Recombinant Human UBE2D3 protein (ab113600)

Overview

Description

  • NatureRecombinant
  • SourceEscherichia coli
  • Amino Acid Sequence
    • AccessionP61077
    • SpeciesHuman
    • SequenceMGSSHHHHHHSSGLVPRGSHMLSNRKCLSKELSDLARDPPAQCSAGPVGD DMFHWQATIMGPNDSPYQGGVFFLTIHFPTDYPFKPPKVAFTTRIYHPNI NSNGSICLDILRSQWSPALTISKVLLSICSLLCDPNPDDPLVPEIARIYK TDRDKYNRISREWTQKYAM
    • Molecular weight19 kDa including tags
    • Amino acids1 to 149
    • TagsHis tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab113600 in the following tested applications.

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

  • Applications

    Mass Spectrometry

    SDS-PAGE

  • Mass spectrometry
    MALDI-TOF
  • Purity> 90 % SDS-PAGE.
    ab113600 was purified using conventional chromatography techniques.
  • FormLiquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles.

    pH: 8.00
    Constituents: 0.32% Tris HCl, 40% Glycerol, 0.88% Sodium chloride, 0.02% DTT

General Info

  • Alternative names
    • E2(17)KB3
    • MGC43926
    • MGC5416
    • PRO2116
    • UB2D3_HUMAN
    • UBC 4/5
    • UBC4/5
    • UBC4/5 homolog yeast
    • UBC4/5, S. cerevisiae, homolog of
    • UBCH 5C
    • UBCH5C
    • Ube2d3
    • Ubiquitin carrier protein
    • Ubiquitin carrier protein D3
    • Ubiquitin conjugating enzyme E2 17 kDa 3
    • Ubiquitin conjugating enzyme E2 D3
    • Ubiquitin conjugating enzyme E2D 3
    • Ubiquitin conjugating enzyme E2D 3 (homologous to yeast UBC4/5)
    • Ubiquitin conjugating enzyme E2D 3 (UBC4/5 homolog yeast)
    • Ubiquitin protein ligase D3
    • Ubiquitin-conjugating enzyme E2 D3
    • Ubiquitin-conjugating enzyme E2(17)KB 3
    • Ubiquitin-conjugating enzyme E2-17 kDa 3
    • Ubiquitin-protein ligase D3
    see all
  • FunctionAccepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'-, as well as 'Lys-48'-linked polyubiquitination. Cooperates with the E2 CDC34 and the SCF(FBXW11) E3 ligase complex for the polyubiquitination of NFKBIA leading to its subsequent proteasomal degradation. Acts as an initiator E2, priming the phosphorylated NFKBIA target at positions 'Lys-21' and/or 'Lys-22' with a monoubiquitin. Ubiquitin chain elongation is then performed by CDC34, building ubiquitin chains from the UBE2D3-primed NFKBIA-linked ubiquitin. Acts also as an initiator E2, in conjunction with RNF8, for the priming of PCNA. Monoubiquitination of PCNA, and its subsequent polyubiquitination, are essential events in the operation of the DNA damage tolerance (DDT) pathway that is activated after DNA damage caused by UV or chemical agents during S-phase. Associates with the BRCA1/BARD1 E3 ligase complex to perform ubiquitination at DNA damage sites following ionizing radiation leading to DNA repair. Targets DAPK3 for ubiquitination which influences promyelocytic leukemia protein nuclear body (PML-NB) formation in the nucleus. In conjunction with the MDM2 and TOPORS E3 ligases, functions ubiquitination of p53/TP53. Supports NRDP1-mediated ubiquitination and degradation of ERBB3 and of BRUCE which triggers apoptosis. In conjunction with the CBL E3 ligase, targets EGFR for polyubiquitination at the plasma membrane as well as during its internalization and transport on endosomes. In conjunction with the STUB1 E3 quality control E3 ligase, ubiquitinates unfolded proteins to catalyze their immediate destruction.
  • PathwayProtein modification; protein ubiquitination.
  • Sequence similaritiesBelongs to the ubiquitin-conjugating enzyme family.
  • Cellular localizationCell membrane. Endosome membrane.
  • Information by UniProt

Recombinant Human UBE2D3 protein images

  • 15% SDS-PAGE showing ab113600 (3 µg) at approximately 19.1 kDa.

References for Recombinant Human UBE2D3 protein (ab113600)

ab113600 has not yet been referenced specifically in any publications.

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