The basal lamina contains Collagen Type IV, proteoglycans, and glycoproteins. Laminin is a high molecular weight (850 kDa) oligomer, consisting of three different chains (α, β, and γ) joined by disulfide bonds. The structure of 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. Laminin γ1 (laminin B2) contains 14 glycosylation sites and 12 cysteine repeat domains. 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.
Pikkarainen, T. et al. (1988) J Biol Chem. 263(14):6751.
*For more information, see UniProt Accession P11047
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
This kit contains: