Caspase 3, Apoptosis-Related Cysteine Peptidase (CASP3) (AA 1-219) antibody

Antigen: 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

Binding Site: AA 1-219

Clonality: Monoclonal (19)

Host: Mouse

Reactivity: Human

Conjugate: Un-conjugated

Application: Western Blotting (WB), Immunoprecipitation (IP), Fluorescence Microscopy (FM)

Catalog no.: ABIN967902

Additional Information

Alternative name: Caspase-3

Immunogen: Human CPP32

Format: Liquid

Isotype: IgG2a

Clone: 19

Description: Apoptosis, a selective process of genetically programmed cell death, occurs during normal cellular differentiation and development of multicellular organisms. Apoptotic cells are characterized by loss of cell volume, plasma membrane blebbing, nuclear condensation, chromatin aggregation, and endonucleocytic degradation of DNA into nucleosomal fragments. Caspase-3 (CPP32, Yama, apopain) is a member of the family of cysteine proteases which includes interleukin-1beta converting enzyme (ICE) and C. elegans protein, Ced-3. An apoptotic signal such as granzyme B of cytotoxic T-cells (CTLs) or ICE-like proteases induces the intracellular cleavage of Caspase-3 from the inactive pro-form (32 kDa) to the active form which consists of the p20, p17, and p12 subunits. The active form of Caspase-3 cleaves several other apoptotic proteins including proteins such as DNA Fragmentation Factor (DFF). Apoptosis can be inhibited by coexpression of Bcl-2 as well as inhibitors of Caspase-3 or other members of the family of cysteine proteases. This antibody recognizes the human pro-form (inactive) of Caspase-3 at 32 kDa. In addition, it has been reported to recognize the active form of Caspase-3 at 20-21 kD in apoptotic cell lysates.
Synonyms: CPP32

Characteristics: 1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2. Source of all serum proteins is from USDA inspected abattoirs located in the United States.
3. Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
4. Please refer to us for technical protocols.

Molecular Weight: 32 kDa

Comments:

Related Products: ABIN968537, ABIN967389, ABIN967299

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

Concentration: 250 µg/ml

Purity: Purified

Purification: Purified from tissue culture supernatant or ascites by affinity chromatography.

Buffer: Aqueous buffered solution containing BSA, glycerol.

Preservative: 0.09% Sodium azide.

Storage: Store undiluted at -20°C.

Research Area: Apoptosis/Necrosis, Autophagy

Restrictions: For Research Use only

Images

Western blot analysis of Caspase-3 on a Jurkat cell lysate (Human T-cell leukemia, ATCC TIB-152) . Lane 1: 1:1000, lane 2: 1:2000, lane 3: 1:4000 dilution of the mouse anti-human Caspase-3 antibody.

Publications

Product: Fernandes-Alnemri, Litwack, Alnemri: "CPP32, a novel human apoptotic protein with homology to Caenorhabditis elegans cell death protein Ced-3 and mammalian interleukin-1 beta-converting enzyme." in: The Journal of biological chemistry, Vol. 269, Issue 49, pp. 30761-4, 1995 (PubMed).

Scaffidi, Fulda, Srinivasan et al.: "Two CD95 (APO-1/Fas) signaling pathways." in: The EMBO journal, Vol. 17, Issue 6, pp. 1675-87, 1998 (PubMed).

Donoghue, Baden, Lauder et al.: "Immunohistochemical localization of caspase-3 correlates with clinical outcome in B-cell diffuse large-cell lymphoma." in: Cancer research, Vol. 59, Issue 20, pp. 5386-91, 1999 (PubMed).

Li, Chen, Sinogeeva et al.: "Arsenic trioxide promotes histone H3 phosphoacetylation at the chromatin of CASPASE-10 in acute promyelocytic leukemia cells." in: The Journal of biological chemistry, Vol. 277, Issue 51, pp. 49504-10, 2002 (PubMed).

Takemoto, Nagai, Miyawaki et al.: "Spatio-temporal activation of caspase revealed by indicator that is insensitive to environmental effects." in: The Journal of cell biology, Vol. 160, Issue 2, pp. 235-43, 2003 (PubMed).