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.
Synonyme(s) :
IL-1β Converting Enzyme, ICE
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About This Item
Produits recommandés
Produit recombinant
expressed in E. coli
Niveau de qualité
Pureté
≥90% (SDS-PAGE)
Forme
liquid
Activité spécifique
≥25,000 units/mg protein
≥50,000 units/mL
Fabricant/nom de marque
Calbiochem®
Conditions de stockage
OK to freeze
avoid repeated freeze/thaw cycles
Conditions d'expédition
dry ice
Température de stockage
−70°C
Description générale
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.
Actions biochimiques/physiologiques
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.
Avertissement
Toxicity: Standard Handling (A)
Définition de l'unité
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.
Forme physique
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).
Autres remarques
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.
Informations légales
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 2
Certificats d'analyse (COA)
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Caspase-1 as a regulatory molecule of lipid metabolism
Lipids in Health and Disease, 19(1), 34-34 (2020)
Acid-dependent Interleukin-1 (IL-1) Cleavage Limits Available Pro-IL-1? for Caspase-1 Cleavage
The Journal of Biological Chemistry, 290(42), 25374-25381 (2015)
Role of Caspase-1 in the Pathogenesis of Inflammatory-Associated Chronic Noncommunicable Diseases
Journal of Inflammation Research, 13, 749-764 (2020)
Journal of the American Heart Association, 9(7), e014044-e014044 (2020-04-01)
Background Aortic aneurysms and dissections are highly lethal diseases for which an effective treatment strategy is critically needed to prevent disease progression. The nucleotide-binding oligomerization domain-like receptor pyrin domain containing 3 (NLRP3)-caspase-1 inflammasome cascade was recently shown to play an
Caspase-1 initiates apoptosis in the absence of gasdermin D
Nature Communications, 10(1), 2091-2091 (2019)
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