USP22 KO cell lysate available now. KO validated by Western blot. Free of charge wild type control included. Knockout achieved by using CRISPR/Cas9, Homozygous: 1 bp deletion in exon 1.
Deubiquitinating enzyme 22, KIAA1063, UBP22_HUMAN, USP3L, Ubiquitin carboxyl-terminal hydrolase 22, Ubiquitin specific peptidase 22, Ubiquitin specific peptidase 3 like, Ubiquitin specific protease 22, Ubiquitin thioesterase 22, Ubiquitin thiolesterase 22, Ubiquitin-specific-processing protease 22
USP22 KO cell lysate available now. KO validated by Western blot. Free of charge wild type control included. Knockout achieved by using CRISPR/Cas9, Homozygous: 1 bp deletion in exon 1.
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Lysate preparation: Our lysates are made using RIPA buffer to which we add a protease inhibitor cocktail and phosphatase inhibitor cocktail (ratio: 300:100:10). This means that the protein of interest is denatured. If you require a native form of the protein please use the live cell version. Please refer to our lysis protocol for further details on how our lysates are prepared.
User storage instructions: Lyophilizate may be stored at 4°C. After reconstitution, store at -20°C for short-term storage or -80°C for long-term storage.
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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.
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.
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.
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All lanes: Western blot - Anti-USP22 antibody [EPR18945] (Anti-USP22 antibody [EPR18945] ab195289) at 1/2000 dilution
Lane 1: Western blot - Human USP22 knockout HeLa cell lysate (ab257789)
Lane 1: Wild-type HeLa cell lysate at 20 µg
Lane 2: USP22 knockout HeLa cell lysate at 20 µg
Lane 2: Western blot - Human USP22 knockout HeLa cell line (Human USP22 knockout HeLa cell line ab264888)
Performed under reducing conditions.
Predicted band size: 60 kDa
Observed band size: 59 kDa
All lanes: Western blot - Anti-USP22 antibody [EPR4352(2)] (Anti-USP22 antibody [EPR4352(2)] ab109435) at 1/1000 dilution
Lane 1: Wild-type HeLa cell lysate
Lane 2: USP22 knockout HeLa cell lysate
Performed under reducing conditions.
Predicted band size: 60 kDa
Observed band size: 59 kDa
Homozygous: 1 bp deletion in exon 1
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