Anti-Integrin beta1 Antibody, clone MB1.2 Antibody, Alexa Fluor(R) 647 Conjugate clone MB1.2, from rat, ALEXA FLUOR(R) 647

Integrin beta-1 (UniProt P09055; also known as CD29, Fibronectin receptor subunit beta, GpIIa, VLA-1/2/3/4/5/6 subunit beta) is encoded by the Itgb1 (also known as Fnrb) gene (Gene ID 16412) in murine species. The integrin family of cell adhesion receptors consists of at least 16 membrane-associated heterodimers, composed of an alpha and beta subunit that associate in a non-covalent manner. The structure and functional diversity of the integrin family are based upon the pairing abilities of the individual alpha and beta subunits. Key to these molecular interactions between the integrin receptors and their respective ligands is the recognition of the Arg-Gly-Asp (RGD) sequence known to be present in the extracellular matrix components fibronectin, vitronectin, collagen, fibrinogen, and von Willebrand factor. Integrin beta-1 is a 130 kDa transmembrane glycoprotein that interact with various integrin alpha subunits (including alpha 1, alpha 2, alpha 3, alpha 4, alpha 5, and alpha 6) to form the functional receptor complexes that bind to specific extracellular matrix proteins. Integrin receptors regulate a variety of important biological functions, including embryonic development, wound repair, hemostasis, and prevention of programmed cell death. They are also implicated in abnormal pathological states such as tumor directed angiogenesis, tumor growth and metastasis. These heterodimeric receptors bridge the cytoplasmic actin cytoskeleton with proteins present in the extracellular matrix and/or on adjacent cells. Interactions between integrins and the extracellular matrix lead to the activation of signal transduction pathways and regulation of gene expression.