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Caspase-7/MCH3  Protein, Antibody, ELISA Kit, cDNA Clone

Expression host: E. coli  
20 µg 
10 µg 
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Caspase-7/MCH3 Related Area

Caspase-7/MCH3 Summary & Protein Information

Caspase-7/MCH3 Background

Gene Summary: This CASP7 gene encodes a member of the cysteine-aspartic acid protease (caspase) family. Sequential activation of caspases plays a central role in the execution-phase of cell apoptosis. Caspases exist as inactive proenzymes which undergo proteolytic processing at conserved aspartic residues to produce two subunits, large and small, that dimerize to form the active enzyme. The precursor of caspase 7 is cleaved by caspase 3 and 10, is activated upon cell death stimuli and induces apoptosis. Alternatively spliced transcript variants encoding multiple isoforms have been observed for this gene. [provided by RefSeq, May 2012]
General information above from NCBI
Catalytic activity: Strict requirement for an Asp residue at position P1 and has a preferred cleavage sequence of Asp-Glu-Val-Asp-|-.
Enzyme regulation: ENZYME REGULATION: Inhibited by isatin sulfonamides.
Subunit structure: Heterotetramer that consists of two anti-parallel arranged heterodimers, each one formed by a 20 kDa (p20) and a 11 kDa (p11) subunit. Interacts with BIRC6/bruce. {ECO:0000269|PubMed:11701129, ECO:0000269|PubMed:15200957}.
Subcellular location: Cytoplasm.
Tissue specificity: Highly expressed in lung, skeletal muscle, liver, kidney, spleen and heart, and moderately in testis. No expression in the brain.
Post-translational: Cleavages by granzyme B or caspase-10 generate the two active subunits. Propeptide domains can also be cleaved efficiently by caspase-3. Active heterodimers between the small subunit of caspase-7 and the large subunit of caspase-3, and vice versa, also occur. {ECO:0000269|PubMed:8755496}.
Sequence similarity: Belongs to the peptidase C14A family. {ECO:0000305}.
General information above from UniProt

Caspase 7, also known as caspase-7 and MCH3, belongs to the cysteine-aspartic acid protease (caspase) family. Caspases play a role in the signal transduction pathways of apoptosis, necrosis and inflammation. There are two major classes of caspases: initiators and effectors. The initiator isoforms (caspases-1,-4,-5,-8,-9,-10,-11,-12) are activated by, and interact with, upstream adaptor molecules through protein-protein interaction domains known as CARD and DED. Effector caspases (-3,-6,-7) are responsible for cleaving downstream substrates and are sometimes referred to as the executioner caspases. Caspase 7 exists in lung, skeletal muscle, liver, kidney, spleen and heart, and moderately in testis. Caspase 7 cannot be detected in the brain. Caspase 7 functions in the activation cascade of caspases responsible for apoptosis execution. It cleaves and activates sterol regulatory element binding proteins (SREBPs). It proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp- -Gly-217' bond. Overexpression promotes programmed cell death.

Caspase-7/MCH3 Alternative Name

MCH3,CMH-1,LICE2,CASP-7,ICE-LAP3, [homo-sapiens]
apoptosis-related cysteine protease,apoptotic protease MCH-3,CASP-7,caspase 7,caspase 7 isoform delta,CMH-1,ICE-LAP3,ICE-like apoptotic protease 3,Lice2 alpha/beta/gamma,MCH3,RP11-211N11.6, [human]
AI314680,apoptotic protease Mch-3,CASP-7,caspase-7,CMH-1,cysteine protease LICE2,ICE-IAP3,mCASP-7,Mch3, [mouse]
Mch3,CMH-1,mCASP-7,AI314680,ICE-IAP3,caspase-7, [mus-musculus]

Caspase-7/MCH3 Related Studies

  • Riedl S J, et al. (2001) Structural basis for the inhibition of caspase-3 by XIAP. Cell. 104(5):791-800.
  • Roy N, et al. (1997) The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. EMBO J. 16(23):6914-25.
  • Deveraux Q L, et al. (1997) X-linked IAP is a direct inhibitor of cell-death proteases. Nature. 388(6639): 300-4.