Human LAMA5 gene encodes one of the vertebrate laminin a chains. 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 processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins are composed of 3 non identical chains: laminin a, b and g (formerly A, B1, and B2, respectively) and they form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multi-domain protein encoded by a distinct gene. The protein encoded by this gene is the a-5 subunit of laminin-10 (laminin-511), laminin-11 (laminin-521) and laminin-15 (laminin-523). Recently many functional domains have been identified in various laminin subunit protein.

Human laminin subunit a 5 protein (LAMA5) C-terminal of extracellular domain cDNA ( 3026 – 3482 aa ) was constructed with codon optimization and expressed with a small T7-His-TEV cleavage site Tag (29aa) fusion at its N-terminal. This protein is expressed in E.coli as inclusion bodies. The final product was refolded using our unique “temperature shift inclusion body refolding” technology and chromatographically purified.

1. May be used for in vitro non-glycosylated Laminin a 5 subunit C-terminal domain mediated cell proliferation regulation study with this protein as either coating matrix protein or soluble factor.

2. May be used for Laminin α5 subunit C-terminal domain protein-protein interaction assay.

3. As enzymatic substrate for various proteases.

4. As antigen for specific antibody production.