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Caspase-3 (human), (recombinant) (active)

ALX-201-059-U025 25 U 156.00 USD
ALX-201-059-U100 100 U 356.00 USD
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Product Specification

Alternative Name:CPP32, Yama, Apopain
Source:Produced in E. coli. Contains an N-terminal His-tag.
UniProt ID:P42574
Quality Control:Routinely tested for its ability to cleave the caspase-3 substrates Ac-DEVD-pNA (Prod. No. ALX-260-033) and Ac-DEVD-AFC (Prod. No. ALX-260-032).
Specific Activity:≥15,000 U/mg protein. One unit is defined as the amount of enzyme that cleaves 1nmol of the caspase substrate DEVD-pNA (Prod. No. ALX-260-033) per hour at 37°C in a reaction solution containing 50mM HEPES, pH 7.2, 50mM NaCl, 0.1% CHAPS, 10mM EDTA, 5% glycerol and 10mM DTT.
Application Notes:Useful in studying enzyme regulation, determining target substrate, screening caspase inhibitors, or as a positive control in caspase assays. We recommend using 1 unit per assay for analyzing caspase activity.
For a complete caspase-3 assay protocol, please refer to Caspase-3 Fluorometric or Colorimetric Assay Kits (Prod. No. ALX-850-216 or ALX-850-215).
Reconstitution:Reconstitute to 1U/µl with PBS containing 15% glycerol.
Shipping:Shipped on Dry Ice
Long Term Storage:-80°C
Handling:Avoid freeze/thaw cycles. After reconstitution, prepare aliquots and store at -80°C.
Scientific Background:Caspase-3 is a member of the interleukin-1β converting enzyme (ICE) family of cysteine proteases. It exists in cells as an inactive 32kDa proenzyme. During apoptosis procaspase-3 is processed at aspartate residues by self-proteolysis and/or cleavage by upstream caspases, such as caspase-6, caspase-8 and granzyme B. The processed form of caspase-3 consists of large (17kDa) and small (11kDa) subunits which associate to form the active enzyme. Active caspase-3 has been shown involved in the proteolysis of several important molecules, such as poly(ADP-ribose) polymerase (PARP), the sterol regulatory element binding proteins (SREBPs), focal adhesion kinase (FAK) and others.
Figure: Active human caspase was expressed in E. coli  and purified. The activity of recombinant caspase-3 was determined by cleaving AFC conjugates of DEVD. The cleavage activity was effectively inhibited by the corresponding peptide inhibitor as indicated. 
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Product Literature References

Abolishing Tau cleavage by caspases at Aspartate421 causes memory/synaptic plasticity deficits and pre-pathological Tau alterations: F. Biundo, et al.; Transl. Psychiatry 7, e1198 (2017), Abstract; Full Text
Protein kinase A activation by the anti-cancer drugs ABT-737 and thymoquinone is caspase-3-dependent and correlates with platelet inhibition and apoptosis: N. Rukoyatkina, et al.; Cell Death Dis. 8, e2898 (2017), Abstract; Full Text
BmATG5 and BmATG6 mediate apoptosis following autophagy induced by 20-hydroxyecdysone or starvation: K. Xie, et al.; Autophagy 12, 381 (2016), Abstract; Full Text
Avian reovirus-triggered apoptosis enhances both virus spread and the processing of the viral nonstructural muNS protein: J. Rodriguez-Grille, et al.; Virology 462, 49 (2014), Abstract;
Leukocyte protease binding to nucleic acids promotes nuclear localization and cleavage of nucleic acid binding proteins: M.P. Thomas, et al.; J. Immunol. 192, 5390 (2014), Abstract;
Structural order in Pannexin 1 cytoplasmic domains: G. Spagnol, et al.; Channels 8, 157 (2014), Abstract; Full Text
Differential apoptosis-related protein expression, mitochondrial properties, proteolytic enzyme activity, and DNA fragmentation between skeletal muscles: E.M. McMillan, et al.; Am. J. Physiol. Regul. Integr. Comp. Physiol. 300, R531 (2011), Abstract; Full Text

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