218783
Caspase-1, Human, Recombinant, E. coli
Caspase-1, Human, Recombinant, is expressed in E. coli and is fused at the N-terminus to a His•Tag sequence.
Synonym(s):
IL-1β Converting Enzyme, ICE
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About This Item
UNSPSC Code:
12352202
NACRES:
NA.77
Recommended Products
recombinant
expressed in E. coli
Quality Level
assay
≥90% (SDS-PAGE)
form
liquid
specific activity
≥25,000 units/mg protein
≥50,000 units/mL
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
avoid repeated freeze/thaw cycles
shipped in
dry ice
storage temp.
−70°C
General description
Research area: APOPTOSIS
Caspases are enzymes that belong to the cysteine protease family. In mammals, researchers have discovered 13 caspases. They enhance chemical reactions by targeting specific substances, guided by aspartic acid. These caspases can be further classified into two groups: apoptotic caspases (caspase-2, 3, 6, 7, 8, 9, and 10) and inflammatory caspases (caspase-1, 4, 5, 11, and 12). Apart from inflammatory organs such as the spleen, lymph nodes, and thymus, caspase-1 is also expressed in adipose tissue, liver, and intestine. Recombinant, human caspase-1 fused at the N-terminus to a His•Tag sequence and expressed in E. coli. Useful for the study of enzyme regulation, cleavage of target substrates, and inhibitor screening. M.W. 10000 and 20000.
Caspases are enzymes that belong to the cysteine protease family. In mammals, researchers have discovered 13 caspases. They enhance chemical reactions by targeting specific substances, guided by aspartic acid. These caspases can be further classified into two groups: apoptotic caspases (caspase-2, 3, 6, 7, 8, 9, and 10) and inflammatory caspases (caspase-1, 4, 5, 11, and 12). Apart from inflammatory organs such as the spleen, lymph nodes, and thymus, caspase-1 is also expressed in adipose tissue, liver, and intestine. Recombinant, human caspase-1 fused at the N-terminus to a His•Tag sequence and expressed in E. coli. Useful for the study of enzyme regulation, cleavage of target substrates, and inhibitor screening. M.W. 10000 and 20000.
Application
Caspase-1 enzyme has been used in mediating the proteolysis of pro-IL-1β for regulating the availability and activation of IL-1β.
Biochem/physiol Actions
Caspases belong to the cysteine proteases family of enzymes that are responsible for regulating apoptosis and pyroptosis, a programmed necrosis. The activation of caspase-1 in inflammasomes initiates an inflammatory response for fighting infections or cellular damage. Furthermore, caspase-1 activated interleukin-1 beta (IL-1β) and interleukin-18 (IL-18) are related to various metabolic disorders such as obesity, atherosclerosis, impairment of insulin action and/or secretion, cancer, and nonalcoholic fatty liver disease. Caspase-1 deficiency could play a role in promoting the growth of tumor cells in colon, ovarian, and prostate cancers.
Warning
Toxicity: Standard Handling (A)
Unit Definition
One unit is defined as the amount of enzyme that will cleave 1.0 pmol Ac-YVAD-pNA (Cat. No. 400025) per min at 30°C, pH 7.4.
Physical form
In 100 mM NaCl, 50 mM HEPES, 10 mM DTT, 1 mM EDTA, 10% glycerol, 0.5% CHAPS, pH 7.4.
Reconstitution
Following initial thaw, aliquot and freeze (-70°C).
Other Notes
Thornberry, N.A. 1994. Methods Enzymol. 244, 615.
Thornberry, N.A., et al. 1992. Nature 356, 768.
Thornberry, N.A., et al. 1992. Nature 356, 768.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
wgk_germany
WGK 2
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