Recombinant Human USP22 protein (His-DHFR tag N-Terminus)
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Recombinant Human USP22 protein (His-DHFR tag N-Terminus) is a Human Fragment protein, in the 295 to 513 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.
View Alternative Names
KIAA1063, USP3L, USP22, Ubiquitin carboxyl-terminal hydrolase 22, Deubiquitinating enzyme 22, Ubiquitin thioesterase 22, Ubiquitin-specific-processing protease 22
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Removal of ubiquitin by USP22 regulates gene expression by modulating histone modifications. USP22 acts as a part of the Spt-Ada-Gcn5 acetyltransferase (SAGA) complex which plays a significant role in transcriptional regulation. Through its deubiquitinating activity USP22 alters the ubiquitination status of histone proteins thereby impacting chromatin dynamics and gene transcription.
Pathways
USP22 takes part in critical pathways like the ubiquitin-proteasome system and chromosome structure modulation. Within these processes USP22 closely interacts with proteins such as SAGA complex members and histone H2B. Its activity within this system highlights roles in transcriptional control and cellular growth important for maintaining cellular homeostasis and regulating cell cycle progression.
Specifications
Form
Lyophilized
Additional notes
Purified via His tag
General info
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).
Sequence similarities
Belongs to the peptidase C19 family. UBP8 subfamily.
Post-translational modifications
Phosphorylated in G2/M phase, but not in G1 phase by CDK1.. Ubiquitinated and subsequently degraded in a CDC20-dependent manner.
Subcellular localisation
Nucleus
Target data
Product promise
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