USP22 antibodies are critical for detecting endogenous USP22 protein levels. For example:
Abcam’s ab195289 detects a 65 kDa band in HeLa lysates, confirmed by immunoprecipitation (IP) and KO validation .
Proteintech’s 55110-1-AP is validated for WB and IHC, with protocols available for optimization .
Avivasysbio’s OACA12683 is used to visualize nuclear USP22 localization in fixed cells .
Abcam’s ab195289 stains nuclear USP22 in breast carcinoma tissues, highlighting its role in oncogenesis .
Cusabio’s CSB-RA784212A0HU and FisherSci’s JU63-27 enable intracellular USP22 detection in live or fixed cells .
Abcam’s ab195289 is validated for IP, permitting USP22 complex analysis (e.g., SAGA complex interactions) .
USP22 is a core component of the SAGA complex, where it deubiquitinates histone H2B to promote transcriptional activation . Key findings:
MYC Recruitment: USP22 is recruited to MYC-target genes (e.g., CCND1), enabling oncogenic transcription and cell cycle progression .
PD-L1 Stabilization: USP22 deubiquitinates PD-L1, enhancing its stability and immune tolerance .
Usp22 deficiency in mice reduces PD-L1 expression on antigen-presenting cells, leading to:
Enhanced CD8+ T Cell Activation: Increased cytotoxic T cell responses cause liver immunopathology during LCMV infection .
Interferon Dysregulation: Reduced type I interferon (IFN-α/β) at early infection stages but elevated type II IFN (IFN-γ) later .
USP22 regulates necroptosis via RIPK3 ubiquitination. Depletion of USP22:
Blocks RIPK3 Phosphorylation: Suppresses necroptosis in HT-29 colorectal cancer cells .
Promotes Proteasomal Degradation: Loss of USP22 increases RIPK3 K48-linked ubiquitination, favoring apoptosis .
In B cells, USP22 facilitates class switch recombination (CSR) by:
Enhancing c-NHEJ: USP22-deficient mice show defects in IgG/E CSR but retain IgA CSR, which relies on alt-EJ .
Stabilizing DNA Repair Proteins: USP22 supports γH2AX formation and 53BP1 recruitment to DNA breaks .
The USP22 recombinant monoclonal antibody is synthetically produced in vitro using a systematic approach. Initially, USP22 antibody genes are extracted from B cells isolated from immunoreactive rabbits. These genes undergo amplification and are cloned into suitable phage vectors, which are subsequently introduced into mammalian cell lines to facilitate the production of functional antibodies in significant quantities. The resulting USP22 recombinant monoclonal antibody is subjected to affinity chromatography purification. After rigorous verification, the antibody can be used in ELISA, IF, and FC applications, allowing for precise detection of human USP22 protein.
USP22 is a multifunctional protein that plays a pivotal role in epigenetic regulation by deubiquitinating histones and modulating chromatin structure. Its activities impact gene expression, cell cycle control, stem cell maintenance, DNA repair, and various aspects of development. Dysregulation of USP22 can have significant implications for diseases, including cancer.
USP22 serves as a histone deubiquitinating component of the transcription regulatory histone acetylation (HAT) complex SAGA. It catalyzes the deubiquitination of both histones H2A and H2B, thus acting as a coactivator. USP22 is recruited to specific gene promoters by activators such as MYC, where it is essential for transcription. Furthermore, it is required for nuclear receptor-mediated transactivation and cell cycle progression.