C268
Monoclonal Anti-m-Calpain (Domain III/IV) antibody produced in mouse
clone 107-82, ascites fluid
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About This Item
Empfohlene Produkte
Biologische Quelle
mouse
Qualitätsniveau
Konjugat
unconjugated
Antikörperform
ascites fluid
Antikörper-Produkttyp
primary antibodies
Klon
107-82, monoclonal
Mol-Gew.
antigen 80 kDa
Speziesreaktivität
pig, human, rat, bovine
Methode(n)
indirect immunofluorescence: 1:50
western blot: 1:500
Isotyp
IgG1
UniProt-Hinterlegungsnummer
Versandbedingung
dry ice
Lagertemp.
−20°C
Posttranslationale Modifikation Target
unmodified
Angaben zum Gen
human ... CAPN2(824)
rat ... Capn2(29154)
Allgemeine Beschreibung
Calpain-2 catalytic subunit is a protein encoded by the CAPN2 gene in humans. Calpains are calcium dependent proteases constituting a family of proteins that are involved in essential cellular functions mediated by calcium. They share a homologous cysteine-protease domain and an E-F hand Ca2+-binding domain. The calpain system consists of two ubiquitous forms of calpain (m-calpain and μ-calpain), a tissue specific calpain (n-calpain) and a calpain inhibitory protein (calpastatin).
Spezifität
Epitope mapping studies indicate the epitope is between amino acids 502-699 (domain III/IV) of human m-calpain. The antibody reacts specifically with m-calpain. It does not cross-react with μ-calpain, n-calpain, calmodulin or calpastatin. It is not recommended for immunoprecipitation. By immunoblotting, reactivity is observed with human platelets and erythrocytes, bovine platelets, heart and skeletal muscle and with rat myoblasts, kidney, liver and spleen. By immunofluorescence on pig LLC-PK1 cells, diffuse cytoplasmic staining is observed.
Immunogen
m-calpain from bovine skeletal muscle.
Anwendung
Monoclonal Anti-m-Calpain (Domain III/IV) antibody produced in mouse is suitable for indirect immunofluorescence at a dilution of 1:50 and for western blotting at a dilution of 1:500.
Biochem./physiol. Wirkung
Calpain plays an important role during cellular processes including cytoskeletal remodeling, apoptosis and survival. Calpain-2 over expression is significantly associated with platinum resistant tumours and in ovarian carcinomas may allow prognostic stratification of patients treated with surgery and platinum-based chemotherapy. Its over expression in basal-like or triple-negative disease is associated with adverse breast cancer-specific survival. m-calpain (calpain-2) is significantly associated with triple-negative and basal-like disease.
Physikalische Form
Solution containing 0.05% sodium azide.
Haftungsausschluss
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.
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Lagerklassenschlüssel
10 - Combustible liquids
WGK
nwg
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
Analysenzertifikate (COA)
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Four genes for the calpain family locate on four distinct human chromosomes.
Ohno S, Minoshima S, Kudoh J, Fukuyama R, Shimizu Y, Ohmi-Imajoh S, Shimizu N, Suzuki K.
Cytogenetics and Cell Genetics (1990)
S Imajoh et al.
Biochemistry, 27(21), 8122-8128 (1988-10-18)
A nearly full-length cDNA clone for the large subunit of high-Ca2+-requiring Ca2+-activated neutral protease (mCANP) from human tissues has been isolated. The deduced protein, determined for the first time as an mCANP, has essentially the same structural features as those
A Hata et al.
The Journal of biological chemistry, 264(11), 6404-6411 (1989-04-15)
Calcium-dependent protease (CANP, Calpain) is an intracellular protease involved in essential cellular functions mediated by calcium. To understand the mechanism regulating the expression of CANP at the transcriptional level, we isolated a human gene for the large subunit of mCANP
Monica Averna et al.
PloS one, 10(1), e0116738-e0116738 (2015-01-13)
Here we demonstrate that heat shock protein 90 (HSP90) interacts with calpain-1, but not with calpain-2, and forms a discrete complex in which the protease maintains its catalytic activity, although with a lower affinity for Ca2+. Equilibrium gel distribution experiments
Selective Calpain Inhibition Improves Functional and Histopathological Outcomes in a Canine Spinal Cord Injury Model.
Metwally, et al.
International Journal of Molecular Sciences, 23 (2022)
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