|Application ||WB, IHC|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||32 34 28 38 KDa|
|Antigen Region||185-209 aa|
|Other Names||Caspase-7, CASP-7, Apoptotic protease Mch-3, CMH-1, ICE-like apoptotic protease 3, ICE-LAP3, Caspase-7 subunit p20, Caspase-7 subunit p11, CASP7, MCH3|
|Format||Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.|
|Function||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.|
|Tissue Location||Highly expressed in lung, skeletal muscle, liver, kidney, spleen and heart, and moderately in testis. No expression in the brain|
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Provided below are standard protocols that you may find useful for product applications.
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.
Fernandes-Alnemri T.,et al.Cancer Res. 55:6045-6052(1995).
Duan H.,et al.J. Biol. Chem. 271:1621-1625(1996).
Lippke J.A.,et al.J. Biol. Chem. 271:1825-1828(1996).
Juan T.S.-C.,et al.Genomics 40:86-93(1997).
Kalnine N.,et al.Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
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