Overview

Description

  • Nature
    Recombinant
  • Source
    Wheat germ
  • Amino Acid Sequence
    • Species
      Human
    • Sequence
      LGPCHRMGGNQLFRINEANQLMQYDQCLTKGADGSKVMITHCNLNEFKEW QYFKNLHRFTHIPSGKCLDRSEVLHQVFISNCDSSKTTQKWEMNNIHSV
    • Amino acids
      559 to 657
    • Tags
      proprietary tag N-Terminus

Specifications

Our Abpromise guarantee covers the use of ab162676 in the following tested applications.

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

  • Applications

    ELISA

    Western blot

  • Form
    Liquid
  • Additional notes
    Protein concentration is above or equal to 0.05 mg/ml.
  • 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: 8.00
    Constituents: 0.31% Glutathione, 0.79% Tris HCl

General Info

  • Alternative names
    • GalNAc T7
    • GalNAc-T7
    • GalNAcT7
    • GALNT 7
    • Galnt7
    • GALT7_HUMAN
    • N acetylgalactosaminyltransferase 7
    • N-acetylgalactosaminyltransferase 7
    • Polypeptide GalNAc transferase 7
    • Polypeptide N acetylgalactosaminyltransferase 7
    • pp GaNTase 7
    • pp-GaNTase 7
    • Protein UDP acetylgalactosaminyltransferase 7
    • Protein-UDP acetylgalactosaminyltransferase 7
    • UDP GalNAc:polypeptide N acetylgalactosaminyltransferase 7
    • UDP N acetyl alpha D galactosamine:polypeptide N acetylgalactosaminyltransferase 7
    • UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 7
    see all
  • Function
    Glycopeptide transferase involved in O-linked oligosaccharide biosynthesis, which catalyzes the transfer of an N-acetyl-D-galactosamine residue to an already glycosylated peptide. In contrast to other proteins of the family, it does not act as a peptide transferase that transfers GalNAc onto serine or threonine residue on the protein receptor, but instead requires the prior addition of a GalNAc on a peptide before adding additional GalNAc moieties. Some peptide transferase activity is however not excluded, considering that its appropriate peptide substrate may remain unidentified.
  • Tissue specificity
    Widely expressed. Expressed in uterus, retina, kidney, small intestine, omentum, stomach and CNS.
  • Pathway
    Protein modification; protein glycosylation.
  • Sequence similarities
    Belongs to the glycosyltransferase 2 family. GalNAc-T subfamily.
    Contains 1 ricin B-type lectin domain.
  • Domain
    There are two conserved domains in the glycosyltransferase region: the N-terminal domain (domain A, also called GT1 motif), which is probably involved in manganese coordination and substrate binding and the C-terminal domain (domain B, also called Gal/GalNAc-T motif), which is probably involved in catalytic reaction and UDP-Gal binding.
    The ricin B-type lectin domain binds to GalNAc and contributes to the glycopeptide specificity.
  • Cellular localization
    Golgi apparatus membrane.
  • Information by UniProt

Images

  • ab162676 on a 12.5% SDS-PAGE stained with Coomassie Blue.

References

ab162676 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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