Anti Dystonin (BPAG1/BP230) mAb (Clone 279)

Hemidesmosomes are adhesive structures between cells and the extracellular matrix. They play a role in anchoring intermediate fibers to the extracellular basement membrane. Structurally, hemidesmosomes occur in two forms: Type I and Type II. Type I hemidesmosomes develop in stratified epithelia such as the epidermis. Its main components include the intracellular linker proteins Plectin and BPAG1, the adhesion receptor integrin α6β4 and collagen type BP180/XVII. Type II hemidesmosomes occur in blood vessels, Schwann cells, and digestive tract epithelia as a simplified form of Type I hemidesmosomes, consisting only plectin and integrin α6β4. The hemidesmosomal adhesion receptor is normally associated with Laminin 5 in the basement membrane. Furthermore, Laminin 5 (of which Laminin gamma 2 is a subunit) is linked to collagen fibers in the dermis via type VII collagen. Genetic deletion of hemidesmosome-related proteins causes various forms of epidermolysis bullosa, highlighting their importance in promoting adhesion between the epidermis and the basement membrane.

BPAG1 is a 230-kDa cytoplasmic protein localized to hemidesmosomes of stratified epithelia and is one of the major antigenic proteins of bullous pemphigoid (BP), a chronic autoimmune skin disease. This anti-BPAG1 monoclonal antibody (clone 279) was raised against bovine BPAG1 and can be used in western blotting and immunofluorescent staining (IF) in multiple animal species, including humans and mice.

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