Aperçu rapide pour USP29 anticorps (AA 660-690) (ABIN650701)
Antigène
USP29
(Ubiquitin Specific Peptidase 29 (USP29))
Reactivité
Humain
Hôte
Lapin
Clonalité
Polyclonal
Conjugué
Cet anticorp USP29 est non-conjugé
Application
Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
Clone
RB4373
Épitope
AA 660-690
Purification
This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogène
This USP29 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 660-690 amino acids from the Central region of human USP29.
USP29
Reactivité: Humain
IHC, ELISA
Hôte: Lapin
Polyclonal
unconjugated
Indications d'application
WB: 1:1000. IHC-P: 1:10~50
Restrictions
For Research Use only
Format
Liquid
Buffer
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Agent conservateur
Sodium azide
Précaution d'utilisation
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Stock
4 °C,-20 °C
Stockage commentaire
Maintain refrigerated at 2-8 °C for up to 6 months. For long term storage store at -20 °C in small aliquots to prevent freeze-thaw cycles.
Date de péremption
6 months
Antigène
USP29
(Ubiquitin Specific Peptidase 29 (USP29))
Autre désignation
USP29
Sujet
Modification of target proteins by ubiquitin participates in a wide array of biological functions. Proteins destined for degradation or processing via the 26 S proteasome are coupled to multiple copies of ubiquitin. However, attachment of ubiquitin or ubiquitin-related molecules may also result in changes in subcellular distribution or modification of protein activity. An additional level of ubiquitin regulation, deubiquitination, is catalyzed by proteases called deubiquitinating enzymes, which fall into four distinct families. Ubiquitin C-terminal hydrolases, ubiquitin-specific processing proteases (USPs),1 OTU-domain ubiquitin-aldehyde-binding proteins, and Jab1/Pad1/MPN-domain-containing metallo-enzymes. Among these four families, USPs represent the most widespread and represented deubiquitinating enzymes across evolution. USPs tend to release ubiquitin from a conjugated protein. They display similar catalytic domains containing conserved Cys and His boxes but divergent N-terminal and occasionally C-terminal extensions, which are thought to function in substrate recognition, subcellular localization, and protein-protein interactions.