Laminin subunit beta-2 Recombinant Protein | LAMB2 recombinant protein

Recombinant Human Laminin subunit beta-2 protein

Cat. Num. AAA1265341

• Gene Names: LAMB2; LAMS; NPHS5
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Laminin subunit beta-2; Recombinant Human Laminin subunit beta-2 protein; Laminin B1s chain; 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; S-laminin subunit beta; S-LAM beta; LAMB2 recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 1530-1798aa; Partial
• Sequence: PDSIEMVATRVLELSIPASAEQIQHLAGAIAERVRSLADVDAILARTVGDVRRAEQLLQDARRARSWAEDEKQKAETVQAALEEAQRAQGIAQGAIRGAVADTRDTEQTLYQVQERMAGAERALSSAGERARQLDALLEALKLKRAGNSLAASTAEETAGSAQGRAQEAEQLLRGPLGDQYQTVKALAERKAQGVLAAQARAEQLRDEARDLLQAAQDKLQRLQELEGTYEENERALESKAAQLDGLEARMRSVLQAINLQVQIYNTCQ
• Sequence Length: 1798

• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-PAGE

Related Product Information for LAMB2 recombinant protein

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.

Product Categories/Family for LAMB2 recombinant protein

Cell adhesion

References

Human beta 2 chain of laminin (formerly S chain) cDNA cloning, chromosomal localization, and expression in carcinomas.Wewer U.M., Gerecke D.R., Durkin M.E., Kurtz K.S., Mattei M.-G., Champliaud M.-F., Burgeson R.E., Albrechtsen R.Genomics 24:243-252(1994) The human laminin beta 2 chain (S-laminin) structure, expression in fetal tissues and chromosomal assignment of the LAMB2 gene.Iivanainen A., Vuolteenaho R., Sainio K., Eddy R., Shows T.B., Sariola H., Tryggvason K.Matrix Biol. 14:489-497(1995) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Human laminin beta2 deficiency causes congenital nephrosis with mesangial sclerosis and distinct eye abnormalities.Zenker M., Aigner T., Wendler O., Tralau T., Muentefering H., Fenski R., Pitz S., Schumacher V., Royer-Pokora B., Wuehl E., Cochat P., Bouvier R., Kraus C., Mark K., Madlon H., Doetsch J., Rascher W., Maruniak-Chudek I., Lennert T., Neumann L.M., Reis A.Hum. Mol. Genet. 13:2625-2632(2004) Recessive missense mutations in LAMB2 expand the clinical spectrum of LAMB2-associated disorders.Hasselbacher K., Wiggins R.C., Matejas V., Hinkes B.G., Mucha B., Hoskins B.E., Ozaltin F., Nuernberg G., Becker C., Hangan D., Pohl M., Kuwertz-Broeking E., Griebel M., Schumacher V., Royer-Pokora B., Bakkaloglu A., Nuernberg P., Zenker M., Hildebrandt F.Kidney Int. 70:1008-1012(2006) A novel mutation of LAMB2 in a multigenerational mennonite family reveals a new phenotypic variant of Pierson syndrome.Mohney B.G., Pulido J.S., Lindor N.M., Hogan M.C., Consugar M.B., Peters J., Pankratz V.S., Nasr S.H., Smith S.J., Gloor J., Kubly V., Spencer D., Nielson R., Puffenberger E.G., Strauss K.A., Morton D.H., Eldahdah L., Harris P.C.Ophthalmology 118:1137-1144(2011)

NCBI and Uniprot Product Information

• NCBI GI #: 119703755
• NCBI GeneID: 3913
• NCBI Accession #: NP_002283.3
• NCBI GenBank Nucleotide #: NM_002292.3
• UniProt Accession #: P55268; Q16321
• Molecular Weight: 33.3 kDa
• NCBI Official Full Name: laminin subunit beta-2
• NCBI Official Synonym Full Names: laminin subunit beta 2
• NCBI Official Symbol: LAMB2
• NCBI Official Synonym Symbols: LAMS; NPHS5
• NCBI Protein Information: laminin subunit beta-2
• UniProt Protein Name: Laminin subunit beta-2
• Protein Family: Laminin
• UniProt Gene Name: LAMB2
• UniProt Synonym Gene Names: LAMS; S-LAM beta
• UniProt Entry Name: LAMB2_HUMAN

NCBI 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, 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. [provided by RefSeq, Aug 2011]

Uniprot Description

LAMB2: 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. Defects in LAMB2 are the cause of Pierson syndrome (PIERSS); also known as microcoria-congenital nephrotic syndrome. Pierson syndrome is characterized by nephrotic syndrome with neonatal onset, diffuse mesangial sclerosis and eye abnormalities with microcoria as the leading clinical feature. Death usually occurs within the first weeks of life. Disease severity depends on the mutation type: nontruncating LAMB2 mutations may display variable phenotypes ranging from a milder variant of Pierson syndrome to isolated congenital nephrotic syndrome. Defects in LAMB2 are the cause of nephrotic syndrome type 5 with or without ocular abnormalities (NPHS5). NPHS5 is a renal disease characterized clinically by proteinuria, hypoalbuminemia, hyperlipidemia and edema. Kidney biopsies show non-specific histologic changes such as focal segmental glomerulosclerosis and diffuse mesangial proliferation. Some affected individuals have an inherited steroid-resistant form and progress to end-stage renal failure. NPHS5 is characterized by very early onset of progressive renal failure. A subset of patients may develop mild ocular anomalies, such as myopia, nystagmus, and strabismus.

Protein type: Extracellular matrix; Motility/polarity/chemotaxis; Secreted; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 3p21

Cellular Component: basal lamina; basement membrane; extracellular matrix; extracellular region; laminin-3 complex; synapse

Molecular Function: integrin binding; structural molecule activity

Biological Process: astrocyte development; axon extension involved in regeneration; axon guidance; cell adhesion; extracellular matrix organization and biogenesis; neuromuscular junction development; retina development in camera-type eye; Schwann cell development; visual perception

Disease: Nephrotic Syndrome, Type 5, With Or Without Ocular Abnormalities; Pierson Syndrome