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USP22 Antibody (C-term)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS: 2
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P, E |
|---|---|
| Primary Accession | Q9UPT9 |
| Other Accession | Q8CEG8, A6NNY8, Q5DU02, A6H8I0, P0C8Z3, Q6DCJ1, Q6GNI6 |
| Reactivity | Human |
| Predicted | Xenopus, Bovine, Zebrafish, Mouse |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 59961 Da |
| Antigen Region | 351-380 aa |
| Gene ID | 23326 |
|---|---|
| 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 351-380 amino acids from the C-terminal region of human USP22. |
| Dilution | WB~~1:1000 IHC-P~~1:50~100 |
| 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 (C-term) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | USP22 |
|---|---|
| Synonyms | KIAA1063, USP3L |
| Function | Deubiquitinase that plays a role in several cellular processes including transcriptional regulation, cell cycle progression or innate immunity. As part of the transcription regulatory histone acetylation (HAT) complex SAGA, catalyzes the deubiquitination of both histones H2A and H2B, thereby acting as a transcriptional coactivator (PubMed:18206972, PubMed:18206973, PubMed:18469533). Recruited to specific gene promoters by activators such as MYC, where it is required for transcription. Facilitates cell-cycle progression by stabilizing CCNB1 and antagonizing its proteasome-mediated degradation in a cell cycle-specific manner (PubMed:27030811). Modulates cell cycle progression and apoptosis also by antagonizing TP53 transcriptional activation through deacetylase SIRT1 stabilization (PubMed:22542455). Plays multiple roles in immunity and inflammation. Participates in antiviral response by deubiquitinating the importin KPNA2, leading to IRF3 nuclear translocation and subsequent type I interferon production (PubMed:32130408). Acts as a central regulator of type III IFN signaling by negatively regulating STING1 activation and ubiquitination (PubMed:35933402). Inhibits NLRP3 inflammasome activation by promoting NLRP3 degradation through ATG5-dependent autophagy (By similarity). Deubiquitinates CD274 to induce its stabilization and thereby participates in maintenance of immune tolerance to self (PubMed:31399419). Controls necroptotic cell death by regulating RIPK3 phosphorylation and ubiquitination (PubMed:33369872). During bacterial infection, promotes pro-inflammatory response by targeting TRAF6 and removing its 'Lys-48'-linked polyubiquitination (By similarity). |
| Cellular Location | Nucleus. Cytoplasm {ECO:0000250|UniProtKB:Q5DU02} |
| 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.
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.
References
Kikuno, R., et al., DNA Res. 6(3):197-205 (1999).
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