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

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

ALX-201-059

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Highly active caspase essential for apoptosis

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.

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Caspase-3 (human), (recombinant) (active) image — **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.

Product Details

Alternative Name	CPP32, Yama, Apopain
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).
Formulation	Lyophilized.
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).
Reconstitution	Reconstitute to 1U/µl in water.
Source	Produced in E. coli. Contains an N-terminal His-tag.
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.
UniProt ID	P42574

Handling & Storage

Handling	Avoid freeze/thaw cycles. After reconstitution, prepare aliquots and store at -80°C.
Long Term Storage	-80°C
Shipping	Dry Ice

Regulatory Status	RUO – Research Use Only

Development of caspase-3-selective activity-based probes for PET imaging of apoptosis: L. Lauwerys, et al.; EJNMMI Radiopharm. Chem. 9, 58 (2024), Abstract
Conjunctival epitheliopathy induced by topical exposure to bacterial peptidoglycan, muramyl dipeptide: M.P. Langford, et al.; Exp. Eye Res. 227, 109383 (2023), Abstract
Cardioprotective Effects of Oroxylum indicum Extract Against Doxorubicin and Cyclophosphamide-Induced Cardiotoxicity: S.R. Pondugula, et al.; Cardiovasc. Toxicol. 22, 67 (2022), Abstract
Characterization of circulating molecules and activities in plasma of patients after allogeneic and autologous intraoral bone grafting procedures: a prospective randomized controlled clinical trial in humans: Ö. Solakoğlu, et al.; BMC Oral Health 22, 24 (2022), Abstract
GSDMEa-mediated pyroptosis is bi-directionally regulated by caspase and required for effective bacterial clearance in teleost: H. Xu, et al.; Cell Death Dis. 13, 491 (2022), Abstract
Aptamer-based enrichment of TDP-43 from human cells and tissues with quantification by HPLC-MS/MS: P.D. Taylor, et al.; J. Neurosci. Methods 361, 109344 (2021), Abstract
Separase-triggered apoptosis enforces minimal length of mitosis: S. Hellmuth & O. Stemmann; Nature 580, 542 (2020), Application(s): In vitro cleavage assay, Abstract
Caspase-Activated Oligonucleotide Probe: L. Yang, et al.; Bioconjug. Chem. 31, 2172 (2020), Abstract
BAD sensitizes breast cancer cells to docetaxel with increased mitotic arrest and necroptosis: J. Mann, et al.; Sci. Rep. 10, 355 (2020), Abstract — Full Text
Caspase-mediated cleavage of IRE1 controls apoptotic cell commitment during endoplasmic reticulum stress: A. Shemorry, et al.; Elife 8, e47084 (2019), Abstract — Full Text