Overview

Description

  • NatureRecombinant
  • SourceWheat germ
  • Amino Acid Sequence
    • AccessionP19440
    • SpeciesHuman
    • Molecular weight88 kDa including tags
    • Amino acids1 to 569

Specifications

Our Abpromise guarantee covers the use of ab114433 in the following tested applications.

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

  • Applications

    ELISA

    SDS-PAGE

    Western blot

  • FormLiquid
  • Additional notesProtein concentration is above or equal to 0.05 mg/ml.
    Best use within three months from the date of receipt of this protein.
  • 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: 0.3% Glutathione, 0.79% Tris HCl

General Info

  • Alternative names
    • CD224
    • D22S672
    • D22S732
    • Gamma glutamyl transpeptidase
    • Gamma glutamyltransferase 1
    • Gamma glutamyltranspeptidase 1
    • Gamma-glutamyltransferase 1
    • Gamma-glutamyltranspeptidase 1 light chain
    • GGT
    • GGT 1
    • GGT1
    • GGT1_HUMAN
    • Glutamyl transpeptidase
    • Glutathione hydrolase 1
    • GTG
    • Leukotriene C4 hydrolase
    • MGC96892
    • MGC96904
    • MGC96963
    • OTTHUMP00000028921
    • OTTHUMP00000197959
    see all
  • FunctionInitiates extracellular glutathione (GSH) breakdown, provides cells with a local cysteine supply and contributes to maintain intracelular GSH level. It is part of the cell antioxidant defense mechanism. Catalyzes the transfer of the glutamyl moiety of glutathione to amino acids and dipeptide acceptors. Alternatively, glutathione can be hydrolyzed to give Cys-Gly and gamma glutamate. Isoform 3 seems to be inactive.
  • Tissue specificityDetected in fetal and adult kidney and liver, adult pancreas, stomach, intestine, placenta and lung. Isoform 3 is lung-specific. There are several other tissue-specific forms that arise from alternative promoter usage but that produce the same protein.
  • PathwaySulfur metabolism; glutathione metabolism.
  • Involvement in diseaseDefects in GGT1 are a cause of glutathionuria (GLUTH) [MIM:231950]; also known as gamma-glutamyltranspeptidase deficiency. It is an autosomal recessive disease.
  • Sequence similaritiesBelongs to the gamma-glutamyltransferase family.
  • Post-translational
    modifications
    N-glycosylated on both chains. Contains hexoses, hexosamines and sialic acid residues. Glycosylation profiles tested in kidney and liver tissues reveal the presence of tissue-specific and site-specific glycan composition, despite the overlap in composition among the N-glycans. A total of 36 glycan compositions, with 40 unique structures are observed. Up to 15 different glycans are observed at a single site, with site-specific variation in glycan composition. The difference in glycosylation profiles in the 2 tissues do not affect the enzyme activity.
  • Cellular localizationMembrane.
  • Information by UniProt

Recombinant Human GGT1 protein images

  • ab114433 analysed on a 12.5% SDS-PAGE gel stained with Coomassie Blue.

References for Recombinant Human GGT1 protein (ab114433)

ab114433 has not yet been referenced specifically in any publications.

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