- CITATIONS: 1
|Application ||WB, E|
|Calculated MW||59961 Da|
|Antigen Region||1-30 aa|
|Other Names||Ubiquitin carboxyl-terminal hydrolase 22, Deubiquitinating enzyme 22, Ubiquitin thioesterase 22, Ubiquitin-specific-processing protease 22, USP22, KIAA1063, USP3L|
|Target/Specificity||This USP22 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 1-30 amino acids from the N-terminal region of human USP22.|
|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||USP22 Antibody (N-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. Catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a coactivator. Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Required for nuclear receptor-mediated transactivation and cell cycle progression.|
|Tissue Location||Moderately expressed in various tissues including heart and skeletal muscle, and weakly expressed in lung and liver.|
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.
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