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USP3 Antibody (C-term) Blocking Peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
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- BACKGROUND
| Primary Accession | Q9Y6I4 |
|---|---|
| Other Accession | UBP3_HUMAN |
| Clone Names | 3062712 |
| Gene ID | 9960 |
|---|---|
| Other Names | Ubiquitin carboxyl-terminal hydrolase 3, Deubiquitinating enzyme 3, Ubiquitin thioesterase 3, Ubiquitin-specific-processing protease 3, USP3 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP2132c was selected from the C-term region of human USP3 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| 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. |
| Name | USP3 |
|---|---|
| Function | Deubiquitinase that plays a role in several cellular processes including transcriptional regulation, cell cycle progression or innate immunity. In response to DNA damage, deubiquitinates monoubiquitinated target proteins such as histone H2A and H2AX and thereby counteracts RNF168- and RNF8-mediated ubiquitination. In turn, participates in the recruitment of DNA damage repair factors to DNA break sites (PubMed:24196443). Required for proper progression through S phase and subsequent mitotic entry (PubMed:17980597). Acts as a positive regulator of TP53 by deubiquitinating and stabilizing it to promote normal cell proliferation and transformation (PubMed:28807825). Participates in establishing tolerance innate immune memory through non-transcriptional feedback. Mechanistically, negatively regulates TLR-induced NF-kappa-B signaling by targeting and removing the 'Lys- 63'-linked polyubiquitin chains on MYD88 (PubMed:37971847). Negatively regulates the activation of type I interferon signaling by mediating 'Lys-63'-linked polyubiquitin chains on RIGI and IFIH1 (PubMed:24366338). Also deubiquinates ASC/PYCARD, the central adapter mediating the assembly and activation of most inflammasomes, and thereby promotes inflammasome activation (PubMed:36050480). |
| Cellular Location | Nucleus. Cytoplasm. Note=Localizes preferentially with monoubiquitinated H2A to chromatin (PubMed:17980597). Upon NF-kappa-B signaling activation, exits the nucleus (PubMed:37971847) |
| Tissue Location | Expressed in all tissues examined, with strongest expression in pancreas |
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
Puente, X.S., et al., Nat. Rev. Genet. 4(7):544-558 (2003).Sloper-Mould, K.E., et al., J. Biol. Chem. 274(38):26878-26884 (1999).
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