This fast track antibody is not yet fully characterized. It is subject to these terms and conditions

Overview

Properties

  • Form
    Liquid
  • Storage instructions
    Shipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
  • Storage buffer
    Preservative: 0.02% Sodium Azide
    Constituents: 0.5% BSA, Tris buffered saline, pH 7.3
  • Concentration information loading...
  • Purity
    Immunogen affinity purified
  • Purification notes
    ab87311 was purified by ammonium sulphate precipitation followed by antigen affinity chromatography using the immunizing peptide.
  • Clonality
    Polyclonal
  • Isotype
    IgG
  • Research areas

Target

  • Relevance
    DPM2 regulates the biosynthesis of dolichol phosphate-mannose. Dolichol-phosphate mannose (Dol-P-Man) serves as a donor of mannosyl residues on the lumenal side of the endoplasmic reticulum (ER). Lack of Dol-P-Man results in defective surface expression of GPI-anchored proteins. Dol-P-Man is synthesized from GDP-mannose and dolichol-phosphate on the cytosolic side of the ER by the enzyme dolichyl-phosphate mannosyltransferase. The protein encoded by DPM2 is a hydrophobic protein that contains 2 predicted transmembrane domains and a putative ER localization signal near the C terminus. This protein associates with DPM1 in vivo and is required for the ER localization and stable expression of DPM1 and also enhances the binding of dolichol-phosphate to DPM1.
  • Cellular localization
    Endoplasmic reticulum membrane; Multi-pass membrane protein.
  • Database links
  • Alternative names
    • Dolichol phosphate (beta D) mannosyltransferase 2 antibody
    • Dolichol phosphate mannose biosynthesis regulatory protein antibody
    • Dolichol phosphate mannose synthase 2 antibody
    • Dolichyl phosphate mannosyltransferase 2 antibody
    • Dolichyl phosphate mannosyltransferase polypeptide 2, regulatory subunit antibody
    • R75484 antibody
    • RP23 255P20.5 antibody
    see all

References

ab87311 has not yet been referenced specifically in any publications.

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