LAMB2
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Official Full Name
laminin, beta 2 (laminin S) -
Overview
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. -
Synonyms
LAMB2;laminin, beta 2 (laminin S);LAMS;laminin subunit beta-2;laminin S;S-LAM beta;laminin B1s chain;S-laminin subunit beta;NPHS5
Recombinant Proteins
- Rhesus macaque
- Human
- Rat
- Chicken
- Zebrafish
- Mouse
- Mammalian Cell
- HEK293
- HEK293T
- E.coli
- Mamanlian cells
- His
- Myc&DDK
- His&GST
- His&Fc&Avi
- Flag
- GST
Involved Pathway
LAMB2 involved in several pathways and played different roles in them. We selected most pathways LAMB2 participated on our site, such as PIK-Akt signaling pathway,Focal adhesion,ECM-receptor interaction, which may be useful for your reference. Also, other proteins which involved in the same pathway with LAMB2 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| Small cell lung cancer | TRAF4,PIK3CB,ITGA2B,ITGA6,CCND1,LAMA5,CKS2,APAF1,TRAF1,TRAF3 |
| PIK-Akt signaling pathway | INS,NGF,FLT4,GNG3,SOS1,GNG5,FGF12,GYS1,FGF19,RHEB |
| Pathways in cancer | IL-8,GNG3,TGFB1,PIK3CB,SMAD4,LPAR3,WNT5A,RAC2,ERBB2,STAT1 |
| Focal adhesion | VEGFA,TNN,MYLPFA,THBS1,PAK6,ACTN2,ITGB1A,PIK3CG,Reln,PTENA |
| Amoebiasis | IL12B,LAMB1,C8A,PIK3CD,RAB5C,C8G,IL1B2,ITGB2L,PLCB4,PRKACG |
| Toxoplasmosis | NFKB1,PIK3CG,TLR2,TGFB2,MAP2K6,LAMC2,TAB2,IFNG,IRAK4,MAPK11 |
| ECM-receptor interaction | ITGA8,ITGB1,Npnt,ITGAV,ITGB3,THBS4,VTN,COL2A1,ITGA9,COL24A1 |
Protein Function
LAMB2 has several biochemical functions, for example, integrin binding,structural molecule activity. Some of the functions are cooperated with other proteins, some of the functions could acted by LAMB2 itself. We selected most functions LAMB2 had, and list some proteins which have the same functions with LAMB2. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| structural molecule activity | ODF2,CLDN23,LCE3D,LCE1F,KRT81,MAP4,MPZ,KRT6C,FLG,LELP1 |
| integrin binding | S1PR3,CTGFA,CYR61,SEMA7A,CTGFB,FN1A,ICAM5,CTGF,GFAP,NIPAL1 |
Interacting Protein
LAMB2 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with LAMB2 here. Most of them are supplied by our site. Hope this information will be useful for your research of LAMB2.
PIK3R2;ATXN7;ORC5;ul31_ebvb9;RBL1;STAT3;KPNA2;BNLF1;ZNF512B;PLEKHA5;q9wmx2-pro_0000037548;midostaurin
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References
- Liapis, H; et al. Molecular pathology of nephrotic syndrome in childhood: A contemporary approach to diagnosis. PEDIATRIC AND DEVELOPMENTAL PATHOLOGY 11:254-263(2008).
- Berfield, AK; Hansen, KM; et al. Rat glomerular mesangial cells require laminin-9 to migrate in response to insulin-like growth factor binding protein-5. AMERICAN JOURNAL OF PHYSIOLOGY-CELL PHYSIOLOGY 291:C589-C599(2006).
- Zenker, M; Aigner, T; et al. Human laminin beta 2 deficiency causes congenital nephrosis with mesangial sclerosis and distinct eye abnormalities. HUMAN MOLECULAR GENETICS 13:2625-2632(2004).
