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
Expiry Date
6 months
Tong, Buelow, Guha, Rausch, Yin: "USP2a protein deubiquitinates and stabilizes the circadian protein CRY1 in response to inflammatory signals." in: The Journal of biological chemistry, Vol. 287, Issue 30, pp. 25280-91, (2012) (PubMed).
Haimerl, Erhardt, Sass, Tiegs: "Down-regulation of the de-ubiquitinating enzyme ubiquitin-specific protease 2 contributes to tumor necrosis factor-alpha-induced hepatocyte survival." in: The Journal of biological chemistry, Vol. 284, Issue 1, pp. 495-504, (2008) (PubMed).
Strausberg, Feingold, Grouse, Derge, Klausner, Collins, Wagner, Shenmen, Schuler, Altschul, Zeeberg, Buetow, Schaefer, Bhat, Hopkins, Jordan, Moore, Max, Wang, Hsieh, Diatchenko, Marusina, Farmer et al.: "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. ..." in: Proceedings of the National Academy of Sciences of the United States of America, Vol. 99, Issue 26, pp. 16899-903, (2002) (PubMed).
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.