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AB127325

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

Key facts

Purity

>95% SDS-PAGE

Expression system

Escherichia coli

Tags

His-DHFR tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q9UPT9

Animal free

No

Carrier free

No

Species

Human

Reconstitution

Reconstitute in water

Storage buffer

Constituents: 0.58% Sodium chloride, 0.32% Tris HCl

storage-buffer

Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

Sequence info

[{"sequence":"","proteinLength":"Fragment","predictedMolecularWeight":"24.8 kDa","actualMolecularWeight":null,"aminoAcidEnd":513,"aminoAcidStart":295,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q9UPT9","tags":[{"tag":"His-DHFR","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
False

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

USP22 also known as ubiquitin-specific protease 22 is an enzyme belonging to the class of deubiquitinating enzymes (DUBs). It is characterized by the ability to remove ubiquitin moieties from target proteins which can alter their stability and function. Carrying an approximate mass of 59 kDa USP22 localizes mainly in the nucleus. Expression of USP22 is widespread across a range of tissues with higher levels identified in tissues exhibiting high proliferative capacity.
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.

USP22 shows strong implications in several types of cancer including colorectal and prostate cancer. Abnormal expression levels can alter the transcriptional landscape contributing to tumor progression and metastasis. Further USP22 links to other proteins like MYC in the cancer context highlighting its importance in oncogenic pathways. This connection suggests that targeting USP22 might offer therapeutic potential in treating cancers where its expression is dysregulated.

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

Product protocols

Target data

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).
See full target information USP22

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