Anti-LAMA5 monoclonal antibody (CABT-34834MH)

Mouse anti-Human LAMA5 monoclonal antibody for WB Datasheet

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Specifications


Host Species
Mouse
Antibody Isotype
IgG1
Clone
EML500
Species Reactivity
Human
Immunogen
Recombinant fragment: MGVSLRDKKV HWVYQLGEAG PAVLSIDEDI GEQFAAVSLD RTLQFGHMSV TVERQMIQET KGDTVAPGAE GLLNLRPDDF VFYVGGYPST FTPPPLLRFP , corresponding to amino acids 1-100 of Human Laminin alpha 5
Conjugate
Unconjugated

Applications


Application Notes
WB: 1-5 μg/ml.
*Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.

Target


Alternative Names
LAMA5; laminin, alpha 5; laminin subunit alpha-5; LAMA5; Laminin alpha 5 chain; Laminin subunit alpha 5
Entrez Gene ID
UniProt ID

Product Background


Gene summary
LAMA5 (Laminin Subunit Alpha 5) is a Protein Coding gene. Diseases associated with LAMA5 include galloway-mowat syndrome and alport syndrome. Among its related pathways are Degradation of the extracellular matrix and Metabolism. GO annotations related to this gene include receptor binding and integrin binding. An important paralog of this gene is LAMC2. This gene encodes one of the vertebrate laminin alpha chains. 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. The protein encoded by this gene is the alpha-5 subunit of of laminin-10 (laminin-511), laminin-11 (laminin-521) and laminin-15 (laminin-523).
Antigen Description
IL1F6 is a member of the interleukin 1 cytokine family. It has a conserved 12-stranded beta-trefoil structure. Binding analysis failed to detect interaction with multiple IL1R family members. 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. Laminin subunit alpha-5 is a protein that in humans is encoded by the LAMA5 gene. Components of the extracellular matrix exert myriad effects on tissues throughout the body. In particular, the laminins, a family of heterotrimeric extracellular glycoproteins, affect tissue development and integrity in such diverse organs as the kidney, lung, skin, and nervous system. It is thought that laminins mediate the attachment, migration, and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. Laminins function as heterotrimeric complexes of alpha, beta, and gamma chains, with each chain type representing a different subfamily of proteins. The protein encoded by this gene belongs to the alpha subfamily of laminin chains and is a major component of basement membranes. Two transcript variants encoding different isoforms have been found for this gene, but the full-length nature of one of them has not been determined. The function about LAMA5 antigen include binding; integrin binding; structural molecule activity.
Pathway
Alpha6-Beta4 Integrin Signaling Pathway, organism-specific biosystem; Amoebiasis, organism-specific biosystem; Amoebiasis, conserved biosystem; ECM-receptor interaction, organism-specific biosystem; ECM-receptor interaction, conserved biosystem; Focal Adhesion, organism-specific biosystem; Focal adhesion, conserved biosystem; Inflammatory Response Pathway, organism-specific biosystem; Integrin cell surface interactions, organism-specific biosystem; Pa.

Citations


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References


Fukumoto, S; Miner, JH; et al. Laminin alpha 5 is required for dental epithelium growth and polarity and the development of tooth bud and shape. JOURNAL OF BIOLOGICAL CHEMISTRY 281:5008-5016(2006).
Kikkawa, Y; Virtanen, I; et al. Mesangial cells organize the glomerular capillaries by adhering to the G domain of laminin alpha 5 in the glomerular basement membrane. JOURNAL OF CELL BIOLOGY 161:187-196(2003).

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