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Glutathione S-transferase P 1 (Gst P1) (EC 2.5.1.18) (GST YF-YF) (GST class-pi) (GST-piB) (Preadipocyte growth factor)

 GSTP1_MOUSE             Reviewed;         210 AA.
P19157; Q8BNY4;
01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
30-AUG-2017, entry version 176.
RecName: Full=Glutathione S-transferase P 1;
Short=Gst P1;
EC=2.5.1.18;
AltName: Full=GST YF-YF;
AltName: Full=GST class-pi;
AltName: Full=GST-piB;
AltName: Full=Preadipocyte growth factor;
Name=Gstp1; Synonyms=Gstpib;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ; TISSUE=Liver;
PubMed=2388840; DOI=10.1093/nar/18.15.4606;
Hatayama I., Satoh K., Sato K.;
"A cDNA sequence coding a class pi glutathione S-transferase of
mouse.";
Nucleic Acids Res. 18:4606-4606(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8135745; DOI=10.1042/bj2980385;
Bammler T.K., Smith C.A.D., Wolf R.C.;
"Isolation and characterization of two mouse PI class glutathione S-
transferase genes.";
Biochem. J. 298:385-390(1994).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ; TISSUE=Liver;
PubMed=7982937;
Xu X., Stambrook P.J.;
"Two murine GSTpi genes are arranged in tandem and are differentially
expressed.";
J. Biol. Chem. 269:30268-30273(1994).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
Kawada T., Aoki N., Kamei Y., Sugimoto E.;
"Molecular cloning of mouse preadipocyte growth factor.";
Submitted (MAY-1994) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[6]
PROTEIN SEQUENCE OF 2-12; 56-71; 122-141 AND 192-209, AND
IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=C57BL/6J; TISSUE=Brain, and Hippocampus;
Lubec G., Klug S., Kang S.U.;
Submitted (APR-2007) to UniProtKB.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-210.
STRAIN=C57BL/6J; TISSUE=Embryo;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[8]
CHARACTERIZATION, AND MASS SPECTROMETRY.
STRAIN=CD-1; TISSUE=Liver;
PubMed=8605288; DOI=10.1021/tx00050a009;
Mitchell A.E., Morin D., Lame M.W., Jones A.D.;
"Purification, mass spectrometric characterization, and covalent
modification of murine glutathione S-transferases.";
Chem. Res. Toxicol. 8:1054-1062(1995).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-103 AND LYS-116, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[11]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE
ANALOGS.
PubMed=8145243; DOI=10.1006/jmbi.1994.1232;
Garcia-Saez I., Parraga A., Phillips M.F., Mantle T.J., Coll M.;
"Molecular structure at 1.8 A of mouse liver class pi glutathione S-
transferase complexed with S-(p-nitrobenzyl)glutathione and other
inhibitors.";
J. Mol. Biol. 237:298-314(1994).
[12]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=9446594; DOI=10.1074/jbc.273.5.2844;
Vega M.C., Walsh S.B., Mantle T.J., Coll M.;
"The three-dimensional structure of Cys-47-modified mouse liver
glutathione S-transferase P1-1. Carboxymethylation dramatically
decreases the affinity for glutathione and is associated with a loss
of electron density in the alphaB-310B region.";
J. Biol. Chem. 273:2844-2850(1998).
-!- FUNCTION: Conjugation of reduced glutathione to a wide number of
exogenous and endogenous hydrophobic electrophiles. Can metabolize
1-chloro-2,4-dinitrobenzene. Regulates negatively CDK5 activity
via p25/p35 translocation to prevent neurodegeneration (By
similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
-!- SUBUNIT: Homodimer. Interacts with CDK5 (By similarity).
{ECO:0000250}.
-!- INTERACTION:
O08709:Prdx6; NbExp=2; IntAct=EBI-2309446, EBI-444895;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Mitochondrion
{ECO:0000250}. Nucleus {ECO:0000250}. Note=The 83 N-terminal amino
acids function as un uncleaved transit peptide, and arginine
residues within it are crucial for mitochondrial localization.
{ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
-!- MASS SPECTROMETRY: Mass=23478.8; Mass_error=2;
Method=Electrospray; Range=2-210;
Evidence={ECO:0000269|PubMed:8605288};
-!- SIMILARITY: Belongs to the GST superfamily. Pi family.
{ECO:0000305}.
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EMBL; X53451; CAA37529.1; -; mRNA.
EMBL; X76143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U15654; AAA64837.1; -; Genomic_DNA.
EMBL; D30687; BAA06349.1; -; mRNA.
EMBL; BC002048; AAH02048.1; -; mRNA.
EMBL; BC061109; AAH61109.1; -; mRNA.
EMBL; AK079144; BAC37560.1; -; mRNA.
CCDS; CCDS29411.1; -.
PIR; S12709; B55140.
RefSeq; NP_038569.1; NM_013541.1.
UniGene; Mm.299292; -.
PDB; 1BAY; X-ray; 2.00 A; A/B=2-210.
PDB; 1GLP; X-ray; 1.90 A; A/B=2-210.
PDB; 1GLQ; X-ray; 1.80 A; A/B=2-210.
PDB; 1GSY; X-ray; 2.44 A; A/B=2-210.
PDB; 1GTI; X-ray; 3.00 A; A/B/C/D/E/F=2-210.
PDB; 2GLR; X-ray; 2.20 A; A/B=2-210.
PDB; 2OA7; X-ray; 2.20 A; A/B=2-210.
PDB; 2OAC; X-ray; 2.20 A; A/B=2-210.
PDB; 2OAD; X-ray; 2.50 A; A/B=2-210.
PDB; 3O76; X-ray; 1.77 A; A/B=2-210.
PDBsum; 1BAY; -.
PDBsum; 1GLP; -.
PDBsum; 1GLQ; -.
PDBsum; 1GSY; -.
PDBsum; 1GTI; -.
PDBsum; 2GLR; -.
PDBsum; 2OA7; -.
PDBsum; 2OAC; -.
PDBsum; 2OAD; -.
PDBsum; 3O76; -.
ProteinModelPortal; P19157; -.
SMR; P19157; -.
BioGrid; 200101; 3.
IntAct; P19157; 6.
MINT; MINT-1869068; -.
STRING; 10090.ENSMUSP00000129565; -.
iPTMnet; P19157; -.
PhosphoSitePlus; P19157; -.
SwissPalm; P19157; -.
REPRODUCTION-2DPAGE; P19157; -.
SWISS-2DPAGE; P19157; -.
EPD; P19157; -.
MaxQB; P19157; -.
PaxDb; P19157; -.
PeptideAtlas; P19157; -.
PRIDE; P19157; -.
TopDownProteomics; P19157; -.
Ensembl; ENSMUST00000169613; ENSMUSP00000129565; ENSMUSG00000060803.
Ensembl; ENSMUST00000180480; ENSMUSP00000138073; ENSMUSG00000097830.
GeneID; 14870; -.
KEGG; mmu:14870; -.
UCSC; uc008fyf.1; mouse.
CTD; 2950; -.
MGI; MGI:95865; Gstp1.
eggNOG; KOG1695; Eukaryota.
eggNOG; ENOG4111VAU; LUCA.
GeneTree; ENSGT00550000074559; -.
HOGENOM; HOG000115733; -.
HOVERGEN; HBG108324; -.
InParanoid; P19157; -.
KO; K00799; -.
OMA; LRCKYAT; -.
OrthoDB; EOG091G0K2E; -.
PhylomeDB; P19157; -.
TreeFam; TF105321; -.
BRENDA; 2.5.1.18; 3474.
Reactome; R-MMU-156590; Glutathione conjugation.
Reactome; R-MMU-3299685; Detoxification of Reactive Oxygen Species.
Reactome; R-MMU-6798695; Neutrophil degranulation.
EvolutionaryTrace; P19157; -.
PRO; PR:P19157; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000060803; -.
CleanEx; MM_GSTP1; -.
Genevisible; P19157; MM.
GO; GO:0005737; C:cytoplasm; ISS:BHF-UCL.
GO; GO:0005829; C:cytosol; ISS:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005622; C:intracellular; IDA:BHF-UCL.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005634; C:nucleus; ISS:BHF-UCL.
GO; GO:0005886; C:plasma membrane; ISS:BHF-UCL.
GO; GO:0043234; C:protein complex; IDA:BHF-UCL.
GO; GO:0097057; C:TRAF2-GSTP1 complex; ISO:MGI.
GO; GO:0031982; C:vesicle; ISO:MGI.
GO; GO:0035731; F:dinitrosyl-iron complex binding; ISO:MGI.
GO; GO:0008144; F:drug binding; ISS:BHF-UCL.
GO; GO:0004602; F:glutathione peroxidase activity; ISO:MGI.
GO; GO:0004364; F:glutathione transferase activity; IDA:MGI.
GO; GO:0008432; F:JUN kinase binding; IPI:BHF-UCL.
GO; GO:0019207; F:kinase regulator activity; IMP:BHF-UCL.
GO; GO:0035730; F:S-nitrosoglutathione binding; ISO:MGI.
GO; GO:0031100; P:animal organ regeneration; ISS:BHF-UCL.
GO; GO:0071460; P:cellular response to cell-matrix adhesion; ISS:BHF-UCL.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; ISS:BHF-UCL.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; ISS:BHF-UCL.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:BHF-UCL.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:BHF-UCL.
GO; GO:0035726; P:common myeloid progenitor cell proliferation; IMP:BHF-UCL.
GO; GO:0006749; P:glutathione metabolic process; IDA:MGI.
GO; GO:0002674; P:negative regulation of acute inflammatory response; NAS:BHF-UCL.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:BHF-UCL.
GO; GO:0009890; P:negative regulation of biosynthetic process; IDA:BHF-UCL.
GO; GO:0070373; P:negative regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; ISS:BHF-UCL.
GO; GO:0048147; P:negative regulation of fibroblast proliferation; IMP:BHF-UCL.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:BHF-UCL.
GO; GO:0032691; P:negative regulation of interleukin-1 beta production; IDA:BHF-UCL.
GO; GO:0043508; P:negative regulation of JUN kinase activity; IDA:BHF-UCL.
GO; GO:0070664; P:negative regulation of leukocyte proliferation; IMP:BHF-UCL.
GO; GO:0043407; P:negative regulation of MAP kinase activity; ISS:BHF-UCL.
GO; GO:0071638; P:negative regulation of monocyte chemotactic protein-1 production; IDA:BHF-UCL.
GO; GO:2000429; P:negative regulation of neutrophil aggregation; NAS:BHF-UCL.
GO; GO:0051771; P:negative regulation of nitric-oxide synthase biosynthetic process; IDA:BHF-UCL.
GO; GO:2000469; P:negative regulation of peroxidase activity; IDA:BHF-UCL.
GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IDA:BHF-UCL.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:BHF-UCL.
GO; GO:0014003; P:oligodendrocyte development; ISS:BHF-UCL.
GO; GO:0032930; P:positive regulation of superoxide anion generation; IMP:BHF-UCL.
GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; IDA:BHF-UCL.
GO; GO:0032872; P:regulation of stress-activated MAPK cascade; IDA:BHF-UCL.
GO; GO:0043200; P:response to amino acid; ISS:BHF-UCL.
GO; GO:0032355; P:response to estradiol; ISS:BHF-UCL.
GO; GO:0045471; P:response to ethanol; ISS:BHF-UCL.
GO; GO:0033591; P:response to L-ascorbic acid; ISS:BHF-UCL.
GO; GO:0031667; P:response to nutrient levels; ISS:BHF-UCL.
GO; GO:0000302; P:response to reactive oxygen species; IDA:BHF-UCL.
GO; GO:0009636; P:response to toxic substance; ISS:BHF-UCL.
GO; GO:0006805; P:xenobiotic metabolic process; ISS:UniProtKB.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR003082; GST_pi.
InterPro; IPR012336; Thioredoxin-like_fold.
Pfam; PF14497; GST_C_3; 1.
Pfam; PF02798; GST_N; 1.
PRINTS; PR01268; GSTRNSFRASEP.
SUPFAM; SSF47616; SSF47616; 1.
SUPFAM; SSF52833; SSF52833; 1.
PROSITE; PS50405; GST_CTER; 1.
PROSITE; PS50404; GST_NTER; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Complete proteome; Cytoplasm;
Direct protein sequencing; Mitochondrion; Nucleus; Phosphoprotein;
Reference proteome; Transferase.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.6}.
CHAIN 2 210 Glutathione S-transferase P 1.
/FTId=PRO_0000185903.
DOMAIN 2 81 GST N-terminal.
DOMAIN 83 204 GST C-terminal.
REGION 52 53 Glutathione binding.
{ECO:0000305|PubMed:8145243}.
REGION 65 66 Glutathione binding.
{ECO:0000305|PubMed:8145243}.
BINDING 8 8 Glutathione.
{ECO:0000305|PubMed:8145243}.
BINDING 14 14 Glutathione.
{ECO:0000305|PubMed:8145243}.
BINDING 39 39 Glutathione.
{ECO:0000305|PubMed:8145243}.
BINDING 45 45 Glutathione.
{ECO:0000305|PubMed:8145243}.
MOD_RES 4 4 Phosphotyrosine; by EGFR.
{ECO:0000250|UniProtKB:P09211}.
MOD_RES 62 62 Phosphothreonine.
{ECO:0000250|UniProtKB:P09211}.
MOD_RES 103 103 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 116 116 N6-succinyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 128 128 N6-acetyllysine.
{ECO:0000250|UniProtKB:P09211}.
STRAND 4 8 {ECO:0000244|PDB:3O76}.
STRAND 10 12 {ECO:0000244|PDB:3O76}.
HELIX 13 15 {ECO:0000244|PDB:3O76}.
HELIX 16 24 {ECO:0000244|PDB:3O76}.
STRAND 29 33 {ECO:0000244|PDB:3O76}.
HELIX 36 40 {ECO:0000244|PDB:3O76}.
STRAND 42 44 {ECO:0000244|PDB:1GLQ}.
HELIX 45 47 {ECO:0000244|PDB:3O76}.
STRAND 49 51 {ECO:0000244|PDB:1GTI}.
STRAND 55 58 {ECO:0000244|PDB:3O76}.
STRAND 61 65 {ECO:0000244|PDB:3O76}.
HELIX 66 77 {ECO:0000244|PDB:3O76}.
HELIX 84 110 {ECO:0000244|PDB:3O76}.
HELIX 112 135 {ECO:0000244|PDB:3O76}.
HELIX 138 140 {ECO:0000244|PDB:3O76}.
STRAND 144 148 {ECO:0000244|PDB:1GLQ}.
HELIX 151 166 {ECO:0000244|PDB:3O76}.
TURN 168 173 {ECO:0000244|PDB:3O76}.
HELIX 175 186 {ECO:0000244|PDB:3O76}.
HELIX 188 195 {ECO:0000244|PDB:3O76}.
HELIX 197 200 {ECO:0000244|PDB:3O76}.
STRAND 204 208 {ECO:0000244|PDB:3O76}.
SEQUENCE 210 AA; 23609 MW; DAC7762F4E34FF27 CRC64;
MPPYTIVYFP VRGRCEAMRM LLADQGQSWK EEVVTIDTWM QGLLKPTCLY GQLPKFEDGD
LTLYQSNAIL RHLGRSLGLY GKNQREAAQM DMVNDGVEDL RGKYVTLIYT NYENGKNDYV
KALPGHLKPF ETLLSQNQGG KAFIVGDQIS FADYNLLDLL LIHQVLAPGC LDNFPLLSAY
VARLSARPKI KAFLSSPEHV NRPINGNGKQ


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U0609h CLIA Glutathione S-transferase A3,Glutathione S-transferase A3-3,GST class-alpha member 3,GSTA3,Homo sapiens,Human 96T
U0609h CLIA Glutathione S-transferase A5,Glutathione S-transferase A5-5,GST class-alpha member 5,GSTA5,Homo sapiens,Human 96T
U0609h CLIA Glutathione S-transferase A4,Glutathione S-transferase A4-4,GST class-alpha member 4,GSTA4,Homo sapiens,Human 96T
E0609h ELISA Glutathione S-transferase A4,Glutathione S-transferase A4-4,GST class-alpha member 4,GSTA4,Homo sapiens,Human 96T
E0609m ELISA Glutathione S-transferase 5.7,Glutathione S-transferase A4,GST 5.7,GST A4-4,GST class-alpha member 4,Gsta,Gsta4,GSTA4-4,Mouse,Mus musculus 96T
U0609m CLIA Glutathione S-transferase 5.7,Glutathione S-transferase A4,GST 5.7,GST A4-4,GST class-alpha member 4,Gsta,Gsta4,GSTA4-4,Mouse,Mus musculus 96T
E0609m ELISA kit Glutathione S-transferase 5.7,Glutathione S-transferase A4,GST 5.7,GST A4-4,GST class-alpha member 4,Gsta,Gsta4,GSTA4-4,Mouse,Mus musculus 96T
U0609b CLIA Bos taurus,Bovine,Glutathione S-transferase A1,Glutathione S-transferase alpha-1,GST class-alpha member 1,GSTA1 96T


 

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