Recombinant S. cerevisiae SAE2 / UBA2 protein (ab80727)

Overview

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • Accession856310
    • SpeciesSaccharomyces cerevisiae

Specifications

Our Abpromise guarantee covers the use of ab80727 in the following tested applications.

The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.

  • Applications

    Conjugation

    SDS-PAGE

  • Purity> 90 % SDS-PAGE.

  • FormLyophilised
  • Additional notes

    Typical enzyme concentration to support conjugation in vitro is 50-200 nM depending on conditions.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on dry ice. Upon delivery aliquot and store at -80ºC. Avoid freeze / thaw cycles.

    Preservative: None
    Constituents: 50mM HEPES, 150mM Sodium chloride, pH 8.0

General Info

  • Alternative names
    • Anthracycline associated resistance ARX
    • Anthracycline-associated resistance ARX
    • ARX
    • FLJ13058
    • HRIHFB2115
    • SAE 2
    • SAE2
    • SAE2_HUMAN
    • SUMO 1 activating enzyme subunit 2
    • SUMO activating enzyme subunit 2
    • SUMO-activating enzyme subunit 2
    • UBA2
    • UBA2 ubiquitin activating enzyme E1 homolog
    • Ubiquitin like 1 activating enzyme E1B
    • Ubiquitin like modifier activating enzyme 2
    • Ubiquitin-like 1-activating enzyme E1B
    • UBLE1B
    see all
  • FunctionThe heterodimer acts as a E1 ligase for SUMO1, SUMO2, SUMO3, and probably SUMO4. It mediates ATP-dependent activation of SUMO proteins followed by formation of a thioester bond between a SUMO protein and a conserved active site cysteine residue on UBA2/SAE2.
  • PathwayProtein modification; protein sumoylation.
  • Sequence similaritiesBelongs to the ubiquitin-activating E1 family.
  • Cellular localizationNucleus.
  • Information by UniProt

References for Recombinant S. cerevisiae SAE2 / UBA2 protein (ab80727)

ab80727 has not yet been referenced specifically in any publications.

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