Anti-Laminin subunit gamma-2 LAMC2 Antibody Picoband® Fluoro488 Conjugated

Laminin gamma2, Laminin subunit gamma-2, is a protein that in humans is encoded by the LAMC2 gene. 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 are composed of 3 non identical chains: laminin alpha, beta and gamma (formerly A, B1, and B2, respectively) and 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. 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 2. The gamma 2 chain, formerly though to be a truncated version of beta chain (B2t), is highly homologous to the gamma 1 chain; however, it lacks domain VI, and domains V, IV and III are shorter. It is expressed in several fetal tissues but differently from gamma 1, and is specifically localized to epithelial cells in skin, lung and kidney. The gamma 2 chain together with alpha 3 and beta 3 chains constitute laminin 5 (earlier known as kalinin), which is an integral part of the anchoring filaments that connect epithelial cells to the underlying basement membrane. The epithelium-specific expression of the gamma 2 chain implied its role as an epithelium attachment molecule, and mutations in this gene have been associated with junctional epidermolysis bullosa, a skin disease characterized.

Laminin subunit gamma-2; Cell-scattering factor 140 kDa subunit; CSF 140 kDa subunit; Epiligrin subunit gamma; Kalinin subunit gamma; Kalinin/nicein/epiligrin 100 kDa subunit; Ladsin 140 kDa subunit; Laminin B2t chain; Laminin-5 subunit gamma; Large adhesive scatter factor 140 kDa subunit; Nicein subunit gamma; LAMC2; LAMB2T, LAMNB2

The large variant is expressed only in specific epithelial cells of embryonic and neonatal tissues. In 17-week old embryo the small variant is found in cerebral cortex, lung, and distal tubes of kidney, but not in epithelia except for distal tubuli.

Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Ladsin exerts cell- scattering activity toward a wide variety of cells, including epithelial, endothelial, and fibroblastic cells. .

1. Aberdam, D., Galliano, M.-F., Vailly, J., Pulkkinen, L., Bonifas, J., Christiano, A. M., Tryggvason, K., Uitto, J., Epstein, E. H., Jr., Ortonne, J.-P., Meneguzzi, G.Herlitz's junctional epidermolysis bullosa is linked to mutations in the gene (LAMC2) for the gamma-2 subunit of nicein/kalinin (laminin-5) .Nature Genet. 6: 299-304, 1994. 2. Airenne, T., Haakana, H., Sainio, K., Kallunki, T., Kallunki, P., Sariola, H., Tryggvason, K.Structure of the human laminin gamma-2 chain gene (LAMC2) : alternative splicing with different tissue distribution of two transcripts.Genomics 32: 54-64, 1996. 3. Baudoin, C., Miquel, C., Gagnoux-Palacios, L., Pulkkinen, L., Christiano, A. M., Uitto, J., Tadini, G., Ortonne, J.-P., Meneguzzi, G.A novel homozygous nonsense mutation in the LAMC2 gene in patients with the Herlitz junctional epidermolysis bullosa.Hum. Molec. Genet. 3: 1909-1910, 1994.