Laminin β2/γ1 Subunits Antibody

The human basal lamina contains Collagen Type IV, proteoglycans, and glycoproteins. Laminin is a high molecular weight (850 kDa) oligomer, consisting of three different chains laminin alpha (α), beta (β), and gamma (γ) joined by disulfide bonds. The structure of human laminins include two helical domains (I & II) at the COOH-terminal, a laminin IV domain, multiple EGF-like repeats, and a laminin globular domain (G), as well as an N-terminal domain VI. Domains IV and VI are the binding sites for collagen and heparan sulfate, respectively. Several isoforms have been identified for the genes of each chain including 5 alpha chains, 4 beta chains, and 3 gamma chains. Laminin β2 and γ1 are found in laminin 121, laminin 221, laminin 421, and laminin 521. The expression of the Laminin subunits is found in the basal lamina of tissues. Here, the protein interacts with other extracellular matrix components to mediate cell attachment, migration and organization during embryonic development.

Laminin subunit gamma-1, Laminin B2 chain Laminin-1 Laminin-10 Laminin-11 Laminin-2 Laminin-3 Laminin-4 Laminin-6 Laminin-7 Laminin-8 Laminin-9 S-laminin S-LAM gamma LAMC1 LAMB2 Laminin 521, Laminin beta 2

Clone (M046) was generated from a recombinant human laminin 521 protein that includes a heterotrimer of three subunits laminin α5, laminin β2, and laminin γ1 subunits.

Clone M046 detects native laminin isoforms that include both laminin β2 and γ1 subunits. In native immunoblots, the antibody detects laminin 521, laminin 221, and laminin 121, but does not detect lamin 332 and laminin 411. The antibody weakly detects laminin 511. This antibody can be used for immunocytochemical detection of laminin β2/γ1 subunits, and can also be used for detection of native laminin isoforms in immunoblots and ELISA.