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LAMB1 Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P07942 |
|---|---|
| Clone Names | 100427020 |
| Gene ID | 3912 |
|---|---|
| Other Names | Laminin subunit beta-1, Laminin B1 chain, Laminin-1 subunit beta, Laminin-10 subunit beta, Laminin-12 subunit beta, Laminin-2 subunit beta, Laminin-6 subunit beta, Laminin-8 subunit beta, LAMB1 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP13983b was selected from the C-term region of LAMB1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | LAMB1 |
|---|---|
| Function | 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. Involved in the organization of the laminar architecture of cerebral cortex. It is probably required for the integrity of the basement membrane/glia limitans that serves as an anchor point for the endfeet of radial glial cells and as a physical barrier to migrating neurons. Radial glial cells play a central role in cerebral cortical development, where they act both as the proliferative unit of the cerebral cortex and a scaffold for neurons migrating toward the pial surface. |
| Cellular Location | Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component |
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Provided below are standard protocols that you may find useful for product applications.
Background
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 processesincluding cell adhesion, differentiation, migration, signaling,neurite outgrowth and metastasis. Laminins are composed of 3 nonidentical chains: laminin alpha, beta and gamma (formerly A, B1,and B2, respectively) and they form a cruciform structureconsisting of 3 short arms, each formed by a different chain, and along arm composed of all 3 chains. Each laminin chain is amultidomain protein encoded by a distinct gene. Several isoformsof each chain have been described. Different alpha, beta and gammachain isomers combine to give rise to different heterotrimericlaminin isoforms which are designated by Arabic numerals in theorder of their discovery, i.e. alpha1beta1gamma1 heterotrimer islaminin 1. The biological functions of the different chains andtrimer molecules are largely unknown, but some of the chains havebeen shown to differ with respect to their tissue distribution,presumably reflecting diverse functions in vivo. This gene encodesthe beta chain isoform laminin, beta 1. The beta 1 chain has 7structurally distinct domains which it shares with other beta chainisomers. The C-terminal helical region containing domains I and IIare separated by domain alpha, domains III and V contain severalEGF-like repeats, and domains IV and VI have a globularconformation. Laminin, beta 1 is expressed in most tissues thatproduce basement membranes, and is one of the 3 chains constitutinglaminin 1, the first laminin isolated from Engelbreth-Holm-Swarm(EHS) tumor. A sequence in the beta 1 chain that is involved incell attachment, chemotaxis, and binding to the laminin receptorwas identified and shown to have the capacity to inhibitmetastasis.
References
Joslyn, G., et al. Alcohol. Clin. Exp. Res. 34(5):800-812(2010)McGovern, D.P., et al. Nat. Genet. 42(4):332-337(2010)Wheeler, H.E., et al. PLoS Genet. 5 (10), E1000685 (2009) :Rooney, J.E., et al. Proc. Natl. Acad. Sci. U.S.A. 106(19):7991-7996(2009)Delektorskaya, V.V., et al. Bull. Exp. Biol. Med. 146(5):616-619(2008)
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