Recombinant S. cerevisiae Ubiquitin protein (ab189715)

Overview

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species
      Saccharomyces cerevisiae
    • Sequence
      MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQL EDGRTLSDYNIQKESTLHLVLRLRGG
    • Molecular weight
      9 kDa
    • Amino acids
      1 to 76
    • Additional sequence information
      This protein sequence is for S.cerevisiae and is exactly the same for S.pombe.

Specifications

Our Abpromise guarantee covers the use of ab189715 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 concentration to support in vitro conjugation is 500 μM to 1 mM depending on conditions.

  • Applications

    SDS-PAGE

    Functional Studies

  • Purity
    >95% by SDS-PAGE .

  • Form
    Lyophilised
  • Additional notes

    ab189715 is highly purified Ubiquitin and is free of glycine and buffer salts which can interfere with chemical and in vitro reactions.

  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at +4°C.

    Lyophilized from a solution in deionized water.

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

  • Reconstitution
    Reconstitute at 10 mg/mL in an aqueous solution. Store reconstituted stock solution at -20°C. Avoid multiple freeze/thaw cycles. (Solubility: Aqueous solutions up to 20 mg/mL.)

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

References

ab189715 has not yet been referenced specifically in any publications.

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Please note: All products are "FOR RESEARCH USE ONLY AND ARE NOT INTENDED FOR DIAGNOSTIC OR THERAPEUTIC USE"

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