Recombinant Human Ubiquitin Activating Enzyme (UBE1), CF


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Product Details

Reactivity HuSpecies Glossary
Applications Enzyme Activity

Order Details

Recombinant Human Ubiquitin Activating Enzyme (UBE1), CF Summary

Details of Functionality
Recombinant Human Ubiquitin Activating Enzyme (UBE1) is a member of the Ubiquitin-activating (E1) enzyme family that is required for the first step of the enzymatic cascade that subsequently utilizes a Ubiquitin-conjugating (E2) enzyme and 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 Ubiquitin Activating Enzyme (UBE1) concentration of 50-200 nM.
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human Ubiquitin-activating Enzyme/UBE1 protein
Accession #
Protein/Peptide Type
Recombinant Enzymes
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.


Theoretical MW
118 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
E-305 in the following applications:

Packaging, Storage & Formulations

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.
X mg/ml (X μM) in 50 mM HEPES pH 8.0, 50 mM NaCl, 1 mM TCEP
>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 Ubiquitin Activating Enzyme (UBE1), CF

  • A1S9T and BN75 temperature sensitivity complementing
  • A1S9T
  • A1ST
  • AMCX1
  • GXP1
  • MGC4781
  • POC20 centriolar protein homolog
  • POC20
  • Protein A1S9
  • SMAX2
  • UBA1
  • UBA1, ubiquitin-activating enzyme E1 homolog A
  • UBA1A
  • UBE1
  • UBE1A1S9
  • UBE1X
  • ubiquitin-activating enzyme E1 (A1S9T and BN75 temperature sensitivitycomplementing)
  • Ubiquitin-activating enzyme E1
  • Ubiquitinactivating Enzyme
  • Ubiquitin-activating Enzyme
  • ubiquitin-like modifier activating enzyme 1
  • ubiquitin-like modifier-activating enzyme 1


Ubiquitin-activating Enzyme (UBE1), also known as Ubiquitin-like Modifier Activating Enzyme 1 (UBA1), is a 1058 amino acid (aa) canonical member of the Ubiquitin-activating (E1) enzyme family of proteins with a predicted molecular weight of 118 kDa.  It is ubiquitously expressed and highly conserved; mouse and rat UBE1 share 95% and 96% aa sequence identity with the human UBE1 protein, respectively. UBE1 is found in the cytoplasm and nucleus, and contains a conserved active-site cysteine residue and ATP-binding site common to E1 enzymes (1-3). UBE1 is responsible for the first step in Ubiquitin-protein isopeptide bond formation (4,5). Ubiquitin is activated by UBE1 and thereafter linked to the side chain of a cysteine residue in UBE1, Cys632 in humans, yielding a Ubiquitin-UBE1 conjugate via a thioester bond (5-8). The activated Ubiquitin is then transferred to a lysine residue on the target protein via the Ubiquitin-conjugating  – Ubiquitin ligase enzyme cascade. UBE1 is required for cell cycle progression and has been linked to cellular responses to DNA damage such as nucleotide excision repair (3,9,10). Mutations in UBE1 are associated with X-linked lethal infantile spinal muscular atrophy (11).  UBE1 is a critical component for the initiation of in vitro ubiquitin conjugation reactions.   

  1. Handley, P.M. et al. (1991) Proc. Natl. Acad. Sci. USA 88:258.
  2. Nagai, Y. et al. (1995) J. Cell Sci. 108:2145.
  3. Stephen, A.G. et al. (1996) J. Biol. Chem. 271:15608.
  4. Hershko, A. et al. (1983) J. Biol. Chem. 258:8206.
  5. Schulman, B.A. & J.W. Harper (2009) Nat. Rev. Mol. Cell Biol. 10:319.
  6. Haas, A.L. et al. (1982) J. Biol. Chem. 257:2543.
  7. Haas, A.L. & I.A. Rose (1982) J. Biol. Chem. 257:10329.
  8. Pickart, C.M. et al. (1994) J. Biol. Chem. 269:7115.
  9. Nouspikel, T. & P.C. Hanawalt (2006) Proc. Natl. Acad. Sci. USA 103:16188.
  10. Moundry, P. et al. (2012) Cell Cycle 11:1573.
  11. Ramser, J. et al. (2008) Am. J. Hum. Genet. 82:188.

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Publications for Ubiquitin-activating Enzyme/UBE1 (E-305)(83)

We have publications tested in 7 confirmed species: Human, Mouse, Amoeba - Entamoeba histolytica, Bacteria - E. Coli, N/A, Virus - HPV, Worm - Spodoptera frugiperda (Fall Army Worm).

We have publications tested in 3 applications: Bioassay, Enzyme Assay, Ubiquitination.

Filter By Application
Enzyme Assay
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Filter By Species
Amoeba - Entamoeba histolytica
Bacteria - E. Coli
Virus - HPV
Worm - Spodoptera frugiperda (Fall Army Worm)
All Species
Showing Publications 1 - 10 of 83. Show All 83 Publications.
Publications using E-305 Applications Species
YS Yoo, YJ Park, HS Lee, NTK Oanh, MY Cho, J Heo, ES Lee, H Cho, YY Park, H Cho Mitochondria ubiquitin ligase, MARCH5 resolves hepatitis B virus X protein aggregates in the liver pathogenesis Cell Death Dis, 2019;10(12):938. 2019 [PMID: 31819032] (Bioassay, Human) Bioassay Human
TC Ting, M Goralski, K Klein, B Wang, J Kim, Y Xie, D Nijhawan Aryl Sulfonamides Degrade RBM39 and RBM23 by Recruitment to CRL4-DCAF15 Cell Rep, 2019;29(6):1499-1510.e6. 2019 [PMID: 31693891] (Bioassay, Human) Bioassay Human
J Sitz, SA Blanchet, SF Gameiro, E Biquand, TM Morgan, M Galloy, J Dessapt, EG Lavoie, A Blondeau, BC Smith, JS Mymryk, CA Moody, A Fradet-Tur Human papillomavirus E7 oncoprotein targets RNF168 to hijack the host DNA damage response Proc. Natl. Acad. Sci. U.S.A., 2019;116(39):19552-19562. 2019 [PMID: 31501315] (Bioassay, Virus - HPV) Bioassay Virus - HPV
RM Vaughan, SB Rothbart, BM Dickson The finger loop of the SRA domain in the E3 ligase UHRF1 is a regulator of ubiquitin targeting and is required for maintaining�DNA methylation J. Biol. Chem., 2019;0(0):. 2019 [PMID: 31481468] (Bioassay, Human) Bioassay Human
P Wang, F Yan, Z Li, Y Yu, SE Parnell, Y Xiong Impaired plasma membrane localization of ubiquitin ligase complex underlies 3-M syndrome development J. Clin. Invest., 2019;130(0):. 2019 [PMID: 31343991] (Bioassay, Human) Bioassay Human
P Ma, NN Song, Y Li, Q Zhang, L Zhang, L Zhang, Q Kong, L Ma, X Yang, B Ren, C Li, X Zhao, Y Li, Y Xu, X Gao, YQ Ding, B Mao Fine-Tuning of Shh/Gli Signaling Gradient by Non-proteolytic Ubiquitination during Neural Patterning Cell Rep, 2019;28(2):541-553.e4. 2019 [PMID: 31291587] (Bioassay) Bioassay
F Liang, AS Miller, S Longerich, C Tang, D Maranon, EA Williamson, R Hromas, C Wiese, GM Kupfer, P Sung DNA requirement in FANCD2 deubiquitination by USP1-UAF1-RAD51AP1 in the Fanconi anemia DNA damage response Nat Commun, 2019;10(1):2849. 2019 [PMID: 31253762] (Bioassay, Human) Bioassay Human
M Di Rienzo, M Antonioli, C Fusco, Y Liu, M Mari, I Orhon, G Refolo, F Germani, M Corazzari, A Romagnoli, F Ciccosanti, B Mandriani, MT Pellico, R De La Torr, H Ding, M Dentice, M Neri, A Ferlini, F Reggiori, M Kulesz-Mar, M Piacentini, G Merla, GM Fimia Autophagy induction in atrophic muscle cells requires ULK1 activation by TRIM32 through unanchored K63-linked polyubiquitin chains Sci Adv, 2019;5(5):eaau8857. 2019 [PMID: 31123703] (Ubiquitination, Human) Ubiquitination 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
MCJ Yip, AFA Keszei, Q Feng, V Chu, MJ McKenna, S Shao Mechanism for recycling tRNAs on stalled ribosomes Nat. Struct. Mol. Biol., 2019;0(0):. 2019 [PMID: 31011209] (Ubiquitination, Human) Ubiquitination Human
Show All 83 Publications.

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Gene Symbol UBA1