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USP28 Antibody (C-term) Blocking Peptide

Synthetic peptide

Product Information
Primary Accession Q96RU2
Other Accession NP_065937
Clone Names 3080103
Additional Information
Gene ID 57646
Other Names Ubiquitin carboxyl-terminal hydrolase 28, Deubiquitinating enzyme 28, Ubiquitin thioesterase 28, Ubiquitin-specific-processing protease 28, USP28, KIAA1515
Target/Specificity The synthetic peptide sequence used to generate the antibody AP2152b was selected from the C-term region of human USP28 . 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.
StorageMaintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.
PrecautionsThis product is for research use only. Not for use in diagnostic or therapeutic procedures.
Protein Information
Name USP28
Synonyms KIAA1515
Function Deubiquitinase involved in DNA damage response checkpoint and MYC proto-oncogene stability. Involved in DNA damage induced apoptosis by specifically deubiquitinating proteins of the DNA damage pathway such as CLSPN. Also involved in G2 DNA damage checkpoint, by deubiquitinating CLSPN, and preventing its degradation by the anaphase promoting complex/cyclosome (APC/C). In contrast, it does not deubiquitinate PLK1. Specifically deubiquitinates MYC in the nucleoplasm, leading to prevent MYC degradation by the proteasome: acts by specifically interacting with isoform 1 of FBXW7 (FBW7alpha) in the nucleoplasm and counteracting ubiquitination of MYC by the SCF(FBW7) complex. In contrast, it does not interact with isoform 4 of FBXW7 (FBW7gamma) in the nucleolus, allowing MYC degradation and explaining the selective MYC degradation in the nucleolus.
Cellular Location Nucleus, nucleoplasm
Research Areas
Citations (0)

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Modification of target proteins by ubiquitin participates in a wide array of biological functions. Proteins destined for degradation or processing via the 26 S proteasome are coupled to multiple copies of ubiquitin. However, attachment of ubiquitin or ubiquitin-related molecules may also result in changes in subcellular distribution or modification of protein activity. An additional level of ubiquitin regulation, deubiquitination, is catalyzed by proteases called deubiquitinating enzymes, which fall into four distinct families. Ubiquitin C-terminal hydrolases, ubiquitin-specific processing proteases (USPs),1 OTU-domain ubiquitin-aldehyde-binding proteins, and Jab1/Pad1/MPN-domain-containing metallo-enzymes. Among these four families, USPs represent the most widespread and represented deubiquitinating enzymes across evolution. USPs tend to release ubiquitin from a conjugated protein. They display similar catalytic domains containing conserved Cys and His boxes but divergent N-terminal and occasionally C-terminal extensions, which are thought to function in substrate recognition, subcellular localization, and protein-protein interactions.


Puente, X.S., et al., Nat. Rev. Genet. 4(7):544-558 (2003).Valero, R., et al., Genome Biol. 2 (10), RESEARCH0043 (2001).

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$ 80.00
Cat# BP2152b
(40 western blots)
Availability: In Stock
Bulk Size
Seasonal Special on Bulk Order
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