C270
Monoclonal Anti-Calpastatin antibody produced in mouse
clone 1F7E3D10, ascites fluid, buffered aqueous solution
Synonym(s):
Anti-BS-17, Anti-PLACK
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About This Item
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biological source
mouse
Quality Level
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
1F7E3D10, monoclonal
form
buffered aqueous solution
species reactivity
human, rat, bovine, pig
technique(s)
indirect immunofluorescence: 1:200
western blot: 1:5,000
isotype
IgG1
UniProt accession no.
shipped in
dry ice
storage temp.
−20°C
target post-translational modification
unmodified
Gene Information
human ... CAST(831)
rat ... Cast(25403)
General description
Calpastatin is a protein encoded by the CAST gene in humans. Calpastatin is an endogenous inhibitor of the ubiquitous calcium dependent proteinases μ- and m-calpain. It plays a key role in many cellular physiological and pathological processes. Calpastatin level is very important for controlling calpain activity.
Specificity
Epitope mapping studies indicate the epitope is between amino acids 543-673 (domain IV) of human calpastatin. By immunoblotting, the antibody may detect bands at 150, 125, 90 and 70 kDa, which have been suggested to be proteins translated from different start sites of the calpastatin gene. It does not cross-react with calpains or calmodulin. By immunoblotting, reactivity is observed with human platelets and erythrocytes, bovine platelets, heart and skeletal muscle and in rat myoblasts, kidney, liver and spleen. By immunofluorescence on pig LLC-PK1 cells, diffuse cytoplasmic staining is observed.
Immunogen
calpastatin from bovine skeletal muscle.
Application
Monoclonal Anti-Calpastatin antibody produced in mouse is suitable for indirect immunofluorescence at a dilution of 1:200 and for western blotting at a dilution of 1:5,000.
Biochem/physiol Actions
Calpastatin availability in cytosol is controlled by Ca2+ and cyclic AMP. Prolonged calpain activation promotes degradation of calpastatin. Calpastatin is found to be overexpressed in mycoplasma-contaminated cultured cells. CAST gene is found to be involved in genetic susceptibility to Keratoconus (KC), a genetically heterogeneous corneal dystrophy. It is also found to be associated with Parkinson′s disease (PD) and single nucleotide polymorphisms (SNPs).
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 Code
10 - Combustible liquids
WGK
nwg
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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Lan Zhang et al.
PloS one, 8(8), e70935-e70935 (2013-08-21)
Recent studies point to an association between the late-onset sporadic Parkinson's disease (PD) and single nucleotide polymorphisms (SNPs) rs1559085 and rs27852 in Ca(2+)-dependent protease calpain inhibitor calpastatin (CAST) gene. This finding is of interest since loss of CAST activity could
M Averna et al.
Cellular and molecular life sciences : CMLS, 60(12), 2669-2678 (2003-12-20)
The amount of calpastatin directly available in cytosol is under the control of [Ca2+] and [cyclic AMP]. Prolonged calpain activation also promotes degradation of calpastatin. The fluctuation of calpastatin concentration in cell soluble fraction is accompanied by an initial decrease
Maryam Niapour et al.
The Journal of biological chemistry, 283(31), 21371-21381 (2008-06-12)
The c-Myc transcription factor is commonly dysregulated in cancer. c-Myc also sensitizes cells to apoptosis induced by a variety of toxic events. c-Myc turnover is rapid and mediated by the proteasome and intracellular calpains. Therefore, c-Myc accumulation could contribute to
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
Xiaohui Li et al.
Cornea, 32(5), 696-701 (2013-03-02)
Keratoconus (KC) is a genetically heterogeneous corneal dystrophy. Previously, we performed 2 genome-wide linkage scans in a 4-generation autosomal dominant pedigree and repeatedly mapped a KC locus to a genomic region located on chromosome 5q overlapping the gene encoding the
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