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USP5 Antibody (C-term) Blocking Peptide
Synthetic peptide
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| Primary Accession | P45974 |
|---|---|
| Other Accession | UBP5_HUMAN |
| Clone Names | 3062507 |
| Gene ID | 8078 |
|---|---|
| Other Names | Ubiquitin carboxyl-terminal hydrolase 5, Deubiquitinating enzyme 5, Isopeptidase T, Ubiquitin thioesterase 5, Ubiquitin-specific-processing protease 5, USP5, ISOT |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP2134b was selected from the C-term region of human USP5 . 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 | USP5 |
|---|---|
| Synonyms | ISOT |
| Function | Cleaves linear and branched multiubiquitin polymers with a marked preference for branched polymers. Involved in unanchored 'Lys- 48'-linked polyubiquitin disassembly. Binds linear and 'Lys-63'-linked polyubiquitin with a lower affinity. Knock-down of USP5 causes the accumulation of p53/TP53 and an increase in p53/TP53 transcriptional activity because the unanchored polyubiquitin that accumulates is able to compete with ubiquitinated p53/TP53 but not with MDM2 for proteasomal recognition. |
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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
Strausberg, R.L., et al., Proc. Natl. Acad. Sci. U.S.A. 99(26):16899-16903 (2002).Ansari-Lari, M.A., et al., Genome Res. 6(4):314-326 (1996).Falquet, L., et al., FEBS Lett. 376(3):233-237 (1995).Falquet, L., et al., FEBS Lett. 359(1):73-77 (1995).
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