|Other Names||Ubiquitin carboxyl-terminal hydrolase isozyme L5, UCH-L5, Ubiquitin C-terminal hydrolase UCH37, Ubiquitin thioesterase L5, UCHL5, UCH37|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP2128b was selected from the C-term region of human UCHL5 . 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||Protease that specifically cleaves 'Lys-48'-linked polyubiquitin chains. Deubiquitinating enzyme associated with the 19S regulatory subunit of the 26S proteasome. Putative regulatory component of the INO80 complex; however is inactive in the INO80 complex and is activated by a transient interaction of the INO80 complex with the proteasome via ADRM1.|
|Cellular Location||Cytoplasm. Nucleus. Note=Associates with the proteasome 19S subunit in the cytoplasm. Associates with the INO80 complex in the nucleus|
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Provided below are standard protocols that you may find useful for product applications.
Covalent attachment of the C-terminus of ubiquitin to cellular proteins plays a role in a variety of cellular processes. Ubiquitin C-terminal hydrolysis is catalyzed by deubiquitinating (DUB) enzymes and is necessary for several functions, including liberation of monomeric ubiquitin from the precursors encoded by ubiquitin genes and recycling of ubiquitin monomers. There are 2 distinct families of DUBs, ubiquitin-specific proteases (UBPs) and ubiquitin C-terminal hydrolases (UCHs). Mayer and Wilkinson (1989) identified 4 distinct UCH activities from bovine thymus. All 4 were thiol proteases and had high-affinity binding sites for ubiquitin. Wilkinson et al. (1989) purified the predominant isozyme, UCHL3, and raised antibodies against it. By screening a human B-cell expression library with the antibodies, the authors isolated cDNAs encoding human UCHL3. Sequence comparisons revealed that the sequence of the predicted 230-amino acid human UCHL3 protein is 54% identical to that of UCHL1.
Hu, R.M., et al., Proc. Natl. Acad. Sci. U.S.A. 97(17):9543-9548 (2000).Lai, C.H., et al., Genome Res. 10(5):703-713 (2000).
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