LAMB1 Antibody

Background:

Laminins, a family of extracellular matrix glycoproteins,are the major noncollagenous constituent of basement membranes.They have been implicated in a wide variety of biological processesincluding cell adhesion, differentiation, migration, signaling,neurite outgrowth and metastasis. Laminins are composed of 3 nonidentical chains: laminin alpha, beta and gamma (formerly A, B1,and B2, respectively) and they form a cruciform structureconsisting of 3 short arms, each formed by a different chain, and along arm composed of all 3 chains. Each laminin chain is amultidomain protein encoded by a distinct gene. Several isoformsof each chain have been described. Different alpha, beta and gammachain isomers combine to give rise to different heterotrimericlaminin isoforms which are designated by Arabic numerals in theorder of their discovery, i.e. alpha1beta1gamma1 heterotrimer islaminin 1. The biological functions of the different chains andtrimer molecules are largely unknown, but some of the chains havebeen shown to differ with respect to their tissue distribution,presumably reflecting diverse functions in vivo. This gene encodesthe beta chain isoform laminin, beta 1. The beta 1 chain has 7structurally distinct domains which it shares with other beta chainisomers. The C-terminal helical region containing domains I and IIare separated by domain alpha, domains III and V contain severalEGF-like repeats, and domains IV and VI have a globularconformation. Laminin, beta 1 is expressed in most tissues thatproduce basement membranes, and is one of the 3 chains constitutinglaminin 1, the first laminin isolated from Engelbreth-Holm-Swarm(EHS) tumor. A sequence in the beta 1 chain that is involved incell attachment, chemotaxis, and binding to the laminin receptorwas identified and shown to have the capacity to inhibitmetastasis.