Description

  • Product name

    Recombinant Human GALNT3 protein (His tag)
  • Purity

    > 95 % SDS-PAGE.
    ab199572 is greater than 95% pure as determined by SEC-HPLC and reducing SDS-PAGE.
  • Endotoxin level

    < 1.000 Eu/µg
  • Expression system

    HEK 293 cells
  • Accession

  • Protein length

    Protein fragment
  • Animal free

    No
  • Nature

    Recombinant
    • Species

      Human
    • Sequence

      QREVSVQYSKEESRMERNMKNKNKMLDLMLEAVNNIKDAMPKMQIGAPVR QNIDAGERPCLQGYYTAAELKPVLDRPPQDSNAPGASGKAFKTTNLSVEE QKEKERGEAKHCFNAFASDRISLHRDLGPDTRPPECIEQKFKRCPPLPTT SVIIVFHNEAWSTLLRTVHSVLYSSPAILLKEIILVDDASVDEYLHDKLD EYVKQFSIVKIVRQRERKGLITARLLGATVATAETLTFLDAHCECFYGWL EPLLARIAENYTAVVSPDIASIDLNTFEFNKPSPYGSNHNRGNFDWSLSF GWESLPDHEKQRRKDETYPIKTPTFAGGLFSISKEYFEYIGSYDEEMEIW GGENIEMSFRVWQCGGQLEIMPCSVVGHVFRSKSPHSFPKGTQVIARNQV RLAEVWMDEYKEIFYRRNTDAAKIVKQKAFGDLSKRFEIKHRLQCKNFTW YLNNIYPEVYVPDLNPVISGYIKSVGQPLCLDVGENNQGGKPLIMYTCHG LGGNQYFEYSAQHEIRHNIQKELCLHAAQGLVQLKACTYKGHKTVVTGEQ IWEIQKDQLLYNPFLKMCLSANGEHPSLVSCNPSDPLQKWILSQNDVDHH HHHH
    • Predicted molecular weight

      69 kDa including tags
    • Amino acids

      39 to 633
    • Tags

      His tag C-Terminus

Specifications

Our Abpromise guarantee covers the use of ab199572 in the following tested applications.

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

  • Applications

    SDS-PAGE

    HPLC

  • Form

    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped on Dry Ice. Store at -20°C. Avoid freeze / thaw cycle.

    pH: 7.4
    Constituents: 0.87% Sodium chloride, 99% Phosphate Buffer

General Info

  • Alternative names

    • DKFZp686C10199
    • EC 2.4.1.41
    • GalNAc T3
    • GalNAc transferase 3
    • GalNAc-T3
    • GalNAcT3
    • GALNT3
    • GALT3_HUMAN
    • HFTC
    • HHS
    • MGC61909
    • OTTHUMP00000204915
    • OTTHUMP00000204919
    • Polypeptide GalNAc transferase 3
    • Polypeptide GalNAc transferase T3
    • Polypeptide N acetylgalactosaminyltransferase 3
    • Polypeptide N-acetylgalactosaminyltransferase 3
    • pp-GaNTase 3
    • ppGaNTase 3
    • Protein UDP acetylgalactosaminyltransferase 3
    • Protein-UDP acetylgalactosaminyltransferase 3
    • RP23-306G16.2
    • UDP GalNAc:polypeptide N acetylgalactosaminyltransferase 3
    • UDP N acetyl alpha D galactosamine:polypeptide N acetylgalactosaminyltransferase 3 (GalNAc T3)
    • UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase 3
    • UDP-N-acetyl-alpha-D-galactosamine:polypeptide N-acetylgalactosaminyltransferase 3
    see all
  • Function

    Catalyzes the initial reaction in O-linked oligosaccharide biosynthesis, the transfer of an N-acetyl-D-galactosamine residue to a serine or threonine residue on the protein receptor. Has activity toward HIV envelope glycoprotein gp120, EA2, Muc2 and Muc5. Probably glycosylates fibronectin in vivo. Glycosylates FGF23. Plays a central role in phosphate homeostasis.
  • Tissue specificity

    Expressed in organs that contain secretory epithelial glands. Highly expressed in pancreas, skin, kidney and testis. Weakly expressed in prostate, ovary, intestine and colon. Also expressed in placenta and lung and fetal lung and fetal kidney.
  • Pathway

    Protein modification; protein glycosylation.
  • Involvement in disease

    Defects in GALNT3 are a cause of hyperphosphatemic familial tumoral calcinosis (HFTC) [MIM:211900]. HFTC is a severe autosomal recessive metabolic disorder that manifests with hyperphosphatemia and massive calcium deposits in the skin and subcutaneous tissues. Some patients manifest recurrent, transient, painful swellings of the long bones associated with the radiographic findings of periosteal reaction and cortical hyperostosis and absence of skin involvement.
  • 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 > Golgi stack membrane. Resides preferentially in the trans and medial parts of the Golgi stack.
  • Information by UniProt

References

ab199572 has not yet been referenced specifically in any publications.

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