Mouse section of cortex stained with RPCA-Laminin-AP (red). Blue is DAPI staining of DNA. This antibody reveals strong staining in the basement membranes of blood vessels.
|Western blot analysis of RPCA-Laminin. Blot of rat heart cells lysates (lane 1) and 0.2 μg of purified laminin-111 protein from mouse EHS sarcoma (lane 2) was probed with RPCA-Laminin-AP. This antibody recognizes 3 laminin isotypes: α1 (440kDa), β1 (220kD) and γ1 (220kDa). Also recognized is a laminin binding protein at 120kDa in both rat heart lysates and purified laminin protein. Since this protein always coexpresses with laminin this crossreactivity is irrelevant.
||Rabbit polyclonal antibody to Laminin 111
||LAMA1, LAMB1, LAMC1
||440 kDa and 220 kDa
||Laminin-111 isolated from mouse EHS cells
||Antibody is supplied as purified antibody at 1 mg/ml in 50% glycerol/PBS.
||Western blot, ICC/IF, IHC
|Suggestions for use
||Western blot: 1:1,000-5,000. ICC/IF and IHC: 1:1,000-5,000.
||Shipped on ice. Store at 4°C. For long term storage, leave frozen at -20°C. Avoid freeze / thaw cycles.
Laminins are high-molecular weight (~400kDa) proteins of the extracellular matrix. They are an important and biologically active part of the basal lamina, which is one of the layers of the basement membrane, a protein network foundation for most cells and organs, influencing cell differentiation, migration, and adhesion (1,2). Laminins are heterotrimeric proteins that contain an α-chain, a β-chain, and a γ-chain. The distribution of the different laminin isoforms is tissue-specific (2). The laminin molecules are named according to their chain composition.
Laminin-111 is one of the first laminin isoforms to be discovered . The “111” identifies the isoform’s chain composition of α1β1γ1. Laminin-111 is predominantly expressed in the embryonic epithelium, but can also be found in some adult epithelium such as the kidney,liver, testis, ovaries, and brain blood vessels. Laminin-111 has been identified as a crucial molecule for development of the embryo, genetic ablation of laminin-111 results in embryonic death. The presence of laminin-111 increased muscle strength and protected it from injury (3). The experiments utilizing laminin–111 as a source of therapy for Duchenne muscular dystrophy suggest that it has protective qualities in addition to its association with muscle tissue. Additionally, laminin-111 induces neurites outgrowth via nitric oxide (4). Laminin-111 has also been implicated in cancer by regulation of nuclear actin (5).
1: Aumailley M, Bruckner-Tuderman L, Carter WG, Deutzmann R, Edgar D, Ekblom P, & Yurchenco PD. A simplified laminin nomenclature. Matrix biology, 24:326-332 (2005)
2: Durbeej M. Laminins. Cell and Tissue Research, 339:259-268 (2010).
3: Ekblom M, Falk M, Salmivirta K, Durbeej M, & Ekblom P. Laminin isoforms and epithelial development. Annals of the New York Academy of Sciences, 857:194-211 (1998).
4: Rialas CM, Nomizu M, Patterson, M, Kleinman HK, Weston CA, and Weeks BS . Nitric Oxide mediates laminin-induced neurite outgrowth in PC12 cells. Experimental Cell Research, 260:268-276 (2000).
5: Rooney JE, Gurpur PB, & Burkin DJ. Laminin-111 protein therapy prevents muscle disease in the mdx mouse model for Duchenne muscular dystrophy. PNAS 106:7991-7996 (2009).
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