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Glutathione S-transferase Mu 2 (EC 2.5.1.18) (GST class-mu 2) (GSTM2-2)

 GSTM2_HUMAN             Reviewed;         218 AA.
P28161; B4DRY4; E9PEM9; Q2M318; Q5TZY5; Q8WWE1;
01-APR-1993, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
25-OCT-2017, entry version 181.
RecName: Full=Glutathione S-transferase Mu 2;
EC=2.5.1.18;
AltName: Full=GST class-mu 2;
AltName: Full=GSTM2-2;
Name=GSTM2; Synonyms=GST4;
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).
TISSUE=Muscle;
PubMed=2034681; DOI=10.1073/pnas.88.10.4443;
Vorachek W.R., Pearson W.R., Rule G.S.;
"Cloning, expression, and characterization of a class-mu glutathione
transferase from human muscle, the product of the GST4 locus.";
Proc. Natl. Acad. Sci. U.S.A. 88:4443-4447(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
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).
[3]
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 (OCT-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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 N-TERMINUS.
TISSUE=Testis;
PubMed=8373352; DOI=10.1042/bj2940373;
Ross V.L., Board P.G.;
"Molecular cloning and heterologous expression of an alternatively
spliced human Mu class glutathione S-transferase transcript.";
Biochem. J. 294:373-380(1993).
[7]
PROTEIN SEQUENCE OF 53-69 AND 153-182, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Brain, and Cajal-Retzius cell;
Lubec G., Vishwanath V.;
Submitted (MAR-2007) to UniProtKB.
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE,
AND SUBUNIT.
PubMed=8182750; DOI=10.1006/jmbi.1994.1336;
Raghunathan S., Chandross R.J., Kretsinger R.H., Allison T.J.,
Penington C.J., Rule G.S.;
"Crystal structure of human class mu glutathione transferase GSTM2-2.
Effects of lattice packing on conformational heterogeneity.";
J. Mol. Biol. 238:815-832(1994).
[10]
X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE
ANALOG, FUNCTION, MUTAGENESIS OF THR-210, AND CATALYTIC ACTIVITY.
PubMed=16549767; DOI=10.1073/pnas.0600849103;
Norrgard M.A., Ivarsson Y., Tars K., Mannervik B.;
"Alternative mutations of a positively selected residue elicit gain or
loss of functionalities in enzyme evolution.";
Proc. Natl. Acad. Sci. U.S.A. 103:4876-4881(2006).
[11]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE AND
NBDHEX.
PubMed=19808963; DOI=10.1158/0008-5472.CAN-09-1314;
Federici L., Lo Sterzo C., Pezzola S., Di Matteo A., Scaloni F.,
Federici G., Caccuri A.M.;
"Structural basis for the binding of the anticancer compound 6-(7-
nitro-2,1,3-benzoxadiazol-4-ylthio)hexanol to human glutathione s-
transferases.";
Cancer Res. 69:8025-8034(2009).
-!- FUNCTION: Conjugation of reduced glutathione to a wide number of
exogenous and endogenous hydrophobic electrophiles.
{ECO:0000269|PubMed:16549767}.
-!- CATALYTIC ACTIVITY: RX + glutathione = HX + R-S-glutathione.
{ECO:0000269|PubMed:16549767}.
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16549767,
ECO:0000269|PubMed:19808963, ECO:0000269|PubMed:8182750}.
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P28161-1; Sequence=Displayed;
Name=2;
IsoId=P28161-2; Sequence=VSP_045614;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Muscle.
-!- SIMILARITY: Belongs to the GST superfamily. Mu family.
{ECO:0000305}.
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EMBL; M63509; AAA60963.1; -; mRNA.
EMBL; AK299482; BAG61446.1; -; mRNA.
EMBL; BT019947; AAV38750.1; -; mRNA.
EMBL; AC000031; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC000032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC105038; AAI05039.1; -; mRNA.
EMBL; BC105066; AAI05067.1; -; mRNA.
CCDS; CCDS44192.1; -. [P28161-2]
CCDS; CCDS808.1; -. [P28161-1]
PIR; A39375; A39375.
RefSeq; NP_000839.1; NM_000848.3. [P28161-1]
RefSeq; NP_001135840.1; NM_001142368.1. [P28161-2]
UniGene; Hs.279837; -.
PDB; 1HNA; X-ray; 1.85 A; A=2-218.
PDB; 1HNB; X-ray; 3.50 A; A/B=2-218.
PDB; 1HNC; X-ray; 3.00 A; A/B/C/D=2-218.
PDB; 1XW5; X-ray; 1.80 A; A/B=2-218.
PDB; 1YKC; X-ray; 2.10 A; A/B=2-218.
PDB; 2AB6; X-ray; 2.50 A; A/B/C/D=2-218.
PDB; 2C4J; X-ray; 1.35 A; A/B/C/D=2-218.
PDB; 2GTU; X-ray; 2.55 A; A/B=2-218.
PDB; 3GTU; X-ray; 2.80 A; A/C=2-218.
PDB; 3GUR; X-ray; 2.50 A; A/B/C/D=2-218.
PDBsum; 1HNA; -.
PDBsum; 1HNB; -.
PDBsum; 1HNC; -.
PDBsum; 1XW5; -.
PDBsum; 1YKC; -.
PDBsum; 2AB6; -.
PDBsum; 2C4J; -.
PDBsum; 2GTU; -.
PDBsum; 3GTU; -.
PDBsum; 3GUR; -.
ProteinModelPortal; P28161; -.
SMR; P28161; -.
BioGrid; 109201; 6.
IntAct; P28161; 2.
STRING; 9606.ENSP00000241337; -.
BindingDB; P28161; -.
ChEMBL; CHEMBL4589; -.
DrugBank; DB00143; Glutathione.
DrugBank; DB03310; Oxidized Glutathione Disulfide.
DrugBank; DB04701; S-METHYL-GLUTATHIONE.
SwissLipids; SLP:000001614; -.
iPTMnet; P28161; -.
PhosphoSitePlus; P28161; -.
BioMuta; GSTM2; -.
DMDM; 232204; -.
OGP; P28161; -.
REPRODUCTION-2DPAGE; P28161; -.
EPD; P28161; -.
MaxQB; P28161; -.
PaxDb; P28161; -.
PeptideAtlas; P28161; -.
PRIDE; P28161; -.
DNASU; 2946; -.
Ensembl; ENST00000241337; ENSP00000241337; ENSG00000213366. [P28161-1]
Ensembl; ENST00000442650; ENSP00000416883; ENSG00000213366. [P28161-2]
Ensembl; ENST00000460717; ENSP00000435910; ENSG00000213366. [P28161-2]
GeneID; 2946; -.
KEGG; hsa:2946; -.
UCSC; uc001dyj.4; human. [P28161-1]
CTD; 2946; -.
DisGeNET; 2946; -.
EuPathDB; HostDB:ENSG00000213366.12; -.
GeneCards; GSTM2; -.
HGNC; HGNC:4634; GSTM2.
HPA; CAB040547; -.
HPA; HPA055972; -.
HPA; HPA055973; -.
MIM; 138380; gene.
neXtProt; NX_P28161; -.
OpenTargets; ENSG00000213366; -.
PharmGKB; PA29023; -.
eggNOG; ENOG410IN5J; Eukaryota.
eggNOG; ENOG4110YU0; LUCA.
GeneTree; ENSGT00550000074559; -.
HOGENOM; HOG000115735; -.
HOVERGEN; HBG106842; -.
InParanoid; P28161; -.
KO; K00799; -.
OMA; YANEVAW; -.
PhylomeDB; P28161; -.
TreeFam; TF353040; -.
BRENDA; 2.5.1.18; 2681.
Reactome; R-HSA-156590; Glutathione conjugation.
SABIO-RK; P28161; -.
ChiTaRS; GSTM2; human.
EvolutionaryTrace; P28161; -.
GeneWiki; GSTM2; -.
GenomeRNAi; 2946; -.
PRO; PR:P28161; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000213366; -.
CleanEx; HS_GSTM2; -.
ExpressionAtlas; P28161; baseline and differential.
Genevisible; P28161; HS.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016529; C:sarcoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0043295; F:glutathione binding; IDA:BHF-UCL.
GO; GO:0004602; F:glutathione peroxidase activity; IDA:BHF-UCL.
GO; GO:0004364; F:glutathione transferase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0005102; F:receptor binding; IPI:BHF-UCL.
GO; GO:0070458; P:cellular detoxification of nitrogen compound; IDA:BHF-UCL.
GO; GO:0071313; P:cellular response to caffeine; IDA:BHF-UCL.
GO; GO:1901687; P:glutathione derivative biosynthetic process; TAS:Reactome.
GO; GO:0006749; P:glutathione metabolic process; IDA:UniProtKB.
GO; GO:0043651; P:linoleic acid metabolic process; IDA:BHF-UCL.
GO; GO:0060315; P:negative regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
GO; GO:0018916; P:nitrobenzene metabolic process; IDA:BHF-UCL.
GO; GO:0060316; P:positive regulation of ryanodine-sensitive calcium-release channel activity; IDA:BHF-UCL.
GO; GO:0010881; P:regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion; IC:BHF-UCL.
GO; GO:0010880; P:regulation of release of sequestered calcium ion into cytosol by sarcoplasmic reticulum; IDA:BHF-UCL.
GO; GO:0014809; P:regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion; IC:BHF-UCL.
GO; GO:0055119; P:relaxation of cardiac muscle; TAS:BHF-UCL.
GO; GO:0042178; P:xenobiotic catabolic process; IDA:UniProtKB.
InterPro; IPR010987; Glutathione-S-Trfase_C-like.
InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
InterPro; IPR004045; Glutathione_S-Trfase_N.
InterPro; IPR004046; GST_C.
InterPro; IPR003081; GST_mu.
InterPro; IPR036249; Thioredoxin-like_sf.
Pfam; PF00043; GST_C; 1.
Pfam; PF02798; GST_N; 1.
PRINTS; PR01267; GSTRNSFRASEM.
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; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Phosphoprotein; Polymorphism;
Reference proteome; Transferase.
CHAIN 1 218 Glutathione S-transferase Mu 2.
/FTId=PRO_0000185818.
DOMAIN 2 88 GST N-terminal.
DOMAIN 90 208 GST C-terminal.
REGION 7 8 Glutathione binding.
{ECO:0000269|PubMed:16549767,
ECO:0000269|PubMed:19808963}.
REGION 43 46 Glutathione binding.
{ECO:0000269|PubMed:16549767,
ECO:0000269|PubMed:19808963}.
REGION 59 60 Glutathione binding.
{ECO:0000269|PubMed:16549767,
ECO:0000269|PubMed:19808963}.
REGION 72 73 Glutathione binding.
{ECO:0000269|PubMed:16549767,
ECO:0000269|PubMed:19808963}.
BINDING 50 50 Glutathione.
{ECO:0000250|UniProtKB:P08010}.
BINDING 116 116 Substrate. {ECO:0000250}.
SITE 210 210 Important for substrate specificity.
MOD_RES 27 27 Phosphoserine.
{ECO:0000250|UniProtKB:P08010}.
MOD_RES 44 44 Phosphoserine.
{ECO:0000250|UniProtKB:P08010}.
VAR_SEQ 190 218 GLEKISAYMKSSRFLPRPVFTKMAVWGNK -> HS (in
isoform 2). {ECO:0000305}.
/FTId=VSP_045614.
VARIANT 173 173 S -> N (in dbSNP:rs2229050).
/FTId=VAR_049486.
MUTAGEN 210 210 T->C,F,H,I,K,L,R,Y,W: Reduced enzyme
activity. {ECO:0000269|PubMed:16549767}.
CONFLICT 2 2 P -> S (in Ref. 3; AAV38750).
{ECO:0000305}.
CONFLICT 9 9 N -> D (in Ref. 3; AAV38750).
{ECO:0000305}.
CONFLICT 51 51 F -> L (in Ref. 2; BAG61446).
{ECO:0000305}.
STRAND 3 11 {ECO:0000244|PDB:2C4J}.
HELIX 12 14 {ECO:0000244|PDB:2C4J}.
HELIX 15 23 {ECO:0000244|PDB:2C4J}.
STRAND 28 33 {ECO:0000244|PDB:2C4J}.
TURN 38 41 {ECO:0000244|PDB:2C4J}.
HELIX 44 47 {ECO:0000244|PDB:2C4J}.
TURN 48 51 {ECO:0000244|PDB:2C4J}.
STRAND 60 65 {ECO:0000244|PDB:2C4J}.
STRAND 68 72 {ECO:0000244|PDB:2C4J}.
HELIX 73 83 {ECO:0000244|PDB:2C4J}.
HELIX 91 116 {ECO:0000244|PDB:2C4J}.
HELIX 120 142 {ECO:0000244|PDB:2C4J}.
STRAND 150 152 {ECO:0000244|PDB:2C4J}.
HELIX 155 170 {ECO:0000244|PDB:2C4J}.
TURN 172 177 {ECO:0000244|PDB:2C4J}.
HELIX 179 190 {ECO:0000244|PDB:2C4J}.
HELIX 192 199 {ECO:0000244|PDB:2C4J}.
STRAND 200 202 {ECO:0000244|PDB:1XW5}.
STRAND 205 207 {ECO:0000244|PDB:1HNC}.
TURN 208 212 {ECO:0000244|PDB:1HNA}.
STRAND 214 216 {ECO:0000244|PDB:2C4J}.
SEQUENCE 218 AA; 25745 MW; 15203709D4A63789 CRC64;
MPMTLGYWNI RGLAHSIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK FKLGLDFPNL
PYLIDGTHKI TQSNAILRYI ARKHNLCGES EKEQIREDIL ENQFMDSRMQ LAKLCYDPDF
EKLKPEYLQA LPEMLKLYSQ FLGKQPWFLG DKITFVDFIA YDVLERNQVF EPSCLDAFPN
LKDFISRFEG LEKISAYMKS SRFLPRPVFT KMAVWGNK


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E0609h ELISA kit Glutathione S-transferase A3,Glutathione S-transferase A3-3,GST class-alpha member 3,GSTA3,Homo sapiens,Human 96T
E0609m ELISA kit Glutathione S-transferase A2,Glutathione S-transferase GT41A,GST class-alpha member 2,Gsta2,Mouse,Mus musculus 96T
CSB-EL009981RA Rat Glutathione S-transferase Mu 2(GSTM2) ELISA kit 96T
enz-003 Recombinant Human Glutathione S-Transferase MU 2 GSTM2 5
enz-003 Recombinant Human Glutathione S-Transferase MU 2 GSTM2 20
enz-003 Recombinant Human Glutathione S-Transferase MU 2 GSTM2 1mg
CSB-EL009981HU Human Glutathione S-transferase Mu 2(GSTM2) ELISA kit 96T
CSB-EL009981CH Chicken Glutathione S-transferase Mu 2(GSTM2) ELISA kit 96T


 

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