Human Merosin

Human merosin protein affinity purified with monoclonal 5H2 (MAB1922). Clone 5H2binds the laminin alpha2 chain. In native purifications laminin 2 (alpha2beta1gamma1) and laminin 4 (alpha2beta2gamma1) isoforms are isolated via affinity purification over 5H2.
CC085 is immunologically and biologically similar to human laminin (Merosin is an oldername). This preparation contains several bands by SDS-PAGE, with primary bands at ~300-250 kDa, 200 and 80 kDa in 6% reducing gels.

Laminins are a family of large trimeric basement membrane glyco-proteins composed of 3 non-identical chains, the alpha-, beta- and gamma-chains. The three chains associate at their C-terminal end in a coiled coil. 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. The long arm is formed by the coiled coil and the short arms by the N-terminal ends. Each laminin chain is a multi-domain protein encoded by a distinct gene. Several isoforms of each chain have been described. In human, five different alpha, three beta and two gamma chains have been identified, their genes dispersed throughout the genome. The biological functions of the different chains and trimer molecules are largely unknown. Some of the chains have been shown to differ extensively with respect to their tissue distribution, presumably reflecting diverse functions in vivo. The different laminin isoforms consist of different combinations of the alpha-, beta- and gamma-chains which are designated by Arabic numerals in the order of their discovery. Laminin-1 (alpha-1 + beta-1 + gamma-1), laminin-2 (merosin, alpha-2 + beta-1 + gamma-1), laminin-3 (alpha-1 + beta-2 + gamma-1), laminin-4 (alpha-2 + beta-2 + gamma-1), laminin-5 (alpha-3 + beta-3 + gamma-2), laminin-6 (alpha-3 + beta-1 + gamma-1), laminin-7 (alpha-3 + beta-2 + gamma-1), laminin-8 (alpha-4 + beta-1 + gamma-1), laminin-9 (alpha-4 + beta-2 + gamma-1) and laminin-10 (alpha-5 + beta-1 + gamma-1) (Miner et al., J Biol Chem 270(48):28523-28528, 1995). Laminin-2 and -4 are specifically enriched in the basement membranes surrounding skeletal muscle fibers and peripheral nerves. While the beta-1, beta-2 and gamma-1 chains are ubiquitously expressed, tissue-specificity is provided only by the alpha-2 chain, formerly described as merosin.

Laminin-alpha 2 is widely expressed in the basement membrane of skeletal muscle, at neuromuscular synpases, extra-synaptically and in the myotendinous junctions. LAMA2 has been shown to bind to dystroglycan, which interacts with dystrophin and extra-cellular laminin. Recently mutations have been mapped to the LAMA2 gene that seem imply a role in congenital muscular dystrophy (CMD). {http://jmg.bmjjournals.com/cgi/content/full/38/10/649}

Product Source: Human placenta, assayed negative for antibodies to HBsAg, HIV-1, HIV-2.

Suitable for use in ELISA, production of anti-serum, and neurite-stimulation assays, and cell attachment assays. Active in cell attachment assays at 10 μg/mL.

Optimal working dilutions must be determined by end user.

Purified merosin protein in PBS containing 0.1% sodium azide.

Maintain short term at -20ºC in undiluted aliquots for up to three months from date of receipt. For long term storage, maintain at -70ºC in undiluted aliquots for up to one year from date of receipt. Avoid repeated freeze/thaw cycles.

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