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WH0009097M4

Sigma-Aldrich

Monoclonal Anti-USP14 antibody produced in mouse

clone 6D6, purified immunoglobulin, buffered aqueous solution

Synonyme(s) :

Anti-TGT, Anti-ubiquitin specific peptidase 14 (tRNA-guanine transglycosylase)

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About This Item

Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Conjugué

unconjugated

Forme d'anticorps

purified immunoglobulin

Type de produit anticorps

primary antibodies

Clone

6D6, monoclonal

Forme

buffered aqueous solution

Espèces réactives

rat, mouse, human

Technique(s)

indirect ELISA: suitable
indirect immunofluorescence: suitable
western blot: 1-5 μg/mL

Isotype

IgG2aκ

Numéro d'accès GenBank

NM_005151

Numéro d'accès UniProt

P54578

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... USP14(9097)

Description générale

Ubiquitin specific peptidase 14 (USP14) is a 494 amino acid protein containing a 45kDa catalytic domain at its amino-terminus. Its ubiquitin-like (Ubl) domain associates with 19S regulatory particle (RP) 26S proteasome. This binding activates the deubiquitinating activity of the protein. USP14 is part of the ubiquitin-specific processing (UBP) family of proteases.

Immunogène

USP14 (NP_005142, 395 a.a. ~ 494 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
PQKEVKYEPFSFADDIGSNNCGYYDLQAVLTHQGRSSSSGHYVSWVKRKQDEWIKFDDDKVSIVTPEDILRLSGGGDWHIAYVLLYGPRRVEIMEEESEQ

Actions biochimiques/physiologiques

Ubiquitin specific peptidase 14 (USP14) releases ubiquitin from the proteasome-targeted ubiquitinated proteins resulting in regeneration of ubiquitin at the proteasome. It is involved in the degradation of chemokine receptor CXCR4. Under endoplasmic reticulum (ER) stress, USp14 binds to ER stress receptor, which is involved in unfolded protein response (UPR), a mechanism to control the accumulation of unfolded proteins within the ER lumen. Its overexpression leads to ER-associated degradation (ERAD) pathway inhibition.

Forme physique

Solution in phosphate buffered saline, pH 7.4

Informations légales

GenBank is a registered trademark of United States Department of Health and Human Services

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

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

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

Certificats d'analyse (COA)

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Consulter la Bibliothèque de documents

Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14
The Embo Journal (2005)
Deubiquitination of CXCR4 by USP14 is critical for both CXCL12-induced CXCR4 degradation and chemotaxis but not ERK activation
Marjelo A Mines
The Journal of Biological Chemistry (2008)
USP14 inhibits ER-associated degradation via interaction with IRE1alpha
Atsushi Nagai
Biochemical and Biophysical Research Communications (2009)
Zhanyu Ding et al.
Molecular cell, 73(6), 1150-1161 (2019-02-23)
The 26S proteasome is the ATP-dependent protease responsible for regulating the proteome of eukaryotic cells through degradation of mainly ubiquitin-tagged substrates. In order to understand how proteasome responds to ubiquitin signal, we resolved an ensemble of cryo-EM structures of proteasome
Jayashree Chadchankar et al.
PloS one, 14(11), e0225145-e0225145 (2019-11-09)
USP14 is a cysteine protease deubiquitinase associated with the proteasome and plays important catalytic and allosteric roles in proteasomal degradation. USP14 inhibition has been considered a therapeutic strategy for accelerating degradation of aggregation-prone proteins in neurodegenerative diseases and for inhibiting

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