Anti-Filamin antibody,Mouse monoclonal

Filamin, also known as actin-binding protein, is a large flexible V-shaped actin cross-linking cytoplasmic protein present in vertebrates of both muscle and non-muscle cells. It has actin-binding domains at the ends of each arm. It is a polypeptide with molecular weight of approximately 250 kDa and forms dimers in solution. It has a large flexible actin cross-linking protein present in vertebrates in both the muscle and non-muscle cells. The name filamins refers to its filamentous colocalization with actin stress fibers. It has an actin binding domain and a homodimerization domain. Native form comprises of two subunits with one actin-binding site.

Monoclonal Anti-Filamin (mouse IgG1 isotype) is derived from the hybridoma PM6/317 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with human platelet membranes.

human platelet membranes

Monoclonal Anti-Filamin antibody is suitable for indirect immunofluorescence and western blot (chemiluminescent) at a concentration of 0.5-1.0μg/mL using whole extract of human Jurkat or HEK-293Tcells.

Monoclonal Anti-Filamin antibody produced in mouse has been used in:

• immunoblotting
• immunofluorescent staining
• immunoprecipitation

Filamin has been primarily identified from smooth muscle but it has also found in macrophages, neutrophils, platelets and other cell types. It is associated in regulation of the cytoskeletal network by cross-linking actin and linking cell membrane to the cytoskeleton. It is also linked in regulating intracellular signaling pathways, responsible for skeletal development. It binds to the ring zinc finger domain of tumor necrosis factor (TNF) and receptor-associated factor 2 (TRAF2). Filamin cross-links with actin and promotes its aggregation and gelation.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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