Laminin α-1 Antibody (E3-2): sc-65646

Laminin α-1 Antibody (E3-2) is a rat monoclonal IgG2a antibody that detects Laminin α-1 in mouse samples through applications such as immunoprecipitation (IP), immunofluorescence (IF), and immunohistochemistry. Laminin α-1 is a crucial component of basement membranes, which are specialized extracellular matrices that provide structural support and influence various cellular processes. These membranes are essential for maintaining tissue integrity and play a significant role in cell proliferation, migration, and differentiation. The unique structure of Laminin α-1, which consists of a heterotrimer formed by α, β, and γ chain subunits, allows for self-assembly and interaction with other matrix components, facilitating the formation of stable basement membranes. This structural versatility enables Laminin α-1 to mediate interactions with cell surface receptors such as integrins and dystroglycan, thereby influencing cellular behavior and tissue architecture. The human Laminin α-1 gene is located on chromosome 18p11.3 and has been found to be over-expressed in the frontal cortex of individuals with Alzheimer′s disease, highlighting potential roles in neurodegenerative conditions. Anti-Laminin α-1 antibody (E3-2) serves as an invaluable tool for researchers studying basement membrane dynamics and cellular functions in various biological contexts.

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Laminin α-1 Antibody (E3-2) References:

1. Identification of an upstream enhancer in the mouse laminin alpha 1 gene defining its high level of expression in parietal endoderm cells.  |  Niimi, T., et al. 2003. J Biol Chem. 278: 9332-8. PMID: 12519763
2. Laminin alpha 3 LG4 module induces matrix metalloproteinase-1 through mitogen-activated protein kinase signaling.  |  Utani, A., et al. 2003. J Biol Chem. 278: 34483-90. PMID: 12826666
3. Essential and overlapping roles for laminin alpha chains in notochord and blood vessel formation.  |  Pollard, SM., et al. 2006. Dev Biol. 289: 64-76. PMID: 16321372
4. Multiple cell surface receptors for the short arms of laminin: alpha 1 beta 1 integrin and RGD-dependent proteins mediate cell attachment only to domains III in murine tumor laminin.  |  Goodman, SL., et al. 1991. J Cell Biol. 113: 931-41. PMID: 1827447
5. Processing of laminin α chains generates peptides involved in wound healing and host defense.  |  Senyürek, I., et al. 2014. J Innate Immun. 6: 467-84. PMID: 24458132
6. Bipartite mechanism for laminin-integrin interactions: Identification of the integrin-binding site in LG domains of the laminin α chain.  |  Taniguchi, Y., et al. 2020. Matrix Biol. 87: 66-76. PMID: 31669520
7. Identification of cell binding sites in the laminin alpha 1 chain carboxyl-terminal globular domain by systematic screening of synthetic peptides.  |  Nomizu, M., et al. 1995. J Biol Chem. 270: 20583-90. PMID: 7657636
8. The laminin alpha 1 chain Ile-Lys-Val-Ala-Val (IKVAV)-containing peptide promotes liver colonization by human colon cancer cells.  |  Bresalier, RS., et al. 1995. Cancer Res. 55: 2476-80. PMID: 7758002
9. Structural and functional analysis of the globular domain IVa of the laminin alpha 1 chain and its impact on an adjacent RGD site.  |  Schulze, B., et al. 1996. Biochem J. 314 (Pt 3): 847-51. PMID: 8615779
10. Differential expression of five laminin alpha (1-5) chains in developing and adult mouse kidney.  |  Sorokin, LM., et al. 1997. Dev Dyn. 210: 446-62. PMID: 9415429

The preferred Laminin α-1 antibody is Laminin α-1 Antibody (G-12): sc-74418.