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

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Protein Name
(30), (9), (4), (1), (1), (1), (1), (1), (1), (1), (1)
Escherichia coli (E. coli)
(32), (11), (4), (3), (1)
Protein Type Recombinant
High Pressure Liquid Chromatography (HPLC), SDS-PAGE (SDS)
Pubmed 17 references available
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Quantity 5 μg
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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
Pathways Apoptosis, Caspase Cascade in Apoptosis
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. We recommend using 1 unit/assay for analyzing caspase activity. For a complete caspase-3 assay protocol, please refer to Caspase-3/CPP32 Fluorometric or Colorimetric Assay Kits.
Optimal working dilution should be determined by the investigator.

physical form description: Semi-Dry

Restrictions For Research Use only
Format Powder or Liquid
Reconstitution Reconstitute in PBS containing 15 % glycerol.
Handling Advice Centrifuge the vial prior to opening.
Storage -80 °C
Expiry Date 12 months
Supplier Images
Western Blotting (WB) image for Caspase 3, Apoptosis-Related Cysteine Peptidase (CASP3) Protein (ABIN413123) Caspase 3, Apoptosis-Related Cysteine Peptidase (CASP3) protein
Product cited in: Zhou, Li, Tian et al.: "Changes in phosphatidylinositol 3-kinase 55 kDa gamma expression and subcellular localization may be caspase 6 dependent in paraquat-induced SH-SY5Y apoptosis." in: Human & experimental toxicology, Vol. 33, Issue 7, pp. 761-71, 2015 (PubMed).

Xia, Yang, Bu et al.: "Differential regulation of c-Jun protein plays an instrumental role in chemoresistance of cancer cells." in: The Journal of biological chemistry, Vol. 288, Issue 27, pp. 19321-9, 2013 (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).

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).

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).

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).

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).

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).

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).

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).

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) ..." in: Blood, Vol. 110, Issue 5, pp. 1664-74, 2007 (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).

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).

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).

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).

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).

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).

Catalog No. ABIN413123
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