C266
Monoclonal Anti-μ-Calpain (Domain III) antibody produced in mouse
clone 9A4H8D3, ascites fluid, buffered aqueous solution
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About This Item
biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
9A4H8D3, monoclonal
form
buffered aqueous solution
mol wt
antigen 80 kDa
species reactivity
human, rat, pig, bovine
technique(s)
indirect immunofluorescence: 1:100
western blot: 1:2,000
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
Gene Information
human ... CAPN1(823)
rat ... Capn1(29153)
General description
Calpain-1 catalytic subunit is a protein encoded by the CAPN1 gene in humans. Calpains are calcium dependent proteases constituting a family of proteins. 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).
Specificity
Epitope mapping studies indicate the epitope is between amino acids 465-520 (domain III) of human μ-calpain. The antibody reacts specifically with μ-calpain. It does not cross-react with m-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
μ-calpain from bovine skeletal muscle.
Application
Monoclonal Anti-μ-Calpain (Domain III) antibody produced in mouse is suitable for indirect immunofluorescence at a dilution of 1:100 and western blotting at a dilution of 1:2,000.
Biochem/physiol Actions
Calpain is involved in calmodulin-independent pathway for the activation of calcineurin. Endogenous calpain I forms active calcineurin in the human heart by proteolysis of calcineurin A, which may lead to pathogenesis of myocardial disease. μ-calpain, on overexpression, may have relationship with intractable epilepsy as well as the clinicopathological characteristics. The activity of this protein is elevated in skeletal muscle from gastric cancer patients.
Physical form
Solution in phosphate buffered saline and contains 0.05% sodium azide.
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.
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Storage Class
10 - Combustible liquids
wgk_germany
nwg
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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S Ohno et al.
Cytogenetics and cell genetics, 53(4), 225-229 (1990-01-01)
Calcium dependent proteases (calpains, CAPNs, E.C.3.4.22.17) constitute a family of proteins which share a homologous cysteine-protease domain (large subunits, L1, L2, and L3) and an E-F hand Ca2(+)-binding domain (L1, L2, L3, and small subunit, S). We have mapped the
Jian-Chun Wang et al.
Clinical laboratory, 58(11-12), 1145-1152 (2013-01-08)
The calmodulin-independent pathway is thought to involve the activation of calcineurin by calpain. However, the effect of endogenous calpain on calcineurin in human heart is not well known. Proteolysis and activation of recombinant calcineurin by purified calpain isozymes I and
Zhan-hui Feng et al.
Seizure, 20(5), 395-401 (2011-02-15)
This study aims to investigate μ-calpain expression profiles in the anterior temporal neocortex in patients with intractable epilepsy, and to determine whether its pattern of expression is related to pathological changes seen in these patients. The study subjects consisted of
Ira J Smith et al.
Muscle & nerve, 43(3), 410-414 (2011-02-10)
The influence of cancer on skeletal muscle calpain expression and activity in humans is poorly understood. We tested the hypothesis that calpain activity is increased in skeletal muscle from gastric cancer patients with no or <5% weight loss. Muscle biopsies
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