Human GGT1 Protein 5085

$270.00 – $900.00

Summary

Expression: HEK293
Pure: Yes (HPLC)
Amino Acid Range: Pro27-Tyr569

SKU: 5085parent Categories: proteins, Recombinant proteins Tag: active proteins

Weight	1 lbs
Dimensions	9 × 5 × 2 in
accession	P19440
express system	HEK293
product tag	N-His
purity	> 95% as determined by Tris-Bis PAGE;> 95% as determined by HPLC
background	Gamma-glutamyl transferase (GGT; EC 2.3.2.2) is the only enzyme capable of degrading glutathione (GSH) in extra-cytosolic spaces. Overexpression of γ-glutamyl transpeptidase (GGT1) has been implicated in an array of human diseases including asthma, reperfusion injury, and cancer.
molecular weight	The protein has a predicted MW of 59.69 kDa. Due to enzyme lysis and glycosylation, the protein migrates to 55-65 kDa (heavy chain) and 25-30 kDa (light chain) based on Tris-Bis PAGE result.
available size	100 µg, 500 µg
endotoxin	Less than 1EU per μg by the LAL method.

Human GGT1 Protein 5085

protein

Size and concentration 100, 500µg and lyophilized
Form Lyophilized
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles.
Storage buffer Shipped at ambient temperature.
Purity > 95% as determined by Tris-Bis PAGE

target relevance
Gamma-glutamyl transferase (GGT; EC 2.3.2.2) is the only enzyme capable of degrading glutathione (GSH) in extra-cytosolic spaces. Overexpression of γ-glutamyl transpeptidase (GGT1) has been implicated in an array of human diseases including asthma, reperfusion injury, and cancer.
Protein names Glutathione hydrolase 1 proenzyme (EC 3.4.19.13) (Gamma-glutamyltransferase 1) (Gamma-glutamyltranspeptidase 1) (GGT 1) (EC 2.3.2.2) (Leukotriene-C4 hydrolase) (EC 3.4.19.14) (CD antigen CD224) [Cleaved into: Glutathione hydrolase 1 heavy chain; Glutathione hydrolase 1 light chain]
Gene names GGT1,GGT1 GGT
Protein family Gamma-glutamyltransferase family
Mass 9606Da
Function Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates (such as maresin conjugate (13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate, MCTR1) and other gamma-glutamyl compounds (such as leukotriene C4, LTC4) (PubMed:17924658, PubMed:21447318, PubMed:27791009). The metabolism of glutathione by GGT1 releases free glutamate and the dipeptide cysteinyl-glycine, which is hydrolyzed to cysteine and glycine by dipeptidases (PubMed:27791009). In the presence of high concentrations of dipeptides and some amino acids, can also catalyze a transpeptidation reaction, transferring the gamma-glutamyl moiety to an acceptor amino acid to form a new gamma-glutamyl compound (PubMed:17924658, PubMed:21447318, PubMed:7673200, PubMed:7759490, PubMed:8095045, PubMed:8827453). Contributes to cysteine homeostasis, glutathione homeostasis and in the conversion of the leukotriene LTC4 to LTD4.; [Isoform 3]: Seems to be inactive.
Catalytic activity #N/A
Pathway PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis.; PATHWAY: Sulfur metabolism; glutathione metabolism.
Subellular location Cell membrane ; Single-pass type II membrane protein .
Tissues Detected in fetal and adult kidney and liver, adult pancreas, stomach, intestine, placenta and lung. There are several other tissue-specific forms that arise from alternative promoter usage but that produce the same protein.; [Isoform 3]: Lung-specific.
Structure Heterodimer composed of the light and heavy chains. The active site is located in the light chain.
Post-translational modification 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.; Cleaved by autocatalysis into a large and a small subunit and the autocatalytic cleavage is essential to the functional activation of the enzyme.
Target Relevance information above includes information from UniProt accession: P19440
The UniProt Consortium

Data

The purity of Human GGT1 is greater than 95% as determined by SEC-HPLC.

Human GGT1 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

pmid	title	authors	citation
We haven't added any publications to our database yet.

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.