Recombinant Human UCH-L3 Protein, CF

• Reactivity: Hu
• Applications: Enzyme Activity
• Format: Carrier-Free

Recombinant Human UCH-L3 Protein, CF Summary

• Additional Information: Will be discontinued when existing inventory is gone.
• Details of Functionality: Reaction conditions will need to be optimized for each specific application. We recommend an initial Recombinant Human UCH-L3 concentration of 0.05-5 nM. Pre-incubation for 15 minutes with 10 mM DTT is recommended to achieve maximum activity.
• Source: E. coli-derived human UCH-L3 protein
  Met1 - Ala230
• Accession #: P15374.1
• Protein/Peptide Type: Recombinant Enzymes
• Gene: UCHL3
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.

Applications/Dilutions

• Dilutions:
  • Enzyme Activity
• Theoretical MW: 26 kDa.
  Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
• Buffer: Supplied as a solution in HEPES, NaCl and TCEP.
• Purity: >95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human UCH-L3 Protein, CF

• EC 3.4.19.12
• ubiquitin carboxyl-terminal esterase L3 (ubiquitin thiolesterase)
• ubiquitin carboxyl-terminal hydrolase isozyme L3
• Ubiquitin Thioesterase L3
• ubiquitin thiolesterase
• UCHL3
• UCH-L3

Background

Ubiquitin Carboxyl-terminal Esterase L3 (UCH-L3) is a member of the peptidase C12 family of deubiquitinating enzymes. It is widely expressed with the highest levels being observed in heart, testis, thymus and striated muscle (1,2). UCH-L3 is 230 amino acids (aa) in length with a predicted molecular weight of 26.2 kDa (3). It is composed of a single N-terminal UCH domain with a short active-site crossover loop allowing UCH-L3 to process small Ubiquitin derivatives (4,5). Human UCH-L3 shares 98% aa sequence identity with the mouse and rat orthologs. UCH-L3 releases monomeric Ubiquitin from Ubiquitin-protein conjugates (4). Additionally, it cleaves a GGLRQ peptide from the C-terminus of the Ubiquitin-like protein NEDD8, allowing NEDD8 to be conjugated to target proteins (2). UCH-L3 activity is muted in the presence of Ubiquitin dimers (6). UCH-L3 is suggested to function in the central nervous system. In particular, it is involved in the maintenance of neurons of the gracile tract, nucleus tractus solitaris, and area postrema, and in working memory (7,8). UCH-L3 has also been shown to modulate germ cell apoptosis and promote insulin signaling and adipogenesis (9,10). Additionally, UCH-L3 expression has been shown to be correlated with cancer (11-13).

1. Kurihara, L.J. et al. (2000) Mol. Cell. Biol. 20:2498.
2. Wada, H. et al. (1998) Biochem. Biophys. Res. Commun. 251:688.
3. Wilkinson, K.D. et al. (1989) Science 246:670.
4. Larsen, C.N. et al. (1998) Biochemistry 37:3358.
5. Zhou, Z.R. et al. (2012) Biochem. J. 441:143.
6. Setsuie, R. et al. (2009) Neurochem. Int. 54:314.
7. Kurihara, L.J. et al. (2001) Hum. Mol. Genet. 10:1963.
8. Wood, M.A. et al. (2005) Hippocampus 15:610.
9. Kwon, J. (2007) Exp. Anim. 56:71.
10. Suzuki, M. et al. (2009) Endocrinology 150:5230.
11. Nam, M.J. et al. (2003) Proteomics 3:2108.
12. Miyoshi, Y. et al. (2006) Cancer Sci. 97:523.
13. Fang, Y. et al. (2012) Mol. Cell. Biochem. 359:59.

Publications for UCH-L3 (E-325)(4)

Publications using E-325

• Sato, H;Ito, T;Hayashi, T;Kitano, S;Erdjument-Bromage, H;Bott, MJ;Toyooka, S;Zauderer, M;Ladanyi, M; The BAP1 nuclear deubiquitinase is involved in the nonhomologous end-joining pathway of double-strand DNA repair through interaction with DNA-PK Oncogene 2024-02-21 [PMID: 38383726] (Bioassay, N/A)
• ZJ Su, JS Cao, YF Wu, WN Chen, X Lin, YL Wu, X Lin Deubiquitylation of hepatitis B virus X protein (HBx) by ubiquitin-specific peptidase 15 (USP15) increases HBx stability and its transactivation activity Sci Rep, 2017-01-11;7(0):40246. 2017-01-11 [PMID: 28074857] (Ubiquitination)
• Neerav N Shukla Proteasome addiction defined in Ewing's sarcoma is effectively targeted by a novel class of 19S proteasome inhibitors Cancer Res, 2016-06-02;0(0):. 2016-06-02 [PMID: 27256563] (Bioassay, Human)
• Liang , Qin, Dexheimer , Thomas S, Zhang , Ping, Rosenthal , Andrew S, Villamil , Mark A, You , Changjun, Zhang , Qiuting, Chen , Junjun, Ott , Christin, Sun , Hongmao, Luci , Diane K, Yuan , Bifeng, Simeonov , Anton, Jadhav , Ajit, Xiao , Hui, Wang , Yinsheng, Maloney , David J, Zhuang , Zhihao A selective USP1-UAF1 inhibitor links deubiquitination to DNA damage responses. Nat Chem Biol, 2014-02-16;10(4):298-304. 2014-02-16 [PMID: 24531842] (Bioassay)

Bioinformatics

• Gene Symbol: UCHL3
• Uniprot:
  • P15374.1()