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GGT5

  • 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
  • Cell & Tissue Lysates
  • Homo sapiens (Human)
  • Human
  • E.coli
  • E.coli expression system
  • HEK293
  • In Vitro Cell Free System
  • Wheat Germ
  • GST
  • His
  • His|T7
  • N/A
  • N
Species Cat.# Product name Source (Host) Tag Protein Length Price
Human GGT5-773H Recombinant Human GGT5 protein(Ser30-Tyr586), His-tagged HEK293 N-His Ser30-Tyr586
Human GGT5-13244H Recombinant Human GGT5, GST-tagged E.coli GST C-term-300a.a.
Human GGT5-1145H Recombinant Human GGT5 protein, His & T7-tagged E.coli His/T7 Thr388~Tyr586 (Accession # P36269)
Human GGT5-702HCL Recombinant Human GGT5 cell lysate N/A
Human GGT5-2699H Recombinant Human GGT5 Protein (Thr388-Tyr586), N-His tagged E.coli N-His Thr388-Tyr586
Human GGT5-4879H Recombinant Human GGT5 Protein, GST-tagged Wheat Germ GST
Human GGT5-5243HF Recombinant Full Length Human GGT5 Protein, GST-tagged In Vitro Cell Free System GST 587 amino acids
Homo sapiens (Human) RFL35956HF Recombinant Full Length Human Gamma-Glutamyltransferase 5(Ggt5) Protein, His-Tagged E.coli expression system His Full Length (1-387)
  • Involved Pathway
  • Protein Function
  • Interacting Protein
  • GGT5 Related Articles
  • GGT5 Related Research Area

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
Taurine and hypotaurine metabolismGGT5;CDO1;ADOB;CSAD;GAD1;GGT7;BAAT;GAD1B;ADO
Cyanoamino acid metabolismGGT1A;GGT6;GBA3;GGT5;GGT5A;SHMT1;GGT1;GGT7;SHMT2
Glutathione metabolismGSTO1;GSTM6;PGD;GPX1A;GGCT;GCLM;GSTT1;ANPEPB;LAP3
Arachidonic acid metabolismCYP2P7;GGT5;GPX6;GGTLC1;CYP2C38;ALOX8;PTGDS;FAAH2B;CYP2C50
Metabolic pathwaysADH2-1;PI4K2A;PIGV;ATP5IA;AGXT2L2;CYP3A41A;AMY2A4;ALDH9A1B;CYP19A1B

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
gamma-glutamyltransferase activityGGT5A;GGT7;GGT5;GGTLC1;GGT1;GGT6;GGT1A
glutathione hydrolase activityGGT1;GGT5;GGT6;GGT7

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.

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).
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