LAMC1 Mouse Antibody [Clone ID: M046]

Specifications

Product Data
Clone Name	M046
Applications	ICC, WB
Recommend Dilution	WB: 1:1000 ICC: 1:200
Reactivity	Human
Host	Mouse
Immunogen	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.
Specificity	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.
Formulation	PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol
Concentration	lot specific
Purification	Protein A Purified
Conjugation	Unconjugated
Storage Condition	Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C.
Predicted Protein Size	760
Database Link	UniProt ID P11047
Background	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.
Note	Protein G purified tissue culture supernatant.
Reference Data

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