Recombinant Human Ubiquitin Activating Enzyme (UBE1), CF

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications Enzyme Activity
Format
Carrier-Free

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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.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived human Ubiquitin-activating Enzyme/UBE1 protein
Accession #
Protein/Peptide Type
Recombinant Enzymes
Gene
UBA1
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by Colloidal Coomassie® Blue stain.

Applications/Dilutions

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.
Publications
Read Publications using
E-305 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 8.0, 50 mM NaCl, 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 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

Background

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)(63)

We have publications tested in 6 confirmed species: Human, Mouse, Amoeba - Entamoeba histolytica, Bacteria - E. Coli, N/A, Spodoptera frugiperda - Fall Army Worm.

We have publications tested in 6 applications: Bioassay, EnzAct, Enzyme Assay, Ubiquination, Ubiquitination, enzymatic assay.


Filter By Application
Bioassay
(53)
EnzAct
(2)
Enzyme Assay
(2)
Ubiquination
(1)
Ubiquitination
(4)
enzymatic assay
(1)
All Applications
Filter By Species
Human
(32)
Mouse
(1)
Amoeba - Entamoeba histolytica
(1)
Bacteria - E. Coli
(1)
N/A
(15)
Spodoptera frugiperda - Fall Army Worm
(1)
All Species
Showing Publications 1 - 10 of 63. Show All 63 Publications.
Publications using E-305 Applications Species
F Lampert, D Stafa, A Goga, MV Soste, S Gilberto, N Olieric, P Picotti, M Stoffel, M Peter The multi-subunit GID/CTLH E3 ubiquitin ligase promotes cell proliferation and targets the transcription factor Hbp1 for degradation Elife, 2018;7(0):. 2018 [PMID: 29911972] (Bioassay, Human) Bioassay Human
S Ito, A Ueno, T Ueda, H Nakagawa, H Taniguchi, N Kayukawa, A Fujihara-I, F Hongo, K Okihara, O Ukimura CNPY2 inhibits MYLIP-mediated AR protein degradation in prostate cancer cells Oncotarget, 2018;9(25):17645-17655. 2018 [PMID: 29707137] (Bioassay) Bioassay
GS Hewawasam, K Dhatchinam, M Mattingly, C Seidel, JL Gerton Chromatin assembly factor-1 (CAF-1) chaperone regulates Cse4 deposition into chromatin in budding yeast Nucleic Acids Res., 2018;0(0):. 2018 [PMID: 29522205] (Bioassay, Human) Bioassay Human
Y Cho, HG Kang, SJ Kim, S Lee, S Jee, SG Ahn, MJ Kang, JS Song, JY Chung, EC Yi, KH Chun Post-translational modification of OCT4 in breast cancer tumorigenesis Cell Death Differ., 2018;0(0):. 2018 [PMID: 29511337] (Bioassay, Human) Bioassay Human
L Zheng, SD Conner PI5P4K? functions in DTX1-mediated Notch signaling Proc. Natl. Acad. Sci. U.S.A., 2018;0(0):. 2018 [PMID: 29440432] (Bioassay, Human) Bioassay Human
SY Kim, HJ Kim, HJ Kim, DH Kim, CH Kim, JH Han, HK Byeon, K Lee HSPA5 negatively regulates lysosomal activity through ubiquitination of MUL1 in head and neck cancer Autophagy, 2017;0(0):1-89. 2017 [PMID: 29260979] (Bioassay, Human) Bioassay Human
JR Brickner, JM Soll, PM Lombardi, CB Vågbø, MC Mudge, C Oyeniran, R Rabe, J Jackson, ME Sullender, E Blazosky, AK Byrum, Y Zhao, MA Corbett, J Gécz, M Field, A Vindigni, G Slupphaug, C Wolberger, N Mosammapar A ubiquitin-dependent signalling axis specific for ALKBH-mediated DNA dealkylation repair Nature, 2017;551(7680):389-393. 2017 [PMID: 29144457] (Bioassay, Human) Bioassay Human
Y Kopp, WH Lang, TB Schuster, A Martínez-L, HF Hofbauer, R Ernst, G Calloni, RM Vabulas CHIP as a membrane-shuttling proteostasis sensor Elife, 2017;6(0):. 2017 [PMID: 29091030] (Bioassay, Human) Bioassay Human
N Lian, X Liu, X Wang, Y Zhou, H Li, J Li, T Mao COP1 mediates dark-specific degradation of microtubule-associated protein WDL3 in regulating Arabidopsis hypocotyl elongation Proc. Natl. Acad. Sci. U.S.A., 2017;114(46):12321-12326. 2017 [PMID: 29087315] (Bioassay, Human) Bioassay Human
Q Ma, H Ruan, L Peng, M Zhang, MU Gack, WD Yao Proteasome-independent polyubiquitin linkage regulates synapse scaffolding, efficacy, and plasticity Proc. Natl. Acad. Sci. U.S.A., 2017;0(0):. 2017 [PMID: 28973854] (Bioassay, Human) Bioassay Human
Show All 63 Publications.

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Bioinformatics

Gene Symbol UBA1
Entrez
Uniprot