F6682
Anti-Filamin antibody,Mouse monoclonal
clone PM6/317, purified from hybridoma cell culture
Product Name
Anti-Filamin antibody,Mouse monoclonal, clone PM6/317, purified from hybridoma cell culture
biological source
mouse
conjugate
unconjugated
antibody form
purified from hybridoma cell culture
antibody product type
primary antibodies
clone
PM6/317, monoclonal
form
buffered aqueous solution
mol wt
antigen ~190 kDa
species reactivity
human, monkey, hamster, bovine, canine
concentration
~1.0 mg/mL
technique(s)
indirect immunofluorescence: suitable
western blot (chemiluminescent): 0.5-1.0 μg/mL using whole extract of human Jurkat or HEK-293Tcells
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Quality Level
Gene Information
human ... FLNA(2316)
Application
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
Biochem/physiol Actions
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.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
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.
Immunogen
human platelet membranes
Physical form
Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.
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Storage Class
12 - Non Combustible Liquids
wgk
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
Regulatory Information
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Takanori Chiba et al.
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Yuta Yako et al.
Scientific reports, 8(1), 9639-9639 (2018-06-27)
Recent studies have revealed that newly emerging transformed cells are often eliminated from epithelia via cell competition with the surrounding normal epithelial cells. However, it remains unknown whether and how soluble factors are involved in this cancer preventive phenomenon. By
Jie Lu et al.
Human molecular genetics, 16(14), 1661-1675 (2007-05-19)
Filamin B (FLNB) is a cytoplasmic protein that regulates the cytoskeletal network by cross-linking actin, linking cell membrane to the cytoskeleton and regulating intracellular signaling pathways responsible for skeletal development (Stossel, T.P., Condeelis, J., Cooley, L., Hartwig, J.H., Noegel, A.
Structure and Organization of Actin Filaments
Cooper GM et al.
Cell (2000)
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