Caspase-3 (31A1067): MDB00015AB
| Catalog No. | MDB00015AB |
| Applications |
caspase-3 (31A1067) is recommended for detection of caspase-3 and full length procaspase-3 of rabbit, mouse, rat and human origin by Western Blotting (starting dilution 1:200, dilution range 1:100-1:1000), immunoprecipitation [1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)], immunofluores-cence (starting dilution 1:50, dilution range 1:50- 1:500), immunohistochem- istry (including paraffin-embedded sections) (starting dilution 1:50, dilution range 1:50-1:500) and solid phase ELISA (starting dilution 1:30, dilution range 1:30-1:3000). Suitable for use as control antibody for caspase-3 siRNA (h): sc-29237, caspase-3 siRNA (m): sc-29927, caspase-3 shRNA Plasmid (h): sc-29237-SH, caspase-3 shRNA Plasmid (m): sc-29927-SH, caspase-3 shRNA (h) Lentiviral Particles: sc-29237-V and caspase-3 shRNA (m) Lentiviral Particles: sc-29927-V. Molecular Weight of procaspase-3: 32 kDa. Molecular Weight of caspase-3 subunits: 11/17/20 kDa. Positive Controls: PC-3 cell lysate: sc-2220, HeLa whole cell lysate: sc-2200 or U-698-M whole cell lysate: MDB00015AB. |
Product Description
Caspase-3, also known as apopain, SCA-1, Yama and CPP32, is an aspartatespecific cysteine protease that belongs to the ICE subfamily of caspases. Caspase-3 is expressed in cells as an inactive precursor from which the p17 and p11 subunits of the mature caspase-3 are proteolytically generated during apoptosis. The caspase-3 precursor is first cleaved at Asp 175-Ser 176 to produce the p11 subunit and the p20 peptide. Subsequently, the p20 peptide is cleaved at Asp 28-Ser 29 to generate the mature p17 subunit. The active caspase-3 enzyme is a heterodimer composed of two p17 and two p11 subunits. At the onset of apoptosis, caspase-3 proteolytically cleaves PARP at a Asp 216-Gly 217 bond. During the execution of the apoptotic cascade, activated caspase-3 releases SREBP from the membrane of the ER in a proteolytic reaction that is distinct from their normal sterol-dependent activation. Caspase-3 cleaves and activates SREBPs between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Caspase-3 also cleaves and activates caspase-6, -7 and -9. The human caspase-3 gene encodes a cytoplasmic protein that is highly expressed in lung, spleen, heart, liver, kidney and cells of the immune system.
