|Other Names||Ubiquitin carboxyl-terminal hydrolase 21, Deubiquitinating enzyme 21, Ubiquitin thioesterase 21, Ubiquitin-specific-processing protease 21, USP21, USP23|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP1069a was selected from the N-term region of human USP21. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Deubiquitinates histone H2A, a specific tag for epigenetic transcriptional repression, thereby acting as a coactivator. Deubiquitination of histone H2A releaves the repression of di- and trimethylation of histone H3 at 'Lys-4', resulting in regulation of transcriptional initiation. Regulates gene expression via histone H2A deubiquitination (By similarity). Also capable of removing NEDD8 from NEDD8 conjugates but has no effect on Sentrin-1 conjugates (PubMed:10799498). Deubiquitinates BAZ2A/TIP5 leading to its stabilization (PubMed:26100909).|
|Cellular Location||Cytoplasm. Nucleus|
|Tissue Location||Highly expressed in heart, pancreas and skeletal muscle. Also expressed in brain, placenta, liver and kidney, and at very low level in lung|
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Provided below are standard protocols that you may find useful for product applications.
USP21 is a ubiquitin-specific protease, an enzyme that removes ubiquitin from ubiquitinated proteins. The encoded protein belongs to the C19 peptidase family, also known as family 2 of ubiquitin carboxyl-terminal hydrolases. This protein has been reported to be capable of removing NEDD8 from NEDD8 conjugates. Alternatively spliced transcript variants encoding different isoforms have been identified.
Puente, X.S., et al., Nat. Rev. Genet. 4(7):544-558 (2003).Gong, L., et al., J. Biol. Chem. 275(19):14212-14216 (2000).Hillier, L.D., et al., Genome Res. 6(9):807-828 (1996).Smith, T.S., et al., Biochim. Biophys. Acta 1490 (1-2), 184-188 (2000).
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