Recombinant Human GGT1/GGT protein (ab190382)
Key features and details
- Expression system: Escherichia coli
- Purity: > 90% SDS-PAGE
- Tags: His-T7 tag N-Terminus
- Suitable for: Functional Studies, SDS-PAGE
Description
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Product name
Recombinant Human GGT1/GGT protein -
Purity
> 90 % SDS-PAGE.
The final product was refolded using temperature shift inclusion body refolding technology and chromatographically purified. -
Expression system
Escherichia coli -
Accession
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Protein length
Protein fragment -
Animal free
No -
Nature
Recombinant -
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Species
Human -
Sequence
MASMTGGQQMGRGHHHHHHGNLYFQGGESASKEPDNHVYTRAAVAADAKQ CSKIGRDALRDGGSAVDAAIAALLCVGLMNAHSMGIGGGLFLTIYNSTTR KAEVINAREVAPRLAFATMFNSSEQSQKGGLSVAVPGEIRGYELAHQRHG RLPWARLFQPSIQLARQGFPVGKGLAAALENKRTVIEQQPVLCEVFCRDR KVLREGERLTLPQLADTYETLAIEGAQAFYNGSLTAQIVKDIQAAGGIVT AEDLNNYRAELIEHPLNISLGDVVLYMPSAPLSGPVLALILNILKGYNFS RESVESPEQKGLTYHRIVEAFRFAYAKRTLLGDPKFVDVTEVVRNMTSEF FAAQLRAQISDDTTHPISYYKPEFYTPDDGGTAHLSVVAEDGSAVSATST INLYFGSKVRSPVSGILFNNEMDDFSSPSITNEFGVPPSPANFIQPGKQP LSSMCPTIMVGQDGQVRMVVGAAGGTQITTATALAIIYNLWFGYDVKRAV EEPRLHNQLLPNVTTVERNIDQAVTAALETRHHHTQIASTFIAVVQAIVR TAGGWAAASDSRKGGEPAGY -
Predicted 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.
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Associated products
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Related Products
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.
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Applications
Functional Studies
SDS-PAGE
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Form
Liquid -
Additional notes
This product was previously labelled as GGT1
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Concentration information loading...
Preparation and Storage
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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
Constituents: 2% Tris HCl, 1% Potassium chloride, 0.01% DTT, 0.01% EDTA, 10% Glycerol, 10% Sodium chloride
General Info
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Alternative names
- CD224
- D22S672
- D22S732
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
modificationsN-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
Protocols
To our knowledge, customised protocols are not required for this product. Please try the standard protocols listed below and let us know how you get on.
Datasheets and documents
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SDS download
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Datasheet download
References (0)
ab190382 has not yet been referenced specifically in any publications.