Overview

Description

  • Nature
    Recombinant
  • Source
    Escherichia coli
  • Amino Acid Sequence
    • Accession
    • Species
      Human
    • Sequence
      MASMTGGQQMGRGHHHHHHGNLYFQGGESASKEPDNHVYTRAAVAADAKQ CSKIGRDALRDGGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTR KAEVINAREVAPRLAFATMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHG RLPWARLFQPSIQLARQGFPVGKGLAAALENKRTVIEQQPVLCEVFCRDR KVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKDIQAAGGIVT AEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFS RESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEF FAAQLRAQISDDTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATST INLYFGSKVRSPVSGILFNNEMDDFSSPSITNEFGVPPSPANFIQPGKQP LSSMCPTIMVGQDGQVRMVVGAAGGTQITTATALAIIYNLWFGYDVKRAV EEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVR TAGGWAAASDSRKGGEPAGY
    • Molecular weight
      62 kDa
    • Amino acids
      28 to 569
    • Tags
      His-T7 tag N-Terminus
    • Additional sequence information
      NP_038347. Constructed with codon optimization and expressed with a small T7-His-TEV cleavage site Tag (29aa) fusion at N terminal.

Specifications

Our Abpromise guarantee covers the use of ab190382 in the following tested applications.

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

  • Applications

    Functional Studies

    SDS-PAGE

  • Purity
    >90% by SDS-PAGE.
    The final product was refolded using temperature shift inclusion body refolding technology and chromatographically purified.
  • Form
    Liquid
  • Concentration information loading...

Preparation and Storage

  • Stability and Storage

    Shipped at 4°C. Store at +4°C short term (1-2 weeks). Store at -80°C. Avoid freeze / thaw cycle.

    pH: 8.00
    Constituent: 0.32% Tris HCl

    Buffer also contains NaCl, EDTA, KCl, arginine, DTT and glycerol.

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

References

ab190382 has not yet been referenced specifically in any publications.

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