Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Glutathione hydrolase 5 proenzyme (EC 3.4.19.13) (Gamma-glutamyl transpeptidase-related enzyme) (GGT-rel) (Gamma-glutamyltransferase 5) (GGT 5) (EC 2.3.2.2) (Gamma-glutamyltransferase-like activity 1) (Gamma-glutamyltranspeptidase 5) (Leukotriene-C4 hydrolase) (EC 3.4.19.14) [Cleaved into: Glutathione hydrolase 5 heavy chain; Glutathione hydrolase 5 light chain]

 GGT5_HUMAN              Reviewed;         586 AA.
P36269; Q53XM9; Q6GMP0; Q96FC1; Q9UFM5;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
28-FEB-2018, entry version 169.
RecName: Full=Glutathione hydrolase 5 proenzyme;
EC=3.4.19.13;
AltName: Full=Gamma-glutamyl transpeptidase-related enzyme;
Short=GGT-rel;
AltName: Full=Gamma-glutamyltransferase 5;
Short=GGT 5;
EC=2.3.2.2;
AltName: Full=Gamma-glutamyltransferase-like activity 1;
AltName: Full=Gamma-glutamyltranspeptidase 5;
AltName: Full=Leukotriene-C4 hydrolase;
EC=3.4.19.14;
Contains:
RecName: Full=Glutathione hydrolase 5 heavy chain;
Contains:
RecName: Full=Glutathione hydrolase 5 light chain;
Flags: Precursor;
Name=GGT5; Synonyms=GGTLA1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-330.
TISSUE=Placenta;
PubMed=1676842; DOI=10.1073/pnas.88.14.6303;
Heisterkamp N., Rajpert-De Meyts E., Uribe L., Forman H.J.,
Groffen J.;
"Identification of a human gamma-glutamyl cleaving enzyme related to,
but distinct from, gamma-glutamyl transpeptidase.";
Proc. Natl. Acad. Sci. U.S.A. 88:6303-6307(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Small intestine;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Fetal kidney;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-330.
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Brain, and PNS;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-550.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Cleaves the gamma-glutamyl peptide bond of glutathione
conjugates, but maybe not glutathione itself. Converts leukotriene
C4 (LTC4) to leukotriene D4 (LTD4).
-!- CATALYTIC ACTIVITY: A (5-L-glutamyl)-peptide + an amino acid = a
peptide + a 5-L-glutamyl amino acid.
-!- CATALYTIC ACTIVITY: Glutathione + H(2)O = L-cysteinylglycine + L-
glutamate.
-!- CATALYTIC ACTIVITY: Leukotriene C(4) + H(2)O = leukotriene D(4) +
L-glutamate.
-!- PATHWAY: Sulfur metabolism; glutathione metabolism.
-!- PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis.
-!- SUBUNIT: Heterodimer composed of the light and heavy chains. The
active site is located in the light chain (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000250}; Single-pass type II
membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P36269-1; Sequence=Displayed;
Name=2;
IsoId=P36269-2; Sequence=VSP_008146;
Note=No experimental confirmation available.;
Name=3;
IsoId=P36269-3; Sequence=VSP_043470;
Note=No experimental confirmation available.;
-!- PTM: Cleaved by autocatalysis into a large and a small subunit.
{ECO:0000250}.
-!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAB55910.1; Type=Frameshift; Positions=446; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M64099; AAA58503.1; -; mRNA.
EMBL; AL117414; CAB55910.1; ALT_FRAME; mRNA.
EMBL; BT009808; AAP88810.1; -; mRNA.
EMBL; CT841518; CAJ86448.1; -; mRNA.
EMBL; AK292006; BAF84695.1; -; mRNA.
EMBL; AP000353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AP000354; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW59643.1; -; Genomic_DNA.
EMBL; BC011362; AAH11362.1; -; mRNA.
EMBL; BC073999; AAH73999.1; -; mRNA.
CCDS; CCDS13825.1; -. [P36269-1]
CCDS; CCDS42989.1; -. [P36269-2]
CCDS; CCDS42990.1; -. [P36269-3]
PIR; A41125; A41125.
PIR; T17220; T17220.
RefSeq; NP_001093251.1; NM_001099781.2. [P36269-3]
RefSeq; NP_001093252.1; NM_001099782.2. [P36269-2]
RefSeq; NP_001289393.1; NM_001302464.1.
RefSeq; NP_001289394.1; NM_001302465.1.
RefSeq; NP_004112.2; NM_004121.3. [P36269-1]
UniGene; Hs.437156; -.
ProteinModelPortal; P36269; -.
SMR; P36269; -.
BioGrid; 108954; 5.
STRING; 9606.ENSP00000381340; -.
SwissLipids; SLP:000001455; -.
MEROPS; T03.002; -.
iPTMnet; P36269; -.
PhosphoSitePlus; P36269; -.
BioMuta; GGT5; -.
DMDM; 116242493; -.
PaxDb; P36269; -.
PeptideAtlas; P36269; -.
PRIDE; P36269; -.
DNASU; 2687; -.
Ensembl; ENST00000263112; ENSP00000263112; ENSG00000099998. [P36269-2]
Ensembl; ENST00000327365; ENSP00000330080; ENSG00000099998. [P36269-1]
Ensembl; ENST00000398292; ENSP00000381340; ENSG00000099998. [P36269-3]
GeneID; 2687; -.
KEGG; hsa:2687; -.
UCSC; uc002zzo.4; human. [P36269-1]
CTD; 2687; -.
DisGeNET; 2687; -.
EuPathDB; HostDB:ENSG00000099998.17; -.
GeneCards; GGT5; -.
H-InvDB; HIX0138942; -.
HGNC; HGNC:4260; GGT5.
HPA; CAB032489; -.
HPA; HPA008121; -.
MIM; 137168; gene.
neXtProt; NX_P36269; -.
OpenTargets; ENSG00000099998; -.
PharmGKB; PA162389442; -.
eggNOG; KOG2410; Eukaryota.
eggNOG; COG0405; LUCA.
GeneTree; ENSGT00550000074591; -.
HOGENOM; HOG000175620; -.
HOVERGEN; HBG005835; -.
InParanoid; P36269; -.
KO; K18592; -.
OMA; NNGIMWF; -.
OrthoDB; EOG091G03Y3; -.
PhylomeDB; P36269; -.
TreeFam; TF313608; -.
BioCyc; MetaCyc:HS01949-MONOMER; -.
BRENDA; 2.3.2.2; 2681.
BRENDA; 3.4.19.13; 2681.
Reactome; R-HSA-174403; Glutathione synthesis and recycling.
Reactome; R-HSA-2142691; Synthesis of Leukotrienes (LT) and Eoxins (EX).
Reactome; R-HSA-5423646; Aflatoxin activation and detoxification.
UniPathway; UPA00204; -.
UniPathway; UPA00880; -.
GeneWiki; GGTLA1; -.
GenomeRNAi; 2687; -.
PRO; PR:P36269; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000099998; -.
CleanEx; HS_GGT5; -.
ExpressionAtlas; P36269; baseline and differential.
Genevisible; P36269; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031226; C:intrinsic component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0036374; F:glutathione hydrolase activity; IDA:UniProtKB.
GO; GO:0102953; F:hypoglycin A gamma-glutamyl transpeptidase activity; IEA:UniProtKB-EC.
GO; GO:0103068; F:leukotriene C4 gamma-glutamyl transferase activity; IEA:UniProtKB-EC.
GO; GO:0002951; F:leukotriene-C(4) hydrolase; IDA:UniProtKB.
GO; GO:0000048; F:peptidyltransferase activity; IDA:BHF-UCL.
GO; GO:0006520; P:cellular amino acid metabolic process; IDA:UniProtKB.
GO; GO:0006631; P:fatty acid metabolic process; IDA:BHF-UCL.
GO; GO:0006750; P:glutathione biosynthetic process; IEA:UniProtKB-KW.
GO; GO:0006751; P:glutathione catabolic process; IDA:UniProtKB.
GO; GO:0006954; P:inflammatory response; IEA:Ensembl.
GO; GO:1901750; P:leukotriene D4 biosynthetic process; IDA:UniProtKB.
GO; GO:0006691; P:leukotriene metabolic process; TAS:Reactome.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
InterPro; IPR000101; GGT_peptidase.
InterPro; IPR029055; Ntn_hydrolases_N.
PANTHER; PTHR11686; PTHR11686; 1.
SUPFAM; SSF56235; SSF56235; 1.
PROSITE; PS00462; G_GLU_TRANSPEPTIDASE; 1.
1: Evidence at protein level;
Acyltransferase; Alternative splicing; Complete proteome;
Glutathione biosynthesis; Glycoprotein; Hydrolase;
Leukotriene biosynthesis; Membrane; Polymorphism; Protease;
Reference proteome; Signal-anchor; Transferase; Transmembrane;
Transmembrane helix; Zymogen.
CHAIN 1 387 Glutathione hydrolase 5 heavy chain.
{ECO:0000250}.
/FTId=PRO_0000011072.
CHAIN 388 586 Glutathione hydrolase 5 light chain.
{ECO:0000250}.
/FTId=PRO_0000011073.
TOPO_DOM 1 8 Cytoplasmic. {ECO:0000255}.
TRANSMEM 9 29 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 30 586 Extracellular. {ECO:0000255}.
REGION 469 470 Glutamate binding. {ECO:0000250}.
ACT_SITE 388 388 Nucleophile. {ECO:0000250}.
BINDING 110 110 Glutamate. {ECO:0000250}.
BINDING 406 406 Glutamate. {ECO:0000250}.
BINDING 427 427 Glutamate. {ECO:0000250}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 303 303 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 347 347 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 535 535 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 550 550 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
VAR_SEQ 101 132 Missing (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_008146.
VAR_SEQ 445 445 P -> PA (in isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_043470.
VARIANT 11 11 L -> I (in dbSNP:rs5760274).
/FTId=VAR_028006.
VARIANT 330 330 K -> R (in dbSNP:rs2275984).
{ECO:0000269|PubMed:10591208,
ECO:0000269|PubMed:1676842}.
/FTId=VAR_028007.
VARIANT 332 332 Q -> H (in dbSNP:rs6004105).
/FTId=VAR_028008.
VARIANT 475 475 I -> V (in dbSNP:rs7288201).
/FTId=VAR_024455.
CONFLICT 408 408 N -> Y (in Ref. 5; CAB55910).
{ECO:0000305}.
CONFLICT 437 437 R -> W (in Ref. 1; AAA58503).
{ECO:0000305}.
SEQUENCE 586 AA; 62261 MW; EE37B3CE516F5788 CRC64;
MARGYGATVS LVLLGLGLAL AVIVLAVVLS RHQAPCGPQA FAHAAVAADS KVCSDIGRAI
LQQQGSPVDA TIAALVCTSV VNPQSMGLGG GVIFTIYNVT TGKVEVINAR ETVPASHAPS
LLDQCAQALP LGTGAQWIGV PGELRGYAEA HRRHGRLPWA QLFQPTIALL RGGHVVAPVL
SRFLHNSILR PSLQASTLRQ LFFNGTEPLR PQDPLPWPAL ATTLETVATE GVEVFYTGRL
GQMLVEDIAK EGSQLTLQDL AKFQPEVVDA LEVPLGDYTL YSPPPPAGGA ILSFILNVLR
GFNFSTESMA RPEGRVNVYH HLVETLKFAK GQRWRLGDPR SHPKLQNASR DLLGETLAQL
IRQQIDGRGD HQLSHYSLAE AWGHGTGTSH VSVLGEDGSA VAATSTINTP FGAMVYSPRT
GIILNNELLD LCERCPRGSG TTPSPVSGDR VGGAPGRCWP PVPGERSPSS MVPSILINKA
QGSKLVIGGA GGELIISAVA QAIMSKLWLG FDLRAAIAAP ILHVNSKGCV EYEPNFSQEV
QRGLQDRGQN QTQRPFFLNV VQAVSQEGAC VYAVSDLRKS GEAAGY


Related products :

Catalog number Product name Quantity
GGNBP2 GGH Gene gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase)
E1384077 gamma-Glutamyl Hydrolase (Conjugase, Folylpolygammaglutamyl Hydrolase) (GGH) ELISA Kit
E1381751 gamma-Glutamyl Hydrolase (Conjugase, Folylpolygammaglutamyl Hydrolase) (GGH) ELISA Kit 1
GGH-1399H Protein Recombinant Human Gamma-Glutamyl Hydrolase (conjugase, folylpolygammaglutamyl hydrolase), His-tagged 0.5mg
GGH-1399H Protein: Recombinant Human Gamma-Glutamyl Hydrolase (conjugase, folylpolygammaglutamyl hydrolase), His-tagged 0.5mg
CSB-EL009389RA Rat gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase) (GGH) ELISA kit, Species Rat, Sample Type serum, plasma 96T
29-608 Gamma-glutamyl transpeptidase is a membrane-bound protein that is important in the metabolism of glutathione. The protein is similar in sequence to several members of the gamma-glutamyl transpeptidase 0.1 mg
CSB-EL009389BO Bovine gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase) (GGH) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL009389HU Human gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase) (GGH) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL009389MO Mouse gamma-glutamyl hydrolase (conjugase, folylpolygammaglutamyl hydrolase) (GGH) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
15-288-22854 Gamma-glutamyl hydrolase - EC 3.4.19.9; Gamma-Glu-X carboxypeptidase; Conjugase; GH Polyclonal 0.05 mg
15-288-22854 Gamma-glutamyl hydrolase - EC 3.4.19.9; Gamma-Glu-X carboxypeptidase; Conjugase; GH Polyclonal 0.1 mg
26-381 GGTL3 is an enzymes involved in both the metabolism of glutathione and in the transpeptidation of amino acids. Changes in the activity of gamma-glutamyltransferase may signal preneoplastic or toxic co 0.05 mg
30-510 GGTL3 is an enzymes involved in both the metabolism of glutathione and in the transpeptidation of amino acids. Changes in the activity of gamma-glutamyltransferase may signal preneoplastic or toxic co 0.05 mg
KA1410 Polyclonal Rabbit Gamma-glutamyltransferase 4 (heavy chain, Cleaved-Thr472) antibody 100ul
GTX109123 Glutamyl Hydrolase gamma 100 µl
DL-gGH-Hu Human Gamma-Glutamyl Hydrolase (gGH) ELISA Kit 96T
'H00008836-P01-10 Gamma-glutamyl hydrolase _ GGH antigen 10
'H00008836-P01-25 Gamma-glutamyl hydrolase _ GGH antigen 25
REN-242 Recombinant Human Gamma-Glutamyl Hydrolase 5
enz-242 Recombinant Human Gamma-Glutamyl Hydrolase 1mg
enz-242 Recombinant Human Gamma-Glutamyl Hydrolase 5
enz-242 Recombinant Human Gamma-Glutamyl Hydrolase 20
CSB-EL009389RA Rat Gamma-glutamyl hydrolase(GGH) ELISA kit 96T
E98038Hu ELISA Kit for Gamma Glutamyl Hydrolase (gGH) 96T/Kit


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur