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

Details for Product No. ABIN413123
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Protein Name
Synonyms
CC3, CG14902, Cas3, Casp 3, Casp3, Caspase-3, DECAY, Decay, Dmel\\CG14902, Drosophila executioner caspase related to Apopain/Yama, caspase 3, caspase-3, CG7788, DRICE, Dmel\\CG7788, DrICE, DrIce, Dric ... show more
CC3, CG14902, Cas3, Casp 3, Casp3, Caspase-3, DECAY, Decay, Dmel\\CG14902, Drosophila executioner caspase related to Apopain/Yama, caspase 3, caspase-3, CG7788, DRICE, Dmel\\CG7788, DrICE, DrIce, Drice, ICE, crice, drICE, drIce, drice, ice, A830040C14Rik, AC-3, Apopain, CPP32, Lice, Yama, mldy, CPP32B, SCA-1, xcpp32 show less
Origin
Human
(28), (13), (6), (1), (1), (1), (1), (1), (1)
Source
Escherichia coli (E. coli)
(33), (9), (7), (3), (1)
Protein Type Recombinant
Application
Western Blotting (WB), ELISA, Functional Studies (Func)
Pubmed 15 references available
Quantity 5 μg
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Catalog No. ABIN413123
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Alternative Name Caspase-3
Background 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 for its ability to enzymatically cleave these two substrates Ac-DEVD-pNA or Ac-DEVD-AFC (ABIN412342).
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
Gene ID 836
UniProt P42574
Research Area Apoptosis/Necrosis, Autophagy
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 Caspase-3/CPP32 Fluorometric or Colorimetric Assay Kits.
Restrictions For Research Use only
Format Lyophilized
Reconstitution Reconstitute in PBS containing 15 % glycerol.
Handling Advice Centrifuge the vial prior to opening.
Storage -80 °C
Expiry Date 12 months
Product cited in: 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).

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