Caspase 3, Apoptosis-Related Cysteine Peptidase (CASP3) Protein

Name: Caspase 3, Apoptosis-Related Cysteine Peptidase (CASP3)

Synonyms: CC3, Lice, Yama, CPP32, Apopain, Caspase-3, A830040C14Rik, Cas3, Casp3, DECAY, Drosophila executioner caspase related to Apopain/Yama, caspase 3, DmelCG14902, CG14902, DRICE, ICE, DmelCG7788, CG7788, casp3, xcpp32, CASP3

Protein Type: Recombinant

Source: Escherichia Coli (E. coli)

Origin (Gene): Human

Application: Western Blotting (WB), ELISA, Functional Studies (Func)

Catalog no.: ABIN413123

Additional Information

Gene ID: 836

NCBI Acession: P42574

UniProt: P42574

Format: Lyophilized

Reconstitution: Reconstitute in PBS containing 15% glycerol.

Description: Caspase-3 (also know as CPP32, Yama and apopain) is a major member of the caspase-family of cysteine proteases. Caspase-3 exists in cells as an inactive 32 kDa proenzyme. During apoptosis procaspase-3 is processed at aspartate residues by self-proteolysis and/or cleavage by upstream caspases, such as caspase-6 (Mch2), caspase-8 (Flice) and grazyme B. The processed form of caspase-3 consists of large (17 kD) and small (11 kD) subunits which associate to form the active enzyme. The active caspase-3 has been shown involving in the proteolysis of several important molecules, such as poly (ADP-ribose) polymerase (PARP), the sterol regulatory element binding proteins (SREBPs), focal adhesion kinase (FAK), and others. The recombinant active human caspase-3 expressed in E. coli spontaneously undergoes autoprocessing to yield subunits characteristic of the native enzyme (Full length gene Accession No. NP_004337) . The active caspase-3 preferentially cleaves caspase-3 substrates (e.g., DEVD-AFC or DEVD-pNA) and is routinely tested at BioVision for its ability to enzymatically cleave these two substrates Ac-DEVD-pNA (Cat. #1008-200) or Ac-DEVD-AFC (1007-200).
Synonyms: Caspase-3, CASP-3, Apopain, Cysteine protease CPP32, CPP-32, Protein Yama, SREBP cleavage activity 1, SCA-1

Molecular Weight: large (17 kD) and small (11 kD) subunits

Synonyms: CC3, Lice, Yama, CPP32, Apopain, Caspase-3, A830040C14Rik, Cas3, Casp3, DECAY, Drosophila executioner caspase related to Apopain/Yama, caspase 3, DmelCG14902, CG14902, DRICE, ICE, DmelCG7788, CG7788, casp3, xcpp32, CASP3

Application Details

Application Notes: Active caspase-3 is useful in studying enzyme regulation, determining target substrates, screening caspase inhibitors, or as a positive control in caspase activity assays and Western blot analysis. For a complete caspase-3 assay protocol, please refer to BioVision’s Caspase-3/CPP32 Fluorometric or Colorimetric Assay Kits (Cat.#: K105 and K106).

Handling Advice: Centrifuge the vial prior to opening.

Buffer: Lyophilized powder

Storage: -70°C

Expiry Date: 12 months

Restrictions: For Research Use only

Publications

Product: Zelphati, Wang, Kitada et al.: "Intracellular delivery of proteins with a new lipid-mediated delivery system." in: The Journal of biological chemistry, Vol. 276, Issue 37, pp. 35103-10, 2001 (PubMed).

Basu, Lu, Sun et al.: "Proteolytic activation of protein kinase C-epsilon by caspase-mediated processing and transduction of antiapoptotic signals." in: The Journal of biological chemistry, Vol. 277, Issue 44, pp. 41850-6, 2002 (PubMed).

Zeigler, Doseff, Galloway et al.: "Presentation of nitric oxide regulates monocyte survival through effects on caspase-9 and caspase-3 activation." in: The Journal of biological chemistry, Vol. 278, Issue 15, pp. 12894-902, 2003 (PubMed).

Atkin, Farg, Turner et al.: "Induction of the unfolded protein response in familial amyotrophic lateral sclerosis and association of protein-disulfide isomerase with superoxide dismutase 1." in: The Journal of biological chemistry, Vol. 281, Issue 40, pp. 30152-65, 2006 (PubMed).

Wang, Pabla, Wang et al.: "Caspase-mediated cleavage of ATM during cisplatin-induced tubular cell apoptosis: inactivation of its kinase activity toward p53." in: American journal of physiology. Renal physiology, Vol. 291, Issue 6, pp. F1300-7, 2006 (PubMed).

Zhang, Lu, Campbell-Thompson et al.: "Alpha1-antitrypsin protects beta-cells from apoptosis." in: Diabetes, Vol. 56, Issue 5, pp. 1316-23, 2007 (PubMed).

Hasegawa, Yamada, Komiyama et al.: "A novel natural compound, a cycloanthranilylproline derivative (Fuligocandin B), sensitizes leukemia cells to apoptosis induced by tumor necrosis factor related apoptosis-inducing ligand (TRAIL) through 15-deoxy-Delta 12, 14 prostaglandin J2 production." in: Blood, Vol. 110, Issue 5, pp. 1664-74, 2007 (PubMed).

Schmidt, Paes, De Mazière et al.: "EGFL7 regulates the collective migration of endothelial cells by restricting their spatial distribution." in: Development (Cambridge, England), Vol. 134, Issue 16, pp. 2913-23, 2007 (PubMed).

Cen, Mao, Aronchik et al.: "DEVD-NucView488: a novel class of enzyme substrates for real-time detection of caspase-3 activity in live cells." in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology, Vol. 22, Issue 7, pp. 2243-52, 2008 (PubMed).

Chen, Xia, Fang et al.: "Caspase-10-mediated heat shock protein 90 beta cleavage promotes UVB irradiation-induced cell apoptosis." in: Molecular and cellular biology, Vol. 29, Issue 13, pp. 3657-64, 2009 (PubMed).

Duncan, Gao, Huang et al.: "Neisseria gonorrhoeae activates the proteinase cathepsin B to mediate the signaling activities of the NLRP3 and ASC-containing inflammasome." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 182, Issue 10, pp. 6460-9, 2009 (PubMed).

Choi, Feng, Yoon: "FKBP38 protects Bcl-2 from caspase-dependent degradation." in: The Journal of biological chemistry, Vol. 285, Issue 13, pp. 9770-9, 2010 (PubMed).

Chiou, Hodges, Hoa: "Suppression of growth arrest and DNA damage-inducible 45alpha expression confers resistance to sulindac and indomethacin-induced gastric mucosal injury." in: The Journal of pharmacology and experimental therapeutics, Vol. 334, Issue 3, pp. 693-702, 2010 (PubMed).

Murakami, Tolstykh, Bao et al.: "Mechanism of activation of PSI-7851 and its diastereoisomer PSI-7977." in: The Journal of biological chemistry, Vol. 285, Issue 45, pp. 34337-47, 2010 (PubMed).

Nakajima, Hammond, Rosales et al.: "Calpain, not caspase, is the causative protease for hypoxic damage in cultured monkey retinal cells." in: Investigative ophthalmology & visual science, Vol. 52, Issue 10, pp. 7059-67, 2011 (PubMed).