This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.
Immunogen
This USP2 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 380-410 amino acids from the C-terminal region of human USP2.
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Konservierungsmittel
Sodium azide
Vorsichtsmaßnahmen
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Lagerung
4 °C,-20 °C
Informationen zur Lagerung
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.
Haltbarkeit
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).
Alonso, Magyar, Wang, Bisello, Friedman: "Ubiquitination-deubiquitination balance dictates ligand-stimulated PTHR sorting." in: Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research, Vol. 26, Issue 12, pp. 2923-34, (2011) (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.