|Application ||WB, IHC-P, E|
|Calculated MW||62656 Da|
|Antigen Region||24-53 aa|
|Other Names||Ubiquitin carboxyl-terminal hydrolase 21, Deubiquitinating enzyme 21, Ubiquitin thioesterase 21, Ubiquitin-specific-processing protease 21, USP21, USP23|
|Target/Specificity||This USP21 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 24~53 amino acids from the N-terminal region of human USP21.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||USP21 Antibody (N-term P31) is for research use only and 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.
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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