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Collectively, these data show the pathogenicity of LAMB2-S80R and provide the first evidence of genetic modification of Alport phenotypes by variation in another GBM component. This
Age-related modulation of laminin beta1 versus beta2 chain expression changes the functional properties and phenotype of endothelial cells. The dysregulation of the extracellular matrix during vascular aging may contribute to age-associated impairment of organ function and fibrosis.
Disruption of LAMA4, LAMA5, and LAMB2 or the laminin-receptor interaction occurs in neuromuscular diseases including Pierson syndrome and Lambert-Eaton myasthenic syndrome (LEMS). (Review)
In conclusion, we reported three Chinese cases with different LAMB2 mutations and different phenotypes, further broadening the range of eye and kidney pathology associated with mutations in LAMB2.
Laminins 411 and 421 differentially promote tumor cell migration via alpha6beta1 integrin and MCAM (CD146).
No pathogenic LAMB2 mutations were found in the cohort of children with steroid-resistant focal segmental glomerulosclerosis.
Comprehensive gene sequencing revealed a novel LAMB2 variant (c.440A --> G; His147R) that was homozygous in the 9 living, affected family members, observed at a frequency of 2.1% in the Old Order Mennonite population, and absent in 91 non-Mennonite controls
Novel mutations in steroid-resistant nephrotic syndrome diagnosed in Tunisian children were detected in LAMB2.
All previously reported and several novel LAMB2 mutations in relation to the associated phenotype in patients from 39 unrelated families, are reviewed.
Laminin-10/11 and fibronectin differentially prevent apoptosis induced by serum removal via phosphatidylinositol 3-kinase/Akt- and MEK1/ERK-dependent pathways (Laminin 10; separate entry for Laminin 11).
Deficiency in LAMB2 causes congenital nephrosis with mesangial sclerosis and distinct eye abnormalities.
Hepalaminin, an autoantigen from chronic hepatitis C, consists of two domains of laminin beta-2 and a specific domain.
laminin isoform changes are associated with brain tumor invasion and angiogenesis [review]
Mutations in the LAMB2 gene encoding laminin beta2, a component of the glomerular basement membrane and the neuro-muscular junction are responsible for the characteristic renal and eye abnormalities of Pierson syndrome.
Recessive missense mutations in LAMB2 expand the clinical spectrum of LAMB2-associated disorders.
LAMB2 has to be considered as culprit of milder disorders including nephrosis and variable ocular anomalies.
Study summarizes recent progress concerning the molecular mechanisms of laminins in development and disease.
We demonstrated that overabundance of the beta2 chain of laminin is associated with increased basement membrane thickness and is possibly related to spermatogenic dysfunction
Milder phenotypes of Pearson Syndrome may be related to hypomorphic LAMB2 alleles.
Pierson syndrome is defined by the association of mental retardation, microcoria and DMS caused by mutation in LAMB2 gene
Loss of Lamb2 alters calcium sensitivity and voltage-gated calcium channel maturation of neurotransmission at the neuromuscular junction
Isolated a novel mouse strain with a viable nephrotic phenotype and used whole-genome sequencing to isolate a causative hypomorphic mutation in Lamb2 in hereditary nephrotic syndrome.
mild variant of Pierson syndrome caused by the C321R-LAMB2 mutation may be a prototypical ER storage disease, which may benefit from treatment approaches that target the handling of misfolded proteins.
These data suggest that beta2 and gamma3-containing laminins play an important dose-dependent role in development of the cortical pial basement membrane
Deletion of Lamb2 and Lamc3 genes affects astrocyte migration and spatial patterning in the retina.
These results suggest the possibility that up-regulation of LAMB1 in podocytes, should it become achievable, would likely lessen the severity of nephrotic syndrome in patients carrying LAMB2 mutations.
a strong impact of laminin beta2 and gamma3 subunits on the expression and function of both aquaporin-4 and Kir4.1, two important membrane proteins in Muller cells.
R246Q mutation causes nephrotic syndrome by impairing secretion of laminin-521 from podocytes into the glomerular basement membrane (GBM).
Presynaptic VDCCs link the target-derived synapse organizer laminin beta2 to active-zone proteins and function as scaffolding proteins to anchor active-zone proteins to the presynaptic membrane.
Beta2-laminin plays a role in the early structural development of the neuromuscular junction
laminin beta2, a component of the synaptic cleft at the neuromuscular junction, binds directly to calcium channels that are required for neurotransmitter release from motor nerve terminals
Glomerular basement protein permeability to the electron-dense tracer ferritin is dramatically elevated in Lamb2 deficient mice.
These results show that laminins alpha4, alpha5, and beta2 play an autocrine role in coordinating post- with presynaptic maturation.
LM alpha4 and beta2 have roles in in vitro migration and in vivo tumorigenicity of prostate cancer cells
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.
, S-laminin subunit beta
, laminin B1s chain
, laminin S
, laminin subunit 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
, laminin chain B3
, laminin chain beta 2
, laminin beta 2
, laminin, beta 1
, gamma 1 (formerly LAMB2)
, laminin, gamma 1 (formerly LAMB2)