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U5258

Sigma-Aldrich

Anti-Ubiquitin C-terminal Hydrolase L1 (RA-15) antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Sinônimo(s):

Anti-UCH-L1

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About This Item

Número MDL:
Código UNSPSC:
12352203
NACRES:
NA.41

fonte biológica

rabbit

conjugado

unconjugated

forma do anticorpo

IgG fraction of antiserum

tipo de produto de anticorpo

primary antibodies

clone

polyclonal

Formulário

buffered aqueous solution

peso molecular

antigen 27 kDa

reatividade de espécies

human, mouse, rat

técnica(s)

microarray: suitable
western blot: 1:1,000-1:2,000 using cytosolic fraction (S1) of mouse brain or whole cell extract of human lung carcinoma A549 cell line
western blot: 1:5,000-1:10,000 using cytosolic fraction (S1) of rat brain

nº de adesão UniProt

Condições de expedição

dry ice

temperatura de armazenamento

−20°C

modificação pós-traducional do alvo

unmodified

Informações sobre genes

human ... UCHL1(7345)
mouse ... Uchl1(22223)
rat ... Uchl1(29545)

Descrição geral

Ubiquitin C-terminal hydrolase L1 (UCH-L1) is encoded by the gene mapped to human chromosome 4p13. It is a 223 amino acid deubiquitinating enzyme, expressed highly in neurons.

Imunogênio

synthetic peptide corresponding to amino acids 202-216 located near the C-terminus of rat UCH-L1, conjugated to KLH. This sequence is identical in human, mouse, bovine, porcine, and guinea pig UCH-L1. No homology is found with other known UCH-L isoforms.

Aplicação

Anti-Ubiquitin C-terminal Hydrolase L1 (RA-15) antibody produced in rabbit has been used in immunoblotting.

Ações bioquímicas/fisiológicas

Ubiquitin C-terminal hydrolase L1 (UCH-L1) hydrolyze C-terminal ubiquityl esters and amides in vitro, which is an essential reaction during cytoplasmic protein degradation. peptide-ubiquityl amides are the most favorable substrates. UCH-L1 also acts as a ubiquitin (Ub) ligase. Mutation in the gene is associated with the development of neurodegenerative diseases, such as Parkinson′s disease, spinocerebellar ataxia (SCA) and Huntington′s disease.

forma física

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Exoneração de responsabilidade

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.

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Código de classe de armazenamento

10 - Combustible liquids

Classe de risco de água (WGK)

WGK 3

Ponto de fulgor (°F)

Not applicable

Ponto de fulgor (°C)

Not applicable

Equipamento de proteção individual

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)


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The UCH-L1 gene encodes two opposing enzymatic activities that affect alpha-synuclein degradation and Parkinson's disease susceptibility
Liu Y, et al.
Cell, 111(2), 209-218 (2002)
Reduced expression of the G209A alpha-synuclein allele in familial parkinsonism
Markopoulou K, et al.
Annals of Neurology, 46(3), 374-381 (1999)
Krishnan Sriram et al.
Toxicology and applied pharmacology, 449, 116137-116137 (2022-06-25)
Workers in the oil and gas industry are at risk for exposure to a number of physical and chemical hazards at the workplace. Chemical hazard risks include inhalation of crude oil or its volatile components. While several studies have investigated
Karnam Shruthi et al.
Journal of cellular biochemistry, 120(4), 5962-5973 (2018-10-15)
The ubiquitin-proteasome system (UPS) has been implicated in the pathogenesis of many neurodegenerative diseases. Endoplasmic reticulum (ER) stress is shown to play a pathological role in the development of diabetes and its complications. Hence, the current study is aimed to
Robin K Meray et al.
The Journal of biological chemistry, 282(14), 10567-10575 (2007-01-30)
Deubiquitinating enzymes (DUBs) are negative regulators of protein ubiquitination and play an important role in ubiquitin-dependent processes. Recent studies have found that diverse cellular mechanisms are employed to control the activity of DUBs. Ubiquitin C-terminal hydrolase-L1 (UCH-L1) is a highly

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