Overview

Description

  • Nature

    Recombinant
  • Source

    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species

      Human
    • Molecular weight

      18 kDa
    • Additional sequence information

      Wild-type chains (1-7) K63-linked. 8.6 kDa (Ub), 17 kDa (Ub2), 26 kDa (Ub3), 34 kDa (Ub4), 43 kDa (Ub5), 52 kDa (Ub6), and 60 kDa (Ub7) .

Specifications

Our Abpromise guarantee covers the use of ab189749 in the following tested applications.

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

  • Biological activity

    Typical concentrations will depend on specific assay conditions and method of detection.

  • Applications

    Functional Studies

    SDS-PAGE

  • Purity

    > 95 % SDS-PAGE.

  • Form

    Lyophilised
  • Additional notes

    Linkage specific poly-ubiquitin chains are used to investigate mechanisms of chain recognition, binding and hydrolysis by the proteasome, deubiquitinating enzymes, E3 ligases or other proteins that contain ubiquitin-associated domains (UBAs) or ubiquitin-interacting motifs (UIMs). Lys48- linked chains are abundant in vivo and act as a universal signal for proteasomal degradation. This product is formed with wild-type human recombinant ubiquitin and linkage-specific enzymes. The poly-ubiquitin chain mixture contains mono-ubiquitin and higher MW species up to hepta-ubiquitin.

    Solubility: Aqueous solutions up to 5 mg/ml.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at Room Temperature. Store at -20°C. Avoid freeze / thaw cycle.

    This product is an active protein and may elicit a biological response in vivo, handle with caution.

  • Reconstitution
    Reconstitute at 2 mg/mL in an aqueous solution.

General Info

  • Alternative names

    • UBB
    • UBB_HUMAN
    • Ubiquitin
  • 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.
  • Sequence similarities

    Belongs to the ubiquitin family.
    Contains 3 ubiquitin-like domains.
  • Cellular localization

    Cytoplasm. Nucleus.
  • Information by UniProt

References

ab189749 has not yet been referenced specifically in any publications.

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