Overview

Description

  • Nature

    Recombinant
  • Source

    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species

      Human
    • Molecular weight

      9 kDa
    • Amino acids

      1 to 76
    • Additional sequence information

      15N-labeled ubiquitin.

Associated products

Specifications

Our Abpromise guarantee covers the use of ab218617 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

  • Purity

    > 95 % SDS-PAGE.

  • Form

    Liquid
  • Additional notes

    15N-labeled ubiquitin can be used in NMR experiments for determining interactions between ubiquitin and other proteins. It can also be used as a standard for quantification of cellular ubiquitin levels in quantitative mass spectrometric assays.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on Dry Ice. Store at -80°C. Avoid freeze / thaw cycle.

    Constituents: 0.24% Tris, 0.87% Sodium chloride, 0.02% Beta mercaptoethanol, 10% Glycerol

General Info

  • Alternative names

    • Epididymis secretory protein Li 50
    • FLJ25987
    • HEL S 50
    • MGC8385
    • Polyubiquitin B
    • RPS 27A
    • RPS27A
    • UBA 52
    • UBA 80
    • UBA52
    • UBA80
    • UBB
    • UBB_HUMAN
    • UBC
    • UBCEP 1
    • UBCEP 2
    • UBCEP1
    • UBCEP2
    • Ubiquitin
    • Ubiquitin B
    see all
  • Relevance

    Function: Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. Similarity: Belongs to the ubiquitin family. Contains 3 ubiquitin-like domains.
  • Cellular localization

    Cell Membrane, Cytoplasmic and Nuclear

Images

  • SDS-PAGE analysis of ab218617 (5µg). Stained with Coomassie.

References

ab218617 has not yet been referenced specifically in any publications.

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