Recombinant Human UbcH5b/UBE2D2 Protein, CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

Order Details

Recombinant Human UbcH5b/UBE2D2 Protein, CF Summary

Details of Functionality
Recombinant Human UbcH5b/UBE2D2 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 UbcH5b/UBE2D2 concentration of 0.1-1 μM.
Source
E. coli-derived human UbcH5b/UBE2D2 protein
Accession #
Protein/Peptide Type
Recombinant Enzymes
Gene
UBE2D2
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain

Applications/Dilutions

Dilutions
  • Enzyme Activity
Theoretical MW
17 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
E2-622 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 UbcH5b/UBE2D2 Protein, CF

  • E2(17)KB2
  • EC 6.3.2.19
  • PUBC1
  • UBC4/5
  • UBC4ubiquitin-conjugating enzyme E2D 2 (homologous to yeast UBC4/5)
  • UBC5B
  • UBCH4
  • UbcH5b
  • UBE2D2
  • Ubiquitin carrier protein D2
  • ubiquitin-conjugating enzyme E2 D2
  • Ubiquitin-conjugating enzyme E2(17)KB 2
  • Ubiquitin-conjugating enzyme E2-17 kDa 2
  • ubiquitin-conjugating enzyme E2D 2 (UBC4/5 homolog, yeast)
  • Ubiquitin-protein ligase D2

Background

Ubiquitin-conjugating Enzyme H5b (UbcH5b), also known as Ubiquitin-conjugating Enzyme E2D 2 (UBE2D2), is a widely expressed member of the Ubiquitin-conjugating (E2) enzyme family (1). The protein has a predicted molecular weight of 16.5 kDa. UbcH5b/UBE2D2 localizes to both the nucleus and the cytoplasm (2). The human protein shares 100% and 92% amino acid sequence identity with the mouse and rat orthologs, respectively. This enzyme has an E2 catalytic core domain that contains an active site cysteine residue that is required for the formation of a thioester bond with Ubiquitin (3). UbcH5b/UBE2D2 is capable of mediating the formation of Ubiquitin chains linked through Lys11, Lys48, or Lys63 (4). Working with the SCF(Fbxw2) and MDM2/HDM2 Ubiquitin ligases (E3s), UbcH5b/UBE2D2 mediates the ubiquitination and degradation of the transcription factors GCM1 and p53, respectively (5-7). Along with UBE2N/Ubc13, UbcH5b/UBE2D2 may have a role in the endocytosis and endolysosomal degradation of MHC class I molecules (8). Non-proteolytic ubiquitination of TRIM5-alpha by UbcH5b/UBE2D2 has been reported to block HIV reverse transcription (9). Pathologically, UBE2D family members may be critical targets of cadmium during cadmium-induced renal toxicity (10). Additionally, overexpression of UbcH5b/UBE2D2 has been linked to inflammatory bowel disease (11).

  1. Jensen, J.P. et al. (1995) J. Biol. Chem. 270:30408.
  2. Umebayashi, K. et al. (2008) Mol. Biol. Cell 19:3454.
  3. Hershko, A. et al. (1983) J. Biol. Chem. 258:8206.
  4. Ordureau, A. et al. (2008) Biochem. J. 409:43.
  5. Chiang, M.H. et al. (2008) Biol. Reprod. 79:914.
  6. Saville, M.K. et al. (2004) J. Biol. Chem. 279:42169.
  7. Iyappan, S. et al. (2010) J. Biol. Chem. 285:33065.
  8. Duncan, L.M. et al. (2006) EMBO J. 25:1635.
  9. Yamauchi, K. et al. (2008) FEBS J. 275:1540.
  10. Tokumoto, M. et al. (2011) J. Toxicol. Sci. 36:191.
  11. Hetzenecker, A.M. et al. (2012) Digestion 86:34.

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Publications for UbcH5b/UBE2D2 (E2-622)(36)

We have publications tested in 4 confirmed species: Human, Mouse, Escherichia coli, N/A.

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


Filter By Application
Bioassay
(27)
Enzyme Assay
(1)
Ubiquitination
(5)
Ubiquitylation
(2)
All Applications
Filter By Species
Human
(20)
Mouse
(1)
Escherichia coli
(1)
N/A
(8)
All Species
Showing Publications 1 - 10 of 36. Show All 36 Publications.
Publications using E2-622 Applications Species
Y Zhou, R Zheng, S Liu, C Disoma, A Du, S Li, Z Chen, Z Dong, Y Zhang, S Li, P Liu, A Razzaq, X Chen, Y Liao, S Tao, Y Liu, L Xu, Q Zhang, J Peng, X Deng, S Li, T Jiang, Z Xia Host E3 ligase HUWE1 attenuates the pro-apoptotic activity of the MERS-CoV accessory protein ORF3 by promoting its ubiquitin-dependent degradation The Journal of Biological Chemistry, 2022;0(0):101584. 2022 [PMID: 35032548] (Bioassay, Human) Bioassay Human
H Zhou, MS Zaher, JC Walter, A Brown Structure of CRL2Lrr1, the E3 ubiquitin ligase that promotes DNA replication termination in vertebrates Nucleic Acids Research, 2021;0(0):. 2021 [PMID: 34850944] (Bioassay, Human) Bioassay Human
H Zhou, MS Zaher, JC Walter, A Brown Structure of CRL2Lrr1, the E3 ubiquitin ligase that promotes DNA replication termination in vertebrates Nucleic Acids Research, 2021;49(22):13194-13206. 2021 [PMID: 34850944] (Ubiquitylation, N/A) Ubiquitylation N/A
Y Liu, C Qin, Y Rao, C Ngo, JJ Feng, J Zhao, S Zhang, TY Wang, J Carriere, AC Savas, M Zarinfar, S Rice, H Yang, W Yuan, JA Camarero, J Yu, XS Chen, C Zhang, P Feng SARS-CoV-2 Nsp5 Demonstrates Two Distinct Mechanisms Targeting RIG-I and MAVS To Evade the Innate Immune Response MBio, 2021;0(0):e0233521. 2021 [PMID: 34544279] (Bioassay, Escherichia coli) Bioassay Escherichia coli
G Kokic, FR Wagner, A Chernev, H Urlaub, P Cramer Structural basis of human transcription-DNA repair coupling Nature, 2021;0(0):. 2021 [PMID: 34526721] (Bioassay, Human) Bioassay Human
MC Liebl, J Moehlenbri, H Becker, G Raddatz, SK Abdeen, RI Aqeilan, F Lyko, TG Hofmann DAZAP2 acts as specifier of the p53 response to DNA damage Nucleic Acids Research, 2021;0(0):. 2021 [PMID: 33591310] (Ubiquitination, Human) Ubiquitination 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
AM Cathcart, GH Bird, TE Wales, HD Herce, EP Harvey, ZJ Hauseman, CE Newman, U Adhikary, MS Prew, T Oo, S Lee, JR Engen, LD Walensky Targeting a helix-in-groove interaction between E1 and E2 blocks ubiquitin transfer Nat. Chem. Biol., 2020;0(0):. 2020 [PMID: 32807965] (Bioassay, Human) Bioassay Human
AM Cathcart, GH Bird, TE Wales, HD Herce, EP Harvey, ZJ Hauseman, CE Newman, U Adhikary, MS Prew, T Oo, S Lee, JR Engen, LD Walensky Targeting a helix-in-groove interaction between E1 and E2 blocks ubiquitin transfer Nat. Chem. Biol., 2020;0(0):. 2020 [PMID: 32807965] (Bioassay, N/A) Bioassay N/A
CR Kim, T Noda, H Kim, G Kim, S Park, Y Na, S Oura, K Shimada, I Bang, JY Ahn, YR Kim, SK Oh, HJ Choi, JS Kim, I Jung, H Lee, Y Okada, M Ikawa, SH Baek PHF7 Modulates BRDT Stability and Histone-to-Protamine Exchange during Spermiogenesis Cell Rep, 2020;32(4):107950. 2020 [PMID: 32726616] (Bioassay, Mouse) Bioassay Mouse
Show All 36 Publications.

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Bioinformatics

Gene Symbol UBE2D2
Uniprot