Recombinant Mouse His6-UCH-L1/PGP9.5 Protein, CF
Recombinant Mouse His6-UCH-L1/PGP9.5 Protein, CF Summary
Product Specifications
Contains a 6-His tag
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
E-335
| Formulation | X mg/ml (X μM) in 50 mM HEPES, pH 8.0, 2 mM DTT |
| Shipping | The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: UCH-L1/PGP9.5
Ubiquitin Carboxyl-terminal Esterase L1 (UCH-L1), also known as PGP 9.5, is a deubiquitinating enzyme with a predicted molecular weight of 25 kDa (1). The human protein shares 95% amino acid sequence identity with its mouse and rat orthologs. UCH-L1 is expressed abundantly in neurons, accounting for 1-2% of total soluble proteins in the brain (2). It localizes primarily to the cytoplasm, but a subpopulation has been shown to be transiently nuclear (3,4). UCH-L1 contains two catalytic residues, Cys90 and His161, which are required for isopeptide bond cleavage at the C-terminal glycine residue of Ubiquitin (5). The levels of free Ubiquitin appear to be partially regulated by UCH-L1 through the hydrolysis of small Ubiquitin chains and the stabilization of monomeric Ubiquitin (6). Mice lacking functional UCH-L1 show neuronal dysfunction and neurodegeneration, and mutations in this enzyme have been linked to Parkinson's disease, suggesting that it is important for proper central nervous system function (7,8). UCH-L1 also likely plays a complex role in cancer. It has been reported to function as an oncogene in lymphoma, colorectal cancer, and nonsmall cell lung carcinoma (9-11). In contrast, it is thought to function as a tumor suppressor protein in nasopharyngeal and breast cancers (12,13).
- Wilkinson, K.D. et al. (1989) Science 246:670.
- Solano, S.M. et al. (2000) Ann. Neurol. 47:201.
- Henderson, M.J. et al. (2010) J. Biol. Chem. 285:11314.
- Bheda, A. et al. (2010) Cell Cycle 9:980.
- Larsen, C.N. et al. (1996) Biochemistry 35:6735.
- Walters, B.J. et al. (2008) Mol. Cell. Neurosci. 39:539.
- Sakurai, M. et al. (2008) Eur. J. Neurosci. 27:691.
- Andersson, F.I. et al. (2011) J. Mol. Biol. 407:261.
- Hussain, S. et al. (2010) Leukemia 24:1641.
- Akishima-Fukasawa, Y. et al. (2010) Am. J. Clin. Pathol. 134:71.
- Kim, H.J. et al. (2009) Oncogene 28:117.
- Li, L. et al. (2010) Clin. Cancer Res. 16:2949.
- Xiang, T. et al. (2012) PLoS One 7:e29783.
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