Recombinant Human/Mouse/Rat UbcH7/UBE2L3 Protein, CF


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Product Details

Reactivity Hu, Mu, RtSpecies Glossary
Applications Enzyme Activity

Order Details

Recombinant Human/Mouse/Rat 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.
E. coli-derived UbcH7/UBE2L3 protein
Met1 - Met154
Accession #
Protein/Peptide Type
Recombinant Enzymes
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.


  • 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.
Read Publications using
E2-640 in the following applications:

Packaging, Storage & Formulations

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.
Supplied as a solution in HEPES, NaCl, TCEP and Glycerol.
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.


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

Alternate Names for Recombinant Human/Mouse/Rat UbcH7/UBE2L3 Protein, CF

  • E2-F1
  • EC
  • 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


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)(21)

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
Enzyme Assay
All Applications
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All Species
Showing Publications 1 - 10 of 21. Show All 21 Publications.
Publications using E2-640 Applications Species
Chuong, P;Statsyuk, A; Selective Smurf1 E3 ligase inhibitors that prevent transthiolation bioRxiv : the preprint server for biology 2023-10-14 [PMID: 37873387] (Bioassay, N/A) Bioassay N/A
Ardah, MT;Radwan, N;Khan, E;Kitada, T;Haque, ME; Parkin Precipitates on Mitochondria via Aggregation and Autoubiquitination International journal of molecular sciences 2023-05-19 [PMID: 37240373] (Bioassay, N/A) Bioassay N/A
X Du, J Pang, B Gu, T Si, Y Chang, T Li, M Wu, Z Wang, Y Wang, J Feng, N Wu, J Man, H Li, A Li, T Zhang, B Wang, X Duan A bio-orthogonal linear ubiquitin probe identifies STAT3 as a direct substrate of OTULIN in glioblastoma Nucleic Acids Research, 2023-02-22;0(0):. 2023-02-22 [PMID: 36660824] (Bioassay, N/A) Bioassay N/A
C Yan, H Yang, P Su, X Li, Z Li, D Wang, Y Zang, T Wang, Z Liu, Z Bao, S Dong, T Zhuang, J Zhu, Y Ding OTUB1 suppresses Hippo signaling via modulating YAP protein in gastric cancer Oncogene, 2022-10-21;0(0):. 2022-10-21 [PMID: 36271031] (Bioassay, Human) Bioassay Human
SK Pirooznia, H Wang, N Panicker, M Kumar, S Neifert, MA Dar, E Lau, BG Kang, J Redding-Oc, JC Troncoso, VL Dawson, TM Dawson Deubiquitinase CYLD acts as a negative regulator of dopamine neuron survival in Parkinson's disease Science Advances, 2022-04-01;8(13):eabh1824. 2022-04-01 [PMID: 35363524] (Bioassay, N/A) Bioassay N/A
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, 2022-01-09;0(0):. 2022-01-09 [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, 2021-11-23;12(1):6809. 2021-11-23 [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, 2021-05-19;0(0):. 2021-05-19 [PMID: 34012115] (Bioassay, N/A) Bioassay N/A
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, 2020-09-10;11(9):740. 2020-09-10 [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, 2020-08-04;32(5):107985. 2020-08-04 [PMID: 32755579] (Bioassay, Human) Bioassay Human
Show All 21 Publications.

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Gene Symbol UBE2L3