Caspase 3, Apoptosis-Related Cysteine Peptidase (CASP3) 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

Clonality: Monoclonal (31A1067)

Host: Mouse

Reactivity: Human, Mouse (Murine), Rat (Rattus)

Conjugate: Un-conjugated

Application: Immunohistochemistry (Frozen Sections) (IHC (fro)), Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))

Catalog no.: ABIN121218

Additional Information

Alternative name: Caspase-3

UniProt: P42574

Immunogen: Full-length human Caspase-3 protein

Cross-Reactivity: Human, Mouse (Murine), Rat (Rattus)

Isotype: IgG1

Clone: 31A1067

Description: Caspases are a family of cysteine proteases that are key mediators of programmed cell death or apoptosis (1). The precursor form of all caspases is composed of a prodomain, and large and small catalytic subunits. The active forms of caspases are generated by several stimuli including ligand-receptor interactions, growth factor deprivation and inhibitors of cellular functions. All known caspases require cleavage adjacent to aspartates to liberate one large and one small subunit, which associate into a2b2 tetramer to form the active enzyme. Gene for Caspase-3 also known as Yama, CPP32, and apopain codes for a 32-kDa protein (2-4). Caspase-3 cleaves the death substrate poly(ADP-ribose) polymerase (PARP) to a specific 85 kDa form observed during apoptosis and is inhibitable by the CrmA protein. Other Caspase-3 substrates include DNA-PK, actin, GAS2, and procaspase-6, etc. (5). Caspase-3 is activated by cleavage events at Asp-28/Ser-29 (between N-terminal pro-domain) and Asp-175/Ser-176 (between large and small subunits) to generate a large subunit of 17-kDa and a small subunit of 12-kDa (3). Alternate Names: CASP3, Yama protein, Apopain, CPP32, CPP-32, SCA-1, FocusOn51 , Caspase 3, Cysteine protease CPP32, CASP 3, SREBP cleavage activity 1.

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: Immunohistochemistry on frozen (ref.6) and paraffin embedded (ref.7) sections. Recommended Positive Control: Staurosporine (2 mM) treated HeLa, Jurkat, Raw, NIH3T3. Western blot: 2-3 ug/ml. Application Notes ABIN121218 detects both pro caspase-3 (~32 kDa) and the large subunit of the active/cleaved form (~14-21 kDa) of Caspase-3. The large subunit of the cleaved form may appear as one or two or even as a stack of bands depending on the presence or absence of the Caspase-3 pro- domain. Other applications not tested. Optimal dilutions are dependent on conditions and should be determined by the user. 1 / 3

Concentration: 0.5 mg/ml

Purification: Purified

Buffer: PBS containing 0.05 % BSA and 0.05 % sodium azide

Storage: Store the antibody undiluted at 2-8°C for one month or (in aliquots) at -20°C for longer. Avoid repeated freezing and thawing. Shelf Life: one year from despatch.

Research Area: Apoptosis/Necrosis, Autophagy

Restrictions: For Research Use only

Images

Western blot analysis for detection of Caspase-3 activation in HeLa cells. Cells were treated with 2 mM staurosporine for different time periods. Caspase-3 activation is determined by cleavage of pro-Caspase-3, which generates 17 and 12 kDa, larger and smaller catalytic subunit, respectively

Publications

Tewari, Quan, ORourke et al.: "Yama/CPP32 beta, a mammalian homolog of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase." in: Cell, Vol. 81, Issue 5, pp. 801-9, 1995 (PubMed).

Shi, Chen, MacDonald et al.: "Activation of an interleukin 1 converting enzyme-dependent apoptosis pathway by granzyme B." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 93, Issue 20, pp. 11002-7, 1996 (PubMed).

Cohen: "Caspases: the executioners of apoptosis." in: The Biochemical journal, Vol. 326 ( Pt 1), Issue 5693, pp. 1-16, 1997 (PubMed).