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Merck
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資料

安全性情報

14-855

Sigma-Aldrich

Ubiquitin C-terminal hydrolase L1 (UCH-L1), 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

UNSPSCコード:
12352200
eCl@ss:
32160405
NACRES:
NA.32

由来生物

human

品質水準

リコンビナント

expressed in E. coli

比活性

>1000 pmol/min-μg, 25 °C (with 1 μM ubiquitin-AMC as substrate and UCH-L1 at 20 pM (0.54 ng/mL).)

分子量

Mw 24.8 kDa

メーカー/製品名

Upstate®

NCBIアクセッション番号

UniProtアクセッション番号

輸送温度

dry ice

詳細

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. Mammalian neuronal cells abundantly express a deubiquitylating enzyme, ubiquitin carboxy-terminal hydrolase 1 (UCH-L1). Mutations in UCH-L1 are linked to Parkinson′s disease as well as gracile axonal dystrophy (gad) in mice. In contrast to the universally expressed UCH-L3 isozyme, UCH-L1 is expressed exclusively in neurons and testis/ovary. It has been shown that UCH-L1 associates and co-localizes with monoubiquitin and elongates ubiquitin half-life and the suggestion is made that UCH-L1, with avidity and affinity for ubiquitin, ensures ubiquitin stability within neurons.
Product Source: Recombinant human UCH-L1 expressed in E. coli

保管および安定性

As supplied, store at -80°C for up to 12 months from date of receipt. Avoid repeated freeze/thaw cycles. After initial defrost, aliquot (for extended storage it is recommended that aliquots be no smaller then 10 μL) and store at -80°C. Snap-freezing in a dry ice/ethanol bath or liquid nitrogen is recommended. As supplied, the enzyme is stable on ice for several hours.

法的情報

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

免責事項

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.

保管分類コード

12 - Non Combustible Liquids

WGK

WGK 1

引火点(°F)

Not applicable

引火点(℃)

Not applicable


適用法令

試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。

Jan Code

14-855:


試験成績書(COA)

製品のロット番号・バッチ番号を入力して、試験成績書(COA) を検索できます。ロット番号・バッチ番号は、製品ラベルに「Lot」または「Batch」に続いて記載されています。

以前この製品を購入いただいたことがある場合

文書ライブラリで、最近購入した製品の文書を検索できます。

文書ライブラリにアクセスする

I N Day et al.
FEBS letters, 210(2), 157-160 (1987-01-05)
The co-ordinate sequencing of the human neuronal and neuroendocrine marker protein PGP 9.5 and its cDNA is described. The cDNA encodes the complete protein (212 amino acids), and the 340 nucleotide 3'-noncoding region including the polyadenylation signal, indicating an mRNA
C N Larsen et al.
Biochemistry, 35(21), 6735-6744 (1996-05-28)
Ubiquitin C-terminal hydrolases (UCH's) are a newly-defined class of thiol proteases implicated in the proteolytic processing of polymeric ubiquitin. They are important for the generation of monomeric ubiquitin, the active component of the eukaryotic ubiquitin-dependent proteolytic system. There are at
I N Day et al.
The Biochemical journal, 268(2), 521-524 (1990-06-01)
Database search using a bovine thymus ubiquitin C-terminal hydrolase sequence indicated 54% sequence identity with the abundant human neuron-specific protein gene product 9.5 (PGP9.5), which was then shown to possess the same activity [Wilkinson, Lee, Deshpande, Duerksen-Hughes, Boss & Pohl
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)
Yichin Liu et al.
Cell, 111(2), 209-218 (2002-11-01)
The assumption that each enzyme expresses a single enzymatic activity in vivo is challenged by the linkage of the neuronal enzyme ubiquitin C-terminal hydrolase-L1 (UCH-L1) to Parkinson's disease (PD). UCH-L1, especially those variants linked to higher susceptibility to PD, causes

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