Description

  • Product name

    Recombinant Human HIP2/LIG protein
    See all HIP2/LIG proteins and peptides
  • Biological activity

    ab111465 charges and supports ubiquitinylation in vitro. Typical enzyme concentration to support conjugation in vitro is 100 nM to 1 µM
  • Purity

    > 95 % SDS-PAGE.

  • Expression system

    Escherichia coli
  • Accession

  • Protein length

    Full length protein
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Predicted molecular weight

      22 kDa
    • Amino acids

      1 to 200

Specifications

Our Abpromise guarantee covers the use of ab111465 in the following tested applications.

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

  • Applications

    SDS-PAGE

  • Form

    Liquid
  • Additional notes

    ab111465 charges and supports ubiquitinylation in vitro. Typical enzyme concentration to support conjugation in vitro is 100 nM to 1 µM

     This product was previously labelled as HIP2

     

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

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

    pH: 7.50
    Constituents: Tris buffered saline, 0.02% DTT

General Info

  • Alternative names

    • E2 25K
    • E2(25K)
    • HIP-2
    • Huntingtin interacting protein 2
    • Huntingtin-interacting protein 2
    • HYPG
    • LIG
    • UBC1
    • UBE2K
    • UBE2K_HUMAN
    • Ubiquitin carrier protein
    • Ubiquitin conjugating enzyme E2 25 kDa
    • ubiquitin conjugating enzyme E2K
    • ubiquitin conjugating enzyme E2K (UBC1 homolog, yeast)
    • Ubiquitin protein ligase
    • Ubiquitin-conjugating enzyme E2 K
    • Ubiquitin-conjugating enzyme E2(25K)
    • Ubiquitin-conjugating enzyme E2-25 kDa
    • Ubiquitin-conjugating enzyme E2-25K
    • Ubiquitin-protein ligase
    see all
  • Function

    Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1.
  • Tissue specificity

    Expressed in all tissues tested, including spleen, thymus, prostate, testis, ovary, small intestine, colon, peripheral blood leukocytes, T-lymphocytes, monocytes, granulocytes and bone marrow mononuclear cells. Highly expressed in brain, with highest levels found in cortex and striatum and at lower levels in cerebellum and brainstem.
  • Pathway

    Protein modification; protein ubiquitination.
  • Sequence similarities

    Belongs to the ubiquitin-conjugating enzyme family.
    Contains 1 UBA domain.
  • Post-translational
    modifications

    Sumoylation at Lys-14 impairs catalytic activity.
  • Cellular localization

    Cytoplasm.
  • Information by UniProt

References

ab111465 has not yet been referenced specifically in any publications.

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