Overview

Description

  • Nature
    Recombinant
  • Source
    Wheat germ
  • Amino Acid Sequence
    • Accession
    • Species
      Human
    • Sequence
      TAHLSVVAEDGSAVSATSTINLYFGSKVRSPVSGILFNNEMDDFSSPSIT NEFGVPPSPANFIQPGKQPLSSMCPTIMVGQDGQVRMVVG
    • Molecular weight
      36 kDa including tags
    • Amino acids
      381 to 470

Associated products

Specifications

Our Abpromise guarantee covers the use of ab114434 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

  • Form
    Liquid
  • Additional notes
    Protein 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
  • Function
    Initiates 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 specificity
    Detected 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.
  • Pathway
    Sulfur metabolism; glutathione metabolism.
  • Involvement in disease
    Defects in GGT1 are a cause of glutathionuria (GLUTH) [MIM:231950]; also known as gamma-glutamyltranspeptidase deficiency. It is an autosomal recessive disease.
  • Sequence similarities
    Belongs 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 localization
    Membrane.
  • Information by UniProt

Recombinant Human GGT1 protein images

  • ab114434 analysed on a 12.5% SDS-PAGE gel stained with Coomassie Blue.

References for Recombinant Human GGT1 protein (ab114434)

ab114434 has not yet been referenced specifically in any publications.

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