GGT5
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- Overview
- Review / Q&A
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Official Full Name
gamma-glutamyltransferase 5 -
Overview
This gene is a member of a gene family that encodes gamma-glutamyl transpeptidase enzymes. This enzyme consists of a heavy and a light chain, and is able to hydrolyze the gamma-glutamyl moiety of glutathione. It converts leukotriene C4 to leukotriene D4, however, it doesnt convert synthetic substrates that are commonly used to assay gamma-glutamyl transpeptidase. Three transcript variants encoding different isoforms have been found for this gene. -
Synonyms
GGT5;gamma-glutamyltransferase 5;gamma glutamyltransferase like activity 1 , GGTLA1;GGT REL;DKFZP566O011;Gamma glutamyl transpeptidase related enzyme;Gamma glutamyltranspeptidase 5;GGT 5;gamma-glutamyl cleaving enzyme;gamma-glutamyltranspeptidase 5;gamma-glutamyltransferase-like activity 1;gamma-glutamyl transpeptidase-related enzyme;gamma-glutamyl transpeptidase-related protein;GGTLA1;GGT-REL
Recombinant Proteins
- Human
- E.coli
- HEK293
- Wheat Germ
- In Vitro Cell Free System
- GST
- His
- T7
- Non
| Cat.# | Product name | Source (Host) | Species | Tag | Protein Length | Price |
|---|---|---|---|---|---|---|
| GGT5-13244H | Recombinant Human GGT5, GST-tagged | E.coli | Human | GST | C-term-300a.a. | |
| GGT5-1145H | Recombinant Human GGT5 protein, His & T7-tagged | E.coli | Human | His&T7 | Thr388~Tyr586 |
|
| GGT5-773H | Recombinant Human GGT5 protein(Ser30-Tyr586), His-tagged | HEK293 | Human | His | Ser30-Tyr586 |
|
| GGT5-2699H | Recombinant Human GGT5 Protein (Thr388-Tyr586), N-His tagged | E.coli | Human | His | Thr388-Tyr586 |
|
| GGT5-4879H | Recombinant Human GGT5 Protein, GST-tagged | Wheat Germ | Human | GST |
|
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| GGT5-5243HF | Recombinant Full Length Human GGT5 Protein, GST-tagged | In Vitro Cell Free System | Human | GST | Full L. 587 amino acids |
|
| RFL35956HF | Recombinant Full Length Human Gamma-Glutamyltransferase 5(Ggt5) Protein, His-Tagged | E.coli | Human | His | Full L. Full Length (1-387) |
|
Involved Pathway
GGT5 involved in several pathways and played different roles in them. We selected most pathways GGT5 participated on our site, such as Taurine and hypotaurine metabolism,Cyanoamino acid metabolism,Glutathione metabolism, which may be useful for your reference. Also, other proteins which involved in the same pathway with GGT5 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
| Pathway Name | Pathway Related Protein |
|---|---|
| Glutathione metabolism | GPX6,GSTA4,GPX1A,RRM2B,GGT5A,GSTA3,GPX4,GSTP1,GSTT1,GGT6 |
| Cyanoamino acid metabolism | GGT1,GGT1A,GGT7,SHMT2,GGT5A,GBA3,SHMT1,GGT6 |
| Metabolic pathways | DHRS3B,ENO1A,AGPAT9,GLUD2,CYP2C50,AGK,MTAP,PLCD3,LPIN1,XDH |
| Arachidonic acid metabolism | AKR1C21,GPX8,PTGS1,CYP2C70,CYP2P9,CYP4F18,PLA2G4AA,GPX1,CYP1A2,CBR1L |
| Taurine and hypotaurine metabolism | GAD1,GAD2,GGT5A,CDO1,ADOB,GAD1B,BAAT,GGT7,ADO,CSAD |
Protein Function
GGT5 has several biochemical functions, for example, gamma-glutamyltransferase activity,glutathione hydrolase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by GGT5 itself. We selected most functions GGT5 had, and list some proteins which have the same functions with GGT5. You can find most of the proteins on our site.
| Function | Related Protein |
|---|---|
| glutathione hydrolase activity | GGT6,GGT7,GGT1 |
| gamma-glutamyltransferase activity | GGT1,GGT6,GGTLC1,GGT5A,GGT1A,GGT7 |
Interacting Protein
GGT5 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with GGT5 here. Most of them are supplied by our site. Hope this information will be useful for your research of GGT5.
Resources
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References
- Sket, P; Korbar, T; et al. Influence of 3 '-3 ' inversion of polarity site within d(TGGGGT) on inter quartet cation binding. JOURNAL OF MOLECULAR STRUCTURE 1075:49-52(2014).
- Serizawa, M; Kusuhara, M; et al. Identification of Metabolic Signatures Associated with Erlotinib Resistance of Non-small Cell Lung Cancer Cells. ANTICANCER RESEARCH 34:2779-2787(2014).
