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Anti-Laminin subunit alpha-4 Antibody, clone 3H2 detects level of Laminin subunit alpha-4 & has been published & validated for use in WB, IH, IP, ELISA.
More>>Anti-Laminin subunit alpha-4 Antibody, clone 3H2 detects level of Laminin subunit alpha-4 & has been published & validated for use in WB, IH, IP, ELISA. Less<<
SDB (Sicherheitsdatenblätter), Analysenzertifikate und Qualitätszertifikate, Dossiers, Broschüren und andere verfügbare Dokumente.
Laminins are basement membrane, extracellular matrix glycoproteins that are composed of alpha, beta and gamma heterotrimeric chains. Different combinations of five alpha chains, three beta chains, and two gamma chains form at least 12 laminin isoforms. Laminin subunit alpha-4 contains the C-terminal G domain, and although implicated in developmental regulation due to expression profiles, the biological function of laminin subunit alpha-4 is yet to be fully understood. Laminis as a whole play an important role in cell adhesion, differentiation, migration, signaling, neurite outgrowth and metastasis. High expression has been observed in adult heart, lung, ovary, small and large intestines, placenta, and liver, with lower levels observed in skeletal muscle, kidney, pancreas, testis, prostate, and rain.
References
Product Information
Format
Purified
Control
Human serum tissue lysate (non-reduced)
Presentation
Purified mouse monoclonal IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Anti-Laminin subunit alpha-4 Antibody, clone 3H2 detects level of Laminin subunit alpha-4 & has been published & validated for use in WB, IH, IP, ELISA.
Key Applications
Western Blotting
Immunohistochemistry
Immunoprecipitation
ELISA
Application Notes
Immunohistochemistry Analysis: A 1:500 dilution from a previous lot detected Laminin subunit alpha-4 in basal cell carcinoma tissue.
ELISA Analysis: A previous lot was used by an independent laboratory in ELISA. (Wondimu, Z., et al. (2004). Blood. 104(6):1859-1866.)
Immunoprecipitation Analysis: A previous lot was used by an independent laboratory in IP. (Wondimu, Z., et al. (2004). Blood. 104(6):1859-1866.)
Biological Information
Immunogen
Recombinant protein corresponding to human Laminin subunit alpha-4.
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. [provided by RefSeq].
FUUNCTION: 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.
SUBUNIT STRUCTURE: Laminin is a complex glycoprotein, consisting of three different polypeptide chains (alpha, beta, gamma), which are bound to each other by disulfide bonds into a cross-shaped molecule comprising one long and three short arms with globules at each end. Alpha-4 is a subunit of laminin-8 (laminin-411), laminin-9 (laminin-421) and laminin-14 (laminin-423).
SUBCELLLULAR LOCATION: Secreted › extracellular space › extracellular matrix › basement membrane. Note: Major component.
TISSUE SPECIFICTY: In adult, strong expression in heart, lung, ovary small and large intestines, placenta, liver; weak or no expression in skeletal muscle, kidney, pancreas, testis, prostate, brain. High expression in fetal lung and kidney. Expression in fetal and newborn tissues is observed in certain mesenchymal cells in tissues such as smooth muscle and dermis.
DOMAIN: The alpha-helical domains I and II are thought to interact with other laminin chains to form a coiled coil structure.
SEQUENCE CAUTION: The sequence BAE06109.1 differs from that shown. Reason: Erroneous initiation.
Molecular Weight
~202 kDa observed under non-reduced conditions.
Physicochemical Information
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Quality Assurance
Evaluated by Western Blot in human serum tissue lysate under non-reduced conditions.
Western Blot Analysis: A 1:50,000 dilution of this antibody detected Laminin subunit alpha-4 in 10 µg of human serum tissue lysate (non-reduced conditions).
Usage Statement
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
