Recombinant Human UCH-L3 Protein, CF

Please inquire regarding future lot manufacture; Will be discontinued when existing inventory is gone.

Catalog # Availability Size / Price Qty
E-325-025
R&D Systems Recombinant Proteins and Enzymes
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Product Details
Citations (3)
FAQs
Reviews

Recombinant Human UCH-L3 Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.
Activity
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 #
Predicted Molecular Mass
26 kDa

Product Datasheets

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E-325

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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-325

Formulation Supplied as a solution in HEPES, NaCl and TCEP.
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.
  • 6 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
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Background: UCH-L3

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).

References
  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.
Long Name
Ubiquitin C-terminal Hydrolase L3
Entrez Gene IDs
7347 (Human); 50933 (Mouse); 114094 (Rat); 100350137 (Rabbit)
Alternate Names
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

Citations for Recombinant Human UCH-L3 Protein, CF

R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.

3 Citations: Showing 1 - 3
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  1. Deubiquitylation of hepatitis B virus X protein (HBx) by ubiquitin-specific peptidase 15 (USP15) increases HBx stability and its transactivation activity
    Authors: ZJ Su, JS Cao, YF Wu, WN Chen, X Lin, YL Wu, X Lin
    Sci Rep, 2017-01-11;7(0):40246.
    Applications: Ubiquitination
  2. Proteasome addiction defined in Ewing's sarcoma is effectively targeted by a novel class of 19S proteasome inhibitors
    Authors: Neerav N Shukla
    Cancer Res, 2016-06-02;0(0):.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay
  3. A selective USP1-UAF1 inhibitor links deubiquitination to DNA damage responses.
    Authors: 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
    Nat Chem Biol, 2014-02-16;10(4):298-304.
    Applications: Bioassay

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