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Caspase 1, Apoptosis-Related Cysteine Peptidase (Interleukin 1, Beta, Convertase) (CASP1) (Active) Protein
|Synonyms||ICE, P45, IL1BC, Il1bc, Ice, DCP-1, DCP1, l(2)01862, l(2)02132, DmelCG5370, CG5370, CASP1, LOC100033888|
Escherichia Coli (E. coli)
Western Blotting (WB), ELISA, Functional Studies (Func)
|7 references available|
|Price||192.50 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 2 to 3 Business Days|
|Reconstitution||Reconstitute to 1 unit per µL in PBS containing 15% glycerol.|
Caspase-1 (also know as ICE) is a prototypical member of the caspase-family of cysteine proteases. Caspase-1 exists in cells as an inactive 45 kDa proenzyme. The pro-enzyme is matured by proteolysis to yield large (20 kD) and small (10 kD) subunits. The active caspase-1 is a heterotetramer consisting of two large and two small subunits. To date the regulatory mechanism of caspase-1 activation and the role of caspase-1 in apoptosis are poorly understood. In THP-1 cells, a large proportion of the caspase-1 is present in the inactive proenzyme form. The recombinant active human caspase-1 was expressed in E. coli. The active caspase-1 preferentially cleaves caspase-1 substrates (e.g., YVAD-AFC or YVAD-pNA) and is routinely tested at BioVision for its ability to enzymatically cleave these two substrates Ac-YVAD-pNA (Cat. #1104-200) or Ac-YVAD-AFC (1103-200). The rh-Caspase has an N-term His-tag and corresponds to amino acids 120-404 of Caspase-1, gene accession# NP_150634.1.
Synonyms: Caspase-1, CASP-1, Interleukin-1 beta convertase, IL-1BC, IL-1 beta-converting enzyme, p45
|Characteristics||Biological activity: > 5000 units/mg One unit of the recombinant caspase-1 is the enzyme activity that cleaves 1 nmol of the caspase substrate YVAD-pNA (pNA: pnitroanaline) per hour at 37°C in a reaction solution containing 50 mM Hepes, pH 7.2, 50 mM NaCl, 0.1% Chaps, 10 mM EDTA, 5% Glycerol, and 10 mM DTT.|
|Molecular Weight||large (20 kD) and small (10 kD) subunits|
|Application Notes||Active caspase-1 is useful in studying enzyme regulation, determining target substrates, screening caspase inhibitors, or as a positive control in caspase activity assays. We recommend using 1 unit/assay for analyzing caspase activity. For a complete caspase-1 assay protocol, please refer to BioVision’s Caspase-1 Fluorometric or Colorimetric Assay Kits (Cat.#: K110 and K111).|
|Handling Advice||Centrifuge the vial prior to opening.|
|Expiry Date||12 months|
|Restrictions||For Research Use only|
Hasegawa, Yamada, Komiyama et al.: "A novel natural compound, a cycloanthranilylproline derivative (Fuligocandin B), sensitizes leukemia cells to apoptosis induced by tumor necrosis factor related apoptosis-inducing ligand (TRAIL) through 15-deoxy-Delta 12, 14 prostaglandin J2 production." in: Blood, Vol. 110, Issue 5, pp. 1664-74, 2007 (PubMed).
Chen, Xia, Fang et al.: "Caspase-10-mediated heat shock protein 90 beta cleavage promotes UVB irradiation-induced cell apoptosis." in: Molecular and cellular biology, Vol. 29, Issue 13, pp. 3657-64, 2009 (PubMed).
Duncan, Gao, Huang et al.: "Neisseria gonorrhoeae activates the proteinase cathepsin B to mediate the signaling activities of the NLRP3 and ASC-containing inflammasome." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 182, Issue 10, pp. 6460-9, 2009 (PubMed).
Cheng, Chen, Best et al.: "The capsid proteins of Aleutian mink disease virus activate caspases and are specifically cleaved during infection." in: Journal of virology, Vol. 84, Issue 6, pp. 2687-96, 2010 (PubMed).
Murakami, Tolstykh, Bao et al.: "Mechanism of activation of PSI-7851 and its diastereoisomer PSI-7977." in: The Journal of biological chemistry, Vol. 285, Issue 45, pp. 34337-47, 2010 (PubMed).
Lamkanfi, Sarkar, Vande Walle et al.: "Inflammasome-dependent release of the alarmin HMGB1 in endotoxemia." in: Journal of immunology (Baltimore, Md. : 1950), Vol. 185, Issue 7, pp. 4385-92, 2010 (PubMed).
Oh, Kim, Jeong: "Distinct effects of imperatorin on allergic rhinitis: imperatorin inhibits caspase-1 activity in vivo and in vitro." in: The Journal of pharmacology and experimental therapeutics, Vol. 339, Issue 1, pp. 72-81, 2011 (PubMed).
|Hosts||Escherichia Coli (E. coli) (23), Yeast (3), Bacteria (1)|
|Reactivities||Human (14), Mouse (Murine) (6), Rat (Rattus) (4), Pig (Porcine) (3), Wild boar (Sus scrofa) (3)|