Recombinant Human Laminin subunit beta-2 (LAMB2), Truncated

Uniprot Id

P55268

Target Species

Human

Target Name

LAMB2

Target Full Name

Laminin subunit beta-2

Target Function

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.

Target Involvement

Pierson syndrome (PIERSS); Nephrotic syndrome 5 with or without ocular abnormalities (NPHS5)

Target Subcellular Location

Secreted, extracellular space, extracellular matrix, basement membrane. Note=S-laminin is concentrated in the synaptic cleft of the neuromuscular junction.

Target Research Area

Cell Adhesion

Target Synonyms

Lamb2; LAMB2_HUMAN; Laminin B1s chain; Laminin beta 2; laminin S; Laminin subunit beta 2 ; Laminin subunit beta-2; laminin; beta 2 (laminin S); Laminin-11 subunit beta; Laminin-14 subunit beta; Laminin-15 subunit beta; Laminin-3 subunit beta; Laminin-4 subunit beta; Laminin-7 subunit beta; Laminin-9 subunit beta; LAMS; NPHS5; S laminin; S-LAM beta; S-laminin subunit beta

Target Background

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), 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 beta chain isoform laminin, beta 2. The beta 2 chain contains the 7 structural domains typical of beta chains of laminin, including the short alpha region. However, unlike beta 1 chain, beta 2 has a more restricted tissue distribution. It is enriched in the basement membrane of muscles at the neuromuscular junctions, kidney glomerulus and vascular smooth muscle. Transgenic mice in which the beta 2 chain gene was inactivated by homologous recombination, showed defects in the maturation of neuromuscular junctions and impairment of glomerular filtration. Alternative splicing involving a non consensus 5' splice site (gc) in the 5' UTR of this gene has been reported. It was suggested that inefficient splicing of this first intron, which does not change the protein sequence, results in a greater abundance of the unspliced form of the transcript than the spliced form. The full-length nature of the spliced transcript is not known.