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 (alpha), beta (beta), and gamma (gamma) 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 beta2 and gamma1 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.
Clone (M046) was generated from a recombinant human laminin 521 protein that includes a heterotrimer of three subunits laminin alpha5, laminin beta2, and laminin gamma1 subunits.
Target:
Laminin beta2/gamma1 Subunits Antibody
Application Dilute:
WB(1:300-5000)
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