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Documenti

14-856

Sigma-Aldrich

Ubiquitin C-terminal hydrolase L3 (UCH-L3), 50 µg

From human cDNA, expressed in E. coli. Ubiquitin C-terminal hydrolases are a family of cysteine hydrolases that catalyze the hydrolysis of amides, esters & thioesters of the C-terminus of ubiquitin.

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About This Item

Codice UNSPSC:
12352200
eCl@ss:
32160405
NACRES:
NA.32

Origine biologica

human

Livello qualitativo

Ricombinante

expressed in E. coli

Attività specifica

>1000 pmol/min-μg, 25 °C (with 1 μM ubiquitin-AMC as substrate and UCH-L3 at 20 pM (0.58 ng/mL).)

PM

Mw 26.2 kDa

Produttore/marchio commerciale

Upstate®

N° accesso NCBI

N° accesso UniProt

Condizioni di spedizione

dry ice

Descrizione generale

Produced from human cDNA, expressed in E. coli. Ubiquitin C-terminal hydrolases (UCHs) are a family of cysteine hydrolases that catalyze the hydrolysis of amides, esters and thioesters of the C-terminus of ubiquitin. UCH-L3 is a member of the lower molecular weight group of UCHs involved in the hydrolysis of small C-terminal derivatives of ubiquitin that form non-specifically during the process of protein ubiquitinylation.
Product Source: Recombinant human UCH-L3 expressed in E.coli.

Applicazioni

From human cDNA, expressed in E. coli. Ubiquitin C-terminal hydrolases are a family of cysteine hydrolases that catalyze the hydrolysis of amides, esters & thioesters of the C-terminus of ubiquitin.

Stoccaggio e stabilità

Store at -70°C for up to 12 months from date of receipt. As supplied, the enzyme is stable on ice for several hours. Activity is stable up to 6 freeze/thaw cycles (snap freezing in a dry/ice ethanol bath or liquid nitrogen).

Note legali

UPSTATE is a registered trademark of Merck KGaA, Darmstadt, Germany

Esclusione di responsabilità

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

Codice della classe di stoccaggio

12 - Non Combustible Liquids

Classe di pericolosità dell'acqua (WGK)

WGK 1

Punto d’infiammabilità (°F)

Not applicable

Punto d’infiammabilità (°C)

Not applicable


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K D Wilkinson et al.
Journal of molecular biology, 291(5), 1067-1077 (1999-10-16)
The ubiquitin fold is a versatile and widely used targeting signal that is added post-translationally to a variety of proteins. Covalent attachment of one or more ubiquitin domains results in localization of the target protein to the proteasome, the nucleus
Roles of ubiquitinylation in proteolysis and cellular regulation
Wilkinson, K D
Annual Review of Nutrition, 15, 161-189 (1995)
L J Kurihara et al.
Molecular and cellular biology, 20(7), 2498-2504 (2000-03-14)
Mice homozygous for the s(1Acrg) deletion at the Ednrb locus arrest at embryonic day 8.5. To determine the molecular basis of this defect, we initiated positional cloning of the s(1Acrg) minimal region. The mouse Uch-L3 (ubiquitin C-terminal hydrolase L3) gene
Shahram Misaghi et al.
The Journal of biological chemistry, 280(2), 1512-1520 (2004-11-09)
Ubiquitin C-terminal hydrolases (UCHs) comprise a family of small ubiquitin-specific proteases of uncertain function. Although no cellular substrates have been identified for UCHs, their highly tissue-specific expression patterns and the association of UCH-L1 mutations with human disease strongly suggest a
Kinetic and mechanistic studies on the hydrolysis of ubiquitin C-terminal 7-amido-4-methylcoumarin by deubiquitinating enzymes.
Dang, L C, et al.
Biochemistry, 37, 1868-1879 (1998)

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