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Laminins, a family of extracellular matrix glycoproteins, are the major noncollagenous constituent of basement membranes. Additionally we are shipping LAMa4 Proteins (9) and LAMa4 Kits (6) and many more products for this protein.
Showing 10 out of 97 products:
Human Monoclonal LAMa4 Primary Antibody for IP, IHC - ABIN400457
Kawataki, Yamane, Naganuma, Rousselle, Anduraﾩn, Tryggvason, Patarroyo: Laminin isoforms and their integrin receptors in glioma cell migration and invasiveness: Evidence for a role of alpha5-laminin(s) and alpha3beta1 integrin. in Experimental cell research 2007
Show all 2 references for ABIN400457
Human Monoclonal LAMa4 Primary Antibody for EIA, IP - ABIN781770
Wondimu, Geberhiwot, Ingerpuu, Juronen, Xie, Lindbom, Doi, Kortesmaa, Thyboll, Tryggvason, Fadeel, Patarroyo: An endothelial laminin isoform, laminin 8 (alpha4beta1gamma1), is secreted by blood neutrophils, promotes neutrophil migration and extravasation, and protects neutrophils from apoptosis. in Blood 2004
Human Polyclonal LAMa4 Primary Antibody for IF, IHC - ABIN1534454
Mungall, Palmer, Sims, Edwards, Ashurst, Wilming, Jones, Horton, Hunt, Scott, Gilbert, Clamp, Bethel, Milne, Ainscough, Almeida, Ambrose, Andrews, Ashwell, Babbage, Bagguley, Bailey, Banerjee, Barker et al.: The DNA sequence and analysis of human chromosome 6. ... in Nature 2003
Knockdown of Lama4 in zebrafish resulted inthe same kind of cardiac dysfunction & hemorrhages seen in Ilk mutants. There is epistatic regulation between laminin-alpha4 (Lama4), integrin, and Ilk.
LAMA4-integrin signalling affects chondrocyte morphology and gene expression, contributing to cluster formation in osteoarthritic chondrocytes.
LAMA4 expression is lowered in preeclamptic placentas and promotes trophoblast cell invasion, migration, and angiogenesis. hypoxia-reoxygenation decreases LAMA4 expression and decouple the relationship between LAMA4 expression and p38 (show CRK Antibodies) and ERK (show EPHB2 Antibodies) activation.
Oxidative stress plays a vital role in controlling expression of LAMA4 through MAPK (show MAPK1 Antibodies) signaling pathways, which suggests a possible pathological mechanism of pre-eclampsia.
Laminins 411 and 421 differentially promote tumor cell migration via alpha6beta1 integrin and MCAM (CD146 (show MCAM Antibodies)).
These results indicate that mAbs to the laminin a4 globular domain are able to inhibit tumor cell adhesion and migration on laminins 411 and 421, and that alpha6beta1 integrin and MCAM (show MCAM Antibodies) bind a4-laminins at very close sites on the globular domain
laminin alpha4 LG4 module may play an important role in cell adhesion and/or vessel wall formation in the skin by interacting with syndecan-2 (show SDC2 Antibodies) and/or -4.
alpha4 chain Lms have a de-adhesive function and could thus play a role in detachment, migration and invasion of renal carcinoma (show TSC2 Antibodies) cells in vivo.
2 novel mutations (2828C>T [Pro943Leu] & 3217C>T [Arg1073X]) in the integrin-interacting domain of the LAMA4 gene reduce its integrin binding, & cause endothelial cell loss and heart failure.
LAMA4 is specifically up-regulated on both mRNA and protein levels in hepatocelluar carcinoma; potential role in hepatocarcinogenesis and tumor progression.
Concomitant changes take place in laminin- and collagen-binding receptors. Laminin-411 reduces adhesion to laminin-511 (show LAMA5 Antibodies) and fibronectin (show FN1 Antibodies), suggesting that tumor cells could utilize laminin-411 in their invasive behavior
Failure of laminin alpha4-mediated down-regulation of PDGF (show PDGFA Antibodies) activity contributes to the progressive renal lesions in this animal model.
biological functions of the laminin alpha 4 chain G domain and screening of active sites
The activity of a cyclic peptide from a region of laminin alpha 4 on the connecting loop between the E and F strands is highly conformation-dependent, suggesting that the E-F loop structure is crucial for its biological activity.
These results suggest that the cryptic alpha4 LG4-5 fragment derived from the laminin alpha4 chain inhibits de novo adipogenesis by modulating the effect of FGF-2 (show FGF2 Antibodies) through syndecans.
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 alpha chain isoform laminin, alpha 4. The domain structure of alpha 4 is similar to that of alpha 3, both of which resemble truncated versions of alpha 1 and alpha 2, in that approximately 1,200 residues at the N-terminus (domains IV, V and VI) have been lost. Laminin, alpha 4 contains the C-terminal G domain which distinguishes all alpha chains from the beta and gamma chains. The RNA analysis from adult and fetal tissues revealed developmental regulation of expression, however, the exact function of laminin, alpha 4 is not known. Tissue-specific utilization of alternative polyA-signal has been described in literature. Alternative splicing results in multiple transcript variants encoding distinct isoforms.
laminin, alpha 4
, laminin subunit alpha-4
, laminin subunit alpha-4-like
, laminin alpha 4 chain
, laminin [a]4
, laminin-14 subunit alpha
, laminin-8 subunit alpha
, laminin-9 subunit alpha