P3988
20S Proteasome Fraction from rabbit
≥95% (SDS-PAGE), solution
Se connecterpour consulter vos tarifs contractuels et ceux de votre entreprise/organisme
About This Item
Produits recommandés
Source biologique
rabbit
Niveau de qualité
Pureté
≥95% (SDS-PAGE)
Forme
solution
Poids mol.
700 kDa
Numéro d'accès UniProt
Application(s)
cell analysis
Conditions d'expédition
dry ice
Température de stockage
−70°C
Informations sur le gène
rabbit ... PSMA1(100352563) , PSMB1(100343622)
Description générale
Manufactured for Sigma by Boston Biochem., Inc.
Application
20S proteasome fraction from rabbit has been used as a positive control to determine proteasome activity.
Actions biochimiques/physiologiques
Catalytic core of the 26S proteasome that degrades polyubiquitinated proteins.
Hydrolyzes various peptide substrates and proteins with broad specificity in a non-ATP dependent process.
Forme physique
Solution in 50 mM HEPES, pH 7.6, 150 mM sodium chloride, and 1 mM DTT, pH 7.6.
Code de la classe de stockage
10 - Combustible liquids
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (COA)
Recherchez un Certificats d'analyse (COA) en saisissant le numéro de lot du produit. Les numéros de lot figurent sur l'étiquette du produit après les mots "Lot" ou "Batch".
Déjà en possession de ce produit ?
Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.
R L Stein et al.
Biochemistry, 35(13), 3899-3908 (1996-04-02)
In this paper, we report kinetic studies for the chymotryptic activity of the 20S proteasome. Major observations include the following: (1) Reaction progress curves that are recorded at concentrations of Suc-Leu-Leu-Val-Tyr-AMC greater than about 40 microM are biphasic and characterized
Examination of `lipotoxicity? in skeletal muscle of high-fat fed and ob/ob mice
S.M. Turpin
The Journal of Physiology (2009)
R Hough et al.
The Journal of biological chemistry, 262(17), 8303-8313 (1987-06-15)
We have purified two high molecular weight proteases approximately 400-fold from rabbit reticulocyte lysate. Both enzymes hydrolyze 125I-alpha-casein and 4-methylcoumaryl-7-amide peptides with tyrosine, phenylalanine, or arginine at the P1 position. Both are inhibited by hemin, thiol reagents, chymostatin, and leupeptin.
S M Turpin et al.
The Journal of physiology, 587(Pt 7), 1593-1605 (2009-02-11)
Excess lipid accumulation resulting from an elevated supply of plasma fatty acids is linked to the pathogenesis of the metabolic syndrome and heart disease. The term 'lipotoxicity' was coined to describe how lipid accumulation leads to cellular dysfunction and death
Notre équipe de scientifiques dispose d'une expérience dans tous les secteurs de la recherche, notamment en sciences de la vie, science des matériaux, synthèse chimique, chromatographie, analyse et dans de nombreux autres domaines..
Contacter notre Service technique