Product Details
| abID | ab52173 |
|---|---|
| Alternate Name | Caspase-7, CASP-7, Apoptotic protease Mch-3, CMH-1, ICE-like apoptotic protease 3 |
| Gene Symbol | CASP7 |
| Gene ID | 840 |
| Accession # | P55210 |
| Source | E. coli. |
| Appearance | Lyophilized powder |
| Physical Form Description | Lyophilized powder |
| Purity by SDS-PAGE | ≥90% |
| Reconstitution Instructions | Reconstitute to 1 unit per µl in water. |
| Handling | Centrifuge the vial prior to opening. |
| Storage Conditions | -70°C |
| Shipping Conditions | Gel Pack |
| USAGE | For Research Use Only! Not to be used in humans |
Details
Caspase-7 (also know as Mch3, ICE-LAP3, CMH-1) is a member of the caspase-family of cysteine proteases. Similar to other caspases, caspase-7 also exists in cells as an inactive proenzyme. During apoptosis procaspase-7 is processed at aspartate residues by self-proteolysis and/or cleavage by another caspase. The processed active form of caspase-7 consists of large and small subunits which associate to form the active enzyme. Active caspase-7 has been shown involving in the proteolysis of PARP (poly ADP-ribose polymerase), an enzyme that is involved in DNA repair and genomic maintenance. The recombinant active human caspase-7 was expressed in E. coli. The active caspase-7 is routinely tested at BioVision for its ability to enzymatically cleave these two substrates Ac-DEVD-pNA (Cat. #1008-200) or Ac-DEVD-AFC (1007-200).
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Shresh Pathak, Autoimmune inner ear disease patient–associated 28-kDa proinflammatory IL-1β fragment results from caspase-7–mediated cleavage in vitro. JCI Insight., Feb. 2020; 32051334.
Zhou et al., Changes in phosphatidylinositol 3-kinase 55 kDa gamma expression and subcellular localization may be caspase 6 dependent in paraquat-induced SH-SY5Y apoptosis. Human and Experimental Toxicology, Jul 2014; 33: 761 - 771.
Xia et al., Differential Regulation of c-Jun Protein Plays an Instrumental Role in Chemoresistance of Cancer Cells. J. Biol. Chem., Jul 2013; 288: 19321 - 19329.
Murakami, E. et. al. Mechanism of Activation of PSI-7851 and Its Diastereoisomer PSI-7977. J. Biol. Chem., Nov 2010; 285: 34337 - 34347.
Cheng F. et. al. The Capsid Proteins of Aleutian Mink Disease Virus Activate Caspases and Are Specifically Cleaved during Infection J. Virol., Mar 2010; 84: 2687 - 2696.
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