Isoform 2 is reported to interfere with isoform 1 resulting in a dominant negative effect on cell adhesion and migration (in vitro).