The following CASP3 reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

CASP3 Antibodies

CASP3 Antibodies for Homo sapiens (Human)

CASP3 Antibodies for Arabidopsis thaliana (Mouse-ear cress)

CASP3 Proteins

CASP3 Proteins for Mus musculus (Mouse)

CASP3 Proteins for Homo sapiens (Human)

CASP3 Proteins for Xenopus laevis (African clawed frog)

CASP3 Proteins for Rattus norvegicus (Rat)

CASP3 Proteins for Bos taurus (Bovine)

CASP3 Proteins for Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)

CASP3 Proteins for Pan troglodytes (Chimpanzee)

CASP3 Proteins for Saimiri boliviensis boliviensis (Bolivian squirrel monkey)

CASP3 Proteins for Mesocricetus auratus (Golden hamster)

CASP3 Proteins for Felis catus (Cat) (Felis silvestris catus)

CASP3 Proteins for Sus scrofa (Pig)

CASP3 Proteins for Canis lupus familiaris (Dog) (Canis familiaris)

CASP3 Proteins for Oryctolagus cuniculus (Rabbit)


CASP3 ELISA Kit for Mus musculus (Mouse)

CASP3 ELISA Kit for Rattus norvegicus (Rat)

CASP3 ELISA Kit for Homo sapiens (Human)

CASP3 Background

The CASP3 encodes the caspase-3, one of the major executioner caspases [1] in the apoptotic signaling because of its role in coordinating the demolishment of cellular structures such as DNA fragmentation or membrane blebbing. Caspase-3 is produced as a zymogen in an inactive pro-form. Cleavage and activation of pro-caspase-3 are catalyzed by initiator caspases, caspase-8, and caspase-9 through an internal cleavage to separate the large and small subunits to generate the active caspase-3 heterodimer [2]. In the APAF-1/caspase-9 apoptosome-initiated caspase activation cascade, caspase-3 has been shown to mediate feedback processing on caspase-9 [3][4]. Once activated, caspase-3 cleaves Bcl-2 and Bcl-XL, which abolishes the anti-apoptotic function of these proteins and releases C-terminal fragments that are pro-apoptotic. The cleavage of ICAD (inhibitor of caspase-activated DNase) by caspase-3 prompts the release of active CAD, which cleaves DNA and promotes chromatin condensation [5]. Caspase-3 also cleaves and activates gelsolin, a protein that regulates actin dynamics. Activated gelsolin promotes both cytoplasmic and nuclear apoptosis [6]. Katelyn G. Ponder et al. proved an initial cleavage event at D9 is required to allow cleavage at D28 that causes the complete removal of the prodomain allowing for full caspase-3 activation [7].

[1] Boatright KM, Salvesen GS Mechanisms of caspase activation [J]. Curr Opin Cell Biol. 2003 Dec; 15(6):725-31.
[2] Zou, H., Henzel, et al. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3 [J]. Cell 90, 405-413 (1997).
[3] Slee EA, et al. Ordering the cytochrome c-initiated caspase cascade: Hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner [J]. J Cell Biol, 1999, 144:281-292.
[4] Srinivasula SM, Ahmad M, et al. Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization [J]. Mol Cell, 1998, 1:949-957.
[5] Enari, M. et al. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD [J]. Nature 391, 43-50 (1998).
[6] Cohen, G. M. Caspases: the executioners of apoptosis [J]. Biochem. J. 326(Pt 1), 1-16 (1997).
[7] Katelyn G. Ponder and Lawrence H. Boise The prodomain of caspase-3 regulates its own removal and caspase activation [J]. Cell Death Discovery volume 5, Article number: 56 (2019).

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