*Optimal dilutions/concentrations should be determined by the researcher.
|0.5-1ug/ml for 30 minutes at RT
Boiling tissue sections in 10mM Citrate Buffer, pH 6.0, for 10-20 min followed by cooling at RT for 20 minutes
Not tested in other applications.
Laminins are large hetero-trimeric, non-collagenous glycoproteins composed of α, β, and γ chains. This MAb reacts with laminin B2/1 chain of ~210kDa and does not cross-react with other basement membrane components or fibronectin. Its specificity was established by immunoprecipitation and immunofluorescence of human skeletal muscle and kidney with laminin chain-specific MAbs. Epithelial sheets in vivo are separated from the mesenchymal elements of the stroma by a thin layer of a specialized type of extracellular matrix termed the basement membrane (BM). This structure consists of individual components, some of which are ubiquitous in BMs and some are not. The ubiquitous ones comprise laminin (LN), entactin/nidogen (EN), collagen type IV (CIV), and large heparan sulfate proteoglycan (HSPG), which interact specifically with each other to form a continuous and regular BM. Alterations of BM integrity, from local discontinuities up to complete loss, are described in many types of human and animal epithelial neoplasms. This MAb stains uniformly all human and murine basement membranes.
Prepared in 10mM PBS with 0.05% BSA and 0.05% azide.
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Murine EHS laminin preparation
Ab purified from Bioreactor Concentrate by Protein A/G
For laboratory use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Laminin Subunit Gamma 1,Lamb2,Lamc1
Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. They have been implicated in a wide variety of biological processes including cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. Laminins, composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively), have a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains. Each laminin chain is a multidomain protein encoded by a distinct gene. Several isoforms of each chain have been described. Different alpha, beta and gamma chain isomers combine to give rise to different heterotrimeric laminin isoforms which are designated by Arabic numerals in the order of their discovery, i.e. alpha1beta1gamma1 heterotrimer is laminin 1. The biological functions of the different chains and trimer molecules are largely unknown, but some of the chains have been shown to differ with respect to their tissue distribution, presumably reflecting diverse functions in vivo. This gene encodes the gamma chain isoform laminin, gamma 1. The gamma 1 chain, formerly thought to be a beta chain, contains structural domains similar to beta chains, however, lacks the short alpha region separating domains I and II. The structural organization of this gene also suggested that it had diverged considerably from the beta chain genes. Embryos of transgenic mice in which both alleles of the gamma 1 chain gene were inactivated by homologous recombination, lacked basement membranes, indicating that laminin, gamma 1 chain is necessary for laminin heterotrimer assembly. It has been inferred by analogy with the strikingly similar 3' UTR sequence in mouse laminin gamma 1 cDNA, that multiple polyadenylation sites are utilized in human to generate the 2 different sized mRNAs (5.5 and 7.5 kb) seen on Northern analysis. [provided by RefSeq, Aug 2011]