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Monoclonal Anti-Calpastatin antibody produced in mouse

clone 1F7E3D10, ascites fluid, buffered aqueous solution

MDL number:

Quality Level

biological source




antibody form

ascites fluid

antibody product type

primary antibodies


1F7E3D10, monoclonal


buffered aqueous solution

species reactivity

human, rat, bovine, pig


indirect immunofluorescence: 1:200
western blot: 1:5,000



UniProt accession no.

shipped in

dry ice

storage temp.


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.


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.


calpastatin from bovine skeletal muscle.


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.


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.

Storage Class Code

12 - Non Combustible Liquids



Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Certificate of Analysis

Certificate of Origin

Manting Du et al.
Food chemistry, 274, 743-749 (2018-10-31)
The objective of this study was to investigate the effect of phosphorylation on the sensitivity of μ-calpain to the inhibition induced by calpastatin. Purified μ-calpain was incubated with alkaline phosphatase (AP) or protein kinase A (PKA) to modulate the phosphorylation
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
H Persson et al.
Brain research, 611(2), 272-278 (1993-05-21)
The localization of the two Ca-activated extralysosomal proteases m-calpain and mu-calpain in the eye of the adult rabbit was examined by immunohistochemistry, using poly- and monoclonal antibodies against the corresponding rabbit antigens. Immunoreactivity against the two forms of calpains was
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
H Ma et al.
Journal of biochemistry, 113(5), 591-599 (1993-05-01)
Calpain requires Ca2+ for both proteolysis of its substrates and interaction with its endogenous inhibitor, calpastatin. The mechanism of inhibition of calpain by calpastatin has remained unsolved, although Nishimura and Goll [J. Biol. Chem. 266, 11842-11850 (1991)] reported that autolyzed

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