Recombinant Human UbcH7/UBE2L3 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

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Recombinant Human UbcH7/UBE2L3 Protein, CF Summary

Details of Functionality
Recombinant Human UbcH7/UBE2L3 is a member of the Ubiquitin-conjugating (E2) enzyme family that receives Ubiquitin from a Ubiquitin-activating (E1) enzyme and subsequently interacts with a Ubiquitin ligase (E3) to conjugate Ubiquitin to substrate proteins. Reaction conditions will need to be optimized for each specific application. We recommend an initial Recombinant Human UbcH7/UBE2L3 concentration of 0.1-1 μM.
Source
E. coli-derived human UbcH7/UBE2L3 protein
Accession #
Protein/Peptide Type
Recombinant Enzymes
Gene
UBE2L3
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.

Applications/Dilutions

Dilutions
  • Enzyme Activity
Theoretical MW
18 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.
Publications
Read Publications using
E2-640 in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -70 °C as supplied.
  • 3 months, -70 °C under sterile conditions after opening.
Buffer

X mg/ml (X μM) in 50 mM HEPES pH 7.5, 200 mM NaCl, 10% Glycerol (v/v), 1 mM 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 UbcH7/UBE2L3 Protein, CF

  • E2-F1
  • EC 6.3.2.19
  • L-UBC
  • UBCE7
  • UbcH7
  • UBCH7UbcM4
  • UbcM4
  • UBE2L3
  • Ubiquitin carrier protein L3
  • ubiquitin-conjugating enzyme E2 L3
  • Ubiquitin-conjugating enzyme E2-F1
  • ubiquitin-conjugating enzyme E2L 3
  • ubiquitin-conjugating enzyme UBCH7
  • Ubiquitin-protein ligase L3

Background

Ubiquitin-conjugating Enzyme H7 (UbcH7), also known as Ubiquitin-conjugating Enzyme E2L 3 (UBE2L3), is a member of the Ubiquitin-conjugating (E2) enzyme family (1). It has a predicted molecular weight of approximately 18 kDa. The human UbcH7 protein shares 100% amino acid (aa) sequence identity with the mouse and rat orthologs. UbcH7 has an E2 catalytic core domain that contains an active site cysteine residue and comprises 152 of its 154 aa residues. UbcH7 is catalytically active with HECT and RBR domain-containing families of Ubiquitin ligases (E3s) (2,3). UbcH7 localizes to both the nucleus and cytoplasm in human cells. In mice, its ortholog is expressed in many tissues including brain, muscle, heart, lung, lymph node, spleen, thymus, and testis (4,5). UbcH7 depletion results in an extended S phase and a reduced rate of proliferation, suggesting that it may play a role in the cell cycle (6). In humans, single nucleotide polymorphisms in UbcH7 are associated with systemic lupus erythematosus and Crohn's disease, suggesting that UbcH7 is important for proper immune system function (7,8).

 

  1. Nuber, U. et al. (1996) J. Biol. Chem. 271:2795.
  2. Huang, L. et al. (1999) Science 286:1321.
  3. Wenzel, D.M. et al. (2011) Nature 474:105.
  4. Garside, H. et al. (2006) J. Endocrinol. 190:621.
  5. Harbers, K. et al. (1996) Proc. Natl. Acad. Sci. USA 93:12412.
  6. Whitcomb, E.A. et al. (2009) Mol. Biol. Cell 20:1.
  7. Wang, S. et al. (2012) Genes Immun. 13:380.
  8. Fransen, K. et al. (2010) Hum. Mol. Genet. 19:3482.
 

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Publications for UbcH7/UBE2L3 (E2-640)(16)

We have publications tested in 2 confirmed species: Human, N/A.

We have publications tested in 4 applications: Bioassay, Enzyme Assay, Ubiquitination, Ubiquitylation.


Filter By Application
Bioassay
(11)
Enzyme Assay
(1)
Ubiquitination
(1)
Ubiquitylation
(2)
All Applications
Filter By Species
Human
(11)
N/A
(3)
All Species
Showing Publications 1 - 10 of 16. Show All 16 Publications.
Publications using E2-640 Applications Species
S Yoon, K Bogdanov, D Wallach Site-specific ubiquitination of MLKL targets it to endosomes and targets Listeria and Yersinia to the lysosomes Cell Death and Differentiation, 2022;0(0):. 2022 [PMID: 34999730] (Bioassay, Human) Bioassay Human
KP Weston, X Gao, J Zhao, KS Kim, SE Maloney, J Gotoff, S Parikh, YC Leu, KP Wu, M Shinawi, JP Steimel, JS Harrison, JJ Yi Identification of disease-linked hyperactivating mutations in UBE3A through large-scale functional variant analysis Nature Communications, 2021;12(1):6809. 2021 [PMID: 34815418] (Bioassay, Human) Bioassay Human
EG Otten, E Werner, A Crespillo-, KB Boyle, V Dharamdasa, C Pathe, B Santhanam, F Randow Ubiquitylation of lipopolysaccharide by RNF213 during bacterial infection Nature, 2021;0(0):. 2021 [PMID: 34012115] (Ubiquitylation, Human) Ubiquitylation Human
MC Albert, K Brinkmann, W Pokrzywa, SD Günther, M Krönke, T Hoppe, H Kashkar CHIP ubiquitylates NOXA and induces its lysosomal degradation in response to DNA damage Cell Death & Disease, 2020;11(9):740. 2020 [PMID: 32913203] (Ubiquitylation, Human) Ubiquitylation Human
M Gatti, R Imhof, Q Huang, M Baudis, M Altmeyer The Ubiquitin Ligase TRIP12 Limits PARP1 Trapping and Constrains PARP Inhibitor Efficiency Cell Rep, 2020;32(5):107985. 2020 [PMID: 32755579] (Bioassay, Human) Bioassay Human
Q Yin, T Han, B Fang, G Zhang, C Zhang, ER Roberts, V Izumi, M Zheng, S Jiang, X Yin, M Kim, J Cai, EB Haura, JM Koomen, KSM Smalley, L Wan K27-linked ubiquitination of BRAF by ITCH engages cytokine response to maintain MEK-ERK signaling Nat Commun, 2019;10(1):1870. 2019 [PMID: 31015455] (Ubiquitination, Human) Ubiquitination Human
M Bosshard, R Aprigliano, C Gattiker, V Palibrk, E Markkanen, P Hoff Backe, S Pellegrino, FL Raymond, G Froyen, M Altmeyer, M Bjørås, GL Dianov, B van Loon Impaired oxidative stress response characterizes HUWE1-promoted X-linked intellectual disability Sci Rep, 2017;7(1):15050. 2017 [PMID: 29118367] (Bioassay, Human) Bioassay Human
ME French, JL Klosowiak, A Aslanian, SI Reed, JR Yates, T Hunter Mechanism of Ubiquitin Chain Synthesis Employed by a HECT Ubiquitin Ligase J. Biol. Chem., 2017;0(0):. 2017 [PMID: 28461335] (Bioassay) Bioassay
X Zhang, B Li, AH Rezaeian, X Xu, PC Chou, G Jin, F Han, BS Pan, CY Wang, J Long, A Zhang, CY Huang, FJ Tsai, CH Tsai, C Logothetis, HK Lin H3 ubiquitination by NEDD4 regulates H3 acetylation and tumorigenesis Nat Commun, 2017;8(0):14799. 2017 [PMID: 28300060] (Bioassay, N/A) Bioassay N/A
S He, Y Cao, P Xie, G Dong, L Zhang The Nedd8 Non-covalent Binding Region in the Smurf HECT Domain is Critical to its Ubiquitn Ligase Function Sci Rep, 2017;7(0):41364. 2017 [PMID: 28169289] (Bioassay, Human) Bioassay Human
Show All 16 Publications.

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Bioinformatics

Gene Symbol UBE2L3
Uniprot