| Antigen Alias |
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 adhesi |
| Product description |
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 thought 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 by blisters due to disruption of the epidermal-dermal
junction. Two transcript variants resulting from alternative
splicing of the 3' terminal exon, and encoding different isoforms
of gamma 2 chain, have been described. The two variants are
differentially expressed in embryonic tissues, however, the
biological significance of the two forms is not known. Transcript
variants utilizing alternative polyA_signal have also been noted in
literature.1) Tsubota, Y., et al. Int. J. Cancer 127(9):2031-2041(2010) |