Anti-Laminin 5 antibody [P3H9-2] - BSA and Azide free

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Laminin 5 also known as laminin-332 is a heterotrimeric glycoprotein composed of alpha-3 beta-3 and gamma-2 chains with a molecular mass of about 460 kDa. Laminin 5 is expressed in the basement membrane zone of epithelial tissues playing a significant role in tissue structure. This molecule is widely present in areas such as skin lungs and other epithelial cell surfaces facilitating cellular functions like adhesion migration and differentiation. Researchers often use laminin antibodies including those for laminin IHC to visualize this molecule in various tissue samples.

Biological function summary

Laminin 5 forms part of the integrin complexes that modulate interactions between cells and the extracellular matrix. It provides critical structural support and influences cell behavior within the tissue microenvironment. Laminin 5 participates in the anchoring of keratinocytes to the underlying basement membrane which is essential for skin integrity and maintenance. Its interaction with laminin receptors on the cell surface strengthens the cellular attachment impacting the overall integrity and mechanical resistance of tissues.

Pathways

Laminin 5 is integral to the hemidesmosome assembly pathway and the MAPK/ERK signaling pathway. These pathways involve its interactions with integrins such as alpha-6 beta-4 and other proteins like dystroglycan. Laminin molecules including laminin 5 influence the downstream signaling of MAPK/ERK which governs processes like cellular proliferation and differentiation. The linkage with integrin-mediated signaling pathways allows laminin 5 to participate actively in cell adhesion mechanisms and responses to extracellular matrix changes.

Associated diseases and disorders

Laminin 5 associates with junctional epidermolysis bullosa and cancer progression. Mutations in the genes encoding laminin 5 subunits lead to junctional epidermolysis bullosa a disorder marked by fragile skin and blister formations due to defective basement membrane anchoring. In cancer altered expression of laminin 5 facilitates tumor invasion and metastasis often involving interactions with matrix metalloproteinases (MMPs) and other extracellular matrix components. These connections underline the role of laminin 5 in pathological processes highlighting its potential as a therapeutic target.