Quick Order

Home>CASP7
Text Size:AAA

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

Expression host: E. coli  
10049-H08E-20
10049-H08E-10
20 µg 
10 µg 
Add to Cart
  • Slide 1

Caspase-7/MCH3 Related Area

Caspase-7/MCH3 Related Protein, Antibody, cDNA Gene, and ELISA Kits

Caspase-7/MCH3 Related Protein, Antibody, cDNA Gene, and ELISA Kits

Featured Reagent Products

Caspase-7/MCH3 Summary & Protein Information

Caspase-7/MCH3 Background

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]
LICE2, [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.
  • Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"