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Principaux documents

U5258

Sigma-Aldrich

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

IgG fraction of antiserum, buffered aqueous solution

Synonyme(s) :

Anti-UCH-L1

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About This Item

Numéro MDL:
MFCD07370533
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

rabbit

Conjugué

unconjugated

Forme d'anticorps

IgG fraction of antiserum

Type de produit anticorps

primary antibodies

Clone

polyclonal

Forme

buffered aqueous solution

Poids mol.

antigen 27 kDa

Espèces réactives

human, mouse, rat

Technique(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

Numéro d'accès UniProt

P09936

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

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

Description générale

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.

Immunogène

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.

Application

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

Actions biochimiques/physiologiques

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.

Forme physique

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

Clause de non-responsabilité

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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Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

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

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Certificats d'analyse (COA)

Lot/Batch Number
097M4870V
032M4838V
025K4801

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Retrouvez la documentation relative aux produits que vous avez récemment achetés dans la Bibliothèque de documents.

Consulter la Bibliothèque de documents

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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