|Application ||WB, IHC-P, E|
|Other Accession||Q9D9M2, A5D9H7, Q5M981, Q52KZ6, NP_872294|
|Calculated MW||42858 Da|
|Antigen Region||5-35 aa|
|Other Names||Ubiquitin carboxyl-terminal hydrolase 12, Deubiquitinating enzyme 12, Ubiquitin thioesterase 12, Ubiquitin-hydrolyzing enzyme 1, Ubiquitin-specific-processing protease 12, USP12, UBH1, USP12L1|
|Target/Specificity||This USP12 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 5-35 amino acids from the N-terminal region of human USP12.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||USP12 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Deubiquitinating enzyme. Has almost no deubiquitinating activity by itself and requires the interaction with WDR48 to have a high activity. Not involved in deubiquitination of monoubiquitinated FANCD2.|
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Provided below are standard protocols that you may find useful for product applications.
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.
Hansen-Hagge, T.E., et al., Genomics 49(3):411-418 (1998).
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