CASP7 Research Reagents

Caspase-7 is a protein in humans that is encoded by CASP7 gene. Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death.

The following CASP7 reagents supplied by CUSABIO are manufactured under a strict quality control system. Multiple applications have been validated and solid technical support is offered.

CASP7 Antibodies

CASP7 Antibodies for Homo sapiens (Human)

CASP7 Proteins

CASP7 Proteins for Mus musculus (Mouse)

CASP7 Proteins for Homo sapiens (Human)

CASP7 Proteins for Mesocricetus auratus (Golden hamster)

CASP7 ELISA Kit

CASP7 ELISA Kit for Homo sapiens (Human)

CASP7 Background

Caspase-7, encoded by CASP7, is an executioner caspase [1] that carries out apoptosis by cleaving cellular components. Because of the structural similarity [2] and the conservation of the residues facing the catalytic site between caspase-3 and caspase-7, caspase-7 shows high similarities with caspase-3 in vitro substrate preference [3] and functions. Procaspase-7 is synthesized as a 303-amino acid inactive zymogen that resides in the cytosol as a pre-assembled homodimer [4]. Like other caspases, pro-caspase-7 must be proteolytically processed to be an active protease. The activation of the caspase-7 is stimulated by caspase-9 through proteolytic cleavage at specific internal aspartic acid residues to separate the large and small subunits of the mature caspase [5]. Alternatively, caspase-7 can be activated by caspase-8 through DNA-damage-induced mitochondrial cytochrome c leakage into the cytosol to complex with the adaptor protein Apaf-1 to form the apoptosome [6]. Upon activation, caspase-7 is responsible for the proteolytic degradation of the cellular targets, ultimately leading to apoptosis. Caspase-3 and caspase-7 exhibit almost indistinguishable activity toward certain synthetic peptide substrates, which often makes people believe that these two proteases occupy functionally redundant roles within the cell death machinery. Nevertheless, extensive biochemical studies demonstrated that caspase-3 and caspase-7 perform different activities toward multiple protein substrates, with caspase-7 being more selective [7][8]. In addition to its activation during apoptosis, pro-caspase-7 is also processed to mature active caspase-7 in inflammatory conditions. Lamkanfi M et al. confirmed that caspase-7 is a direct substrate of caspase-1 with maturation occurring after the canonical activation sites Asp23 and Asp198 [9].

[1] Boatright KM, Salvesen GS. Mechanisms of caspase activation [J]. Curr Opin Cell Biol. 2003 Dec; 15(6):725-31.
[2] Fernandes-Alnemri T., Takahashi A., et al. Mch3, a novel human apoptotic cysteine protease highly related to CPP32 [J]. Cancer Res. 1995; 55: 6045-6052.
[3] Talanian RV, Quinlan C, et al. Substrate specificities of caspase family proteases [J]. J. Biol. Chem. 1997, 272: 9677-9682.
[4] Boatright KM, Renatus M, et al. A unified model for apical caspase activation [J]. Mol Cell. 2003 Feb; 11(2):529-41.
[5] Srinivasula S.M., Ahmad M., et al. Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization [J]. Mol. Cell. 1998; 1 (a): 949-957.
[6] Slee EA, et al. Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner [J]. J Cell Biol, 1999, 144:281-292.
[7] Slee EA, Adrain C, et al. Executioner caspase-3, -6, and -7 perform distinct, non-redundant roles during the demolition phase of apoptosis [J]. J Biol Chem. 2001 Mar 9; 276(10):7320-6.
[8] Walsh JG, Cullen SP, et al. Executioner caspase-3 and caspase-7 are functionally distinct proteases [J]. Proc Natl Acad Sci U S A. 2008 Sep 2; 105(35):12815-9.
[9] Lamkanfi M, Kanneganti TD, et al. Targeted peptide centric proteomics reveals caspase-7 as a substrate of the caspase-1 inflammasomes [J]. Mol Cell Proteomics. 2008 Dec; 7(12):2350-63.

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