Quick Overview for USP29 antibody (AA 660-690) (ABIN2839199)
Target
USP29
(Ubiquitin Specific Peptidase 29 (USP29))
Reactivity
Human
Host
Rabbit
Clonality
Polyclonal
Conjugate
This USP29 antibody is un-conjugated
Application
Western Blotting (WB), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p))
Clone
RB4373
Binding Specificity
AA 660-690
Purification
This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogen
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
Reactivity: Human
WB, IHC, ELISA
Host: Rabbit
Polyclonal
unconjugated
Application Notes
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.
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C,-20 °C
Storage Comment
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.
Expiry Date
6 months
Target
USP29
(Ubiquitin Specific Peptidase 29 (USP29))
Alternative Name
USP29
Background
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.