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Protein O-GlcNAcase (OGA) (EC 3.2.1.169) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (Bifunctional protein NCOAT) (Meningioma-expressed antigen 5) (N-acetyl-beta-D-glucosaminidase) (EC 3.2.1.52) (N-acetyl-beta-glucosaminidase)

 OGA_MOUSE               Reviewed;         916 AA.
Q9EQQ9; Q3ULY7; Q6ZQ71; Q8BK05; Q8BTT2; Q8CFX2; Q9CSJ4; Q9CUR7;
03-OCT-2006, integrated into UniProtKB/Swiss-Prot.
01-OCT-2001, sequence version 2.
27-SEP-2017, entry version 122.
RecName: Full=Protein O-GlcNAcase {ECO:0000303|PubMed:16517082};
Short=OGA;
EC=3.2.1.169 {ECO:0000269|PubMed:16517082};
AltName: Full=Beta-N-acetylhexosaminidase;
AltName: Full=Beta-hexosaminidase;
AltName: Full=Bifunctional protein NCOAT {ECO:0000303|PubMed:16356930, ECO:0000303|PubMed:16517082};
AltName: Full=Meningioma-expressed antigen 5 {ECO:0000303|PubMed:11341771};
AltName: Full=N-acetyl-beta-D-glucosaminidase;
EC=3.2.1.52 {ECO:0000269|PubMed:16517082};
AltName: Full=N-acetyl-beta-glucosaminidase;
Name=Mgea5; Synonyms=Hexc, Kiaa0679;
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] (ISOFORM 1).
Csoka A.B.;
"Mgea5, the murine homolog of a neutral-active cytosolic beta-N-
acetylglucosaminidase, localized on chromosome 19.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-603 (ISOFORM 1), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 1-77 (ISOFORM 3).
STRAIN=C57BL/6J, and NOD; TISSUE=Head, Mammary gland, and Thymus;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=FVB/N-3; TISSUE=Kidney, and Mammary tumor;
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).
[5]
PROTEIN SEQUENCE OF 109-127, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[6]
PROTEIN SEQUENCE OF 157-167; 775-785 AND 875-886.
PubMed=16356930; DOI=10.1074/jbc.M510485200;
Toleman C.A., Paterson A.J., Kudlow J.E.;
"The histone acetyltransferase NCOAT contains a zinc finger-like motif
involved in substrate recognition.";
J. Biol. Chem. 281:3918-3925(2006).
[7]
DEVELOPMENTAL STAGE.
PubMed=11341771; DOI=10.1006/bbrc.2001.4815;
Comtesse N., Maldener E., Meese E.;
"Identification of a nuclear variant of MGEA5, a cytoplasmic
hyaluronidase and a beta-N-acetylglucosaminidase.";
Biochem. Biophys. Res. Commun. 283:634-640(2001).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[9]
IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC ACTIVITY, FUNCTION,
BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF CYS-166; ASP-174;
ASP-175; ASP-177 AND CYS-878.
PubMed=16517082; DOI=10.1016/j.bbagen.2006.01.017;
Toleman C., Paterson A.J., Kudlow J.E.;
"Location and characterization of the O-GlcNAcase active site.";
Biochim. Biophys. Acta 1760:829-839(2006).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-364, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, 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).
[12]
INTERACTION WITH CLOCK, AND INDUCTION.
PubMed=23395175; DOI=10.1016/j.cmet.2012.12.017;
Kaasik K., Kivimae S., Allen J.J., Chalkley R.J., Huang Y., Baer K.,
Kissel H., Burlingame A.L., Shokat K.M., Ptacek L.J., Fu Y.H.;
"Glucose sensor O-GlcNAcylation coordinates with phosphorylation to
regulate circadian clock.";
Cell Metab. 17:291-302(2013).
-!- FUNCTION: Cleaves GlcNAc but not GalNAc from O-glycosylated
proteins. Can use p-nitrophenyl-beta-GlcNAc and 4-
methylumbelliferone-GlcNAc as substrates but not p-nitrophenyl-
beta-GalNAc or p-nitrophenyl-alpha-GlcNAc (in vitro)
(PubMed:16517082). Does not bind acetyl-CoA and does not have
histone acetyltransferase activity. {ECO:0000250|UniProtKB:O60502,
ECO:0000269|PubMed:16517082}.
-!- CATALYTIC ACTIVITY: [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-
L-serine + H(2)O = [protein]-L-serine + N-acetyl-D-glucosamine.
{ECO:0000269|PubMed:16517082}.
-!- CATALYTIC ACTIVITY: [Protein]-3-O-(N-acetyl-beta-D-glucosaminyl)-
L-threonine + H(2)O = [protein]-L-threonine + N-acetyl-D-
glucosamine. {ECO:0000269|PubMed:16517082}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing N-acetyl-
D-hexosamine residues in N-acetyl-beta-D-hexosaminides.
{ECO:0000269|PubMed:16517082}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.49 mM for pNP-GlcNAc {ECO:0000269|PubMed:16517082};
pH dependence:
Optimum pH is 6.5-7. {ECO:0000269|PubMed:16517082};
-!- SUBUNIT: Monomer (By similarity). Interacts with CLOCK.
{ECO:0000250|UniProtKB:O60502, ECO:0000269|PubMed:23395175}.
-!- INTERACTION:
P62806:Hist4h4; NbExp=2; IntAct=EBI-8321615, EBI-299632;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9EQQ9-1; Sequence=Displayed;
Name=2;
IsoId=Q9EQQ9-2; Sequence=VSP_020870, VSP_020872;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9EQQ9-3; Sequence=VSP_020871;
Note=No experimental confirmation available.;
-!- DEVELOPMENTAL STAGE: Expressed throughout development from
blastocyst stage to embryonic day 16.5.
{ECO:0000269|PubMed:11341771}.
-!- INDUCTION: Expression in the liver oscillates in a circadian
manner with peak levels at CT8-CT12.
{ECO:0000269|PubMed:23395175}.
-!- PTM: Proteolytically cleaved by caspase-3 during apoptosis. The
fragments interact with each other; cleavage does not decrease
enzyme activity. {ECO:0000250|UniProtKB:O60502}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 84 family.
{ECO:0000305}.
-!- CAUTION: Was initially identified as a bi-functional protein that
has an N-terminal domain with O-GlcNAcase activity and a C-
terminal domain with histone acetyltransferase activity
(PubMed:16356930). The histone acetyltransferase activity was
detected only when the protein was expressed in mammalian cells,
but not when expressed in bacterial cells, suggesting that the
histone acetyltransferase activity might be due to the presence of
a contaminant. Characterization of the human protein shows that
this protein does not bind acetyl-CoA and therefore cannot have
acetyltransferase activity. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH41109.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=BAC97998.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAE26311.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF132214; AAG43273.2; -; mRNA.
EMBL; AK129188; BAC97998.1; ALT_INIT; mRNA.
EMBL; BC041109; AAH41109.1; ALT_SEQ; mRNA.
EMBL; BC054821; AAH54821.1; -; mRNA.
EMBL; AK012695; BAB28416.1; -; mRNA.
EMBL; AK014781; BAB29550.1; -; mRNA.
EMBL; AK077613; BAC36900.1; -; mRNA.
EMBL; AK088774; BAC40564.1; -; mRNA.
EMBL; AK145227; BAE26311.1; ALT_INIT; mRNA.
CCDS; CCDS29866.1; -. [Q9EQQ9-1]
RefSeq; NP_076288.1; NM_023799.3. [Q9EQQ9-1]
UniGene; Mm.122725; -.
UniGene; Mm.435821; -.
UniGene; Mm.440640; -.
UniGene; Mm.480399; -.
ProteinModelPortal; Q9EQQ9; -.
BioGrid; 217934; 4.
IntAct; Q9EQQ9; 3.
MINT; MINT-2844950; -.
STRING; 10090.ENSMUSP00000026243; -.
CAZy; GH84; Glycoside Hydrolase Family 84.
iPTMnet; Q9EQQ9; -.
PhosphoSitePlus; Q9EQQ9; -.
EPD; Q9EQQ9; -.
PaxDb; Q9EQQ9; -.
PeptideAtlas; Q9EQQ9; -.
PRIDE; Q9EQQ9; -.
Ensembl; ENSMUST00000026243; ENSMUSP00000026243; ENSMUSG00000025220. [Q9EQQ9-1]
GeneID; 76055; -.
KEGG; mmu:76055; -.
UCSC; uc008hrm.1; mouse. [Q9EQQ9-2]
UCSC; uc008hrn.1; mouse. [Q9EQQ9-1]
CTD; 10724; -.
MGI; MGI:1932139; Mgea5.
eggNOG; KOG3698; Eukaryota.
eggNOG; ENOG410XPBQ; LUCA.
GeneTree; ENSGT00390000007726; -.
HOVERGEN; HBG053044; -.
InParanoid; Q9EQQ9; -.
KO; K15719; -.
OMA; WLGCRSQ; -.
OrthoDB; EOG091G02T9; -.
PhylomeDB; Q9EQQ9; -.
TreeFam; TF313732; -.
BRENDA; 2.3.1.48; 3474.
BRENDA; 3.2.1.169; 3474.
ChiTaRS; Mgea5; mouse.
PRO; PR:Q9EQQ9; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000025220; -.
CleanEx; MM_MGEA5; -.
Genevisible; Q9EQQ9; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0016020; C:membrane; ISO:MGI.
GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
GO; GO:0102167; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
GO; GO:0102571; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-serine/L-threonine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
GO; GO:0102166; F:[protein]-3-O-(N-acetyl-D-glucosaminyl)-L-threonine O-N-acetyl-alpha-D-glucosaminase activity; IEA:UniProtKB-EC.
GO; GO:0016231; F:beta-N-acetylglucosaminidase activity; ISO:MGI.
GO; GO:0102148; F:N-acetyl-beta-D-galactosaminidase activity; IEA:UniProtKB-EC.
GO; GO:0009100; P:glycoprotein metabolic process; IBA:GO_Central.
GO; GO:0006044; P:N-acetylglucosamine metabolic process; ISO:MGI.
GO; GO:0006517; P:protein deglycosylation; ISO:MGI.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR011496; Beta-N-acetylglucosaminidase.
InterPro; IPR017853; Glycoside_hydrolase_SF.
Pfam; PF07555; NAGidase; 1.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF55729; SSF55729; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Glycosidase; Hydrolase; Nucleus;
Phosphoprotein; Reference proteome.
CHAIN 1 916 Protein O-GlcNAcase.
/FTId=PRO_0000252119.
REGION 278 280 Substrate binding.
{ECO:0000250|UniProtKB:Q2CEE3}.
ACT_SITE 175 175 Proton donor.
{ECO:0000250|UniProtKB:O60502}.
BINDING 67 67 Substrate; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q2CEE3}.
BINDING 98 98 Substrate.
{ECO:0000250|UniProtKB:Q0TR53}.
BINDING 174 174 Substrate. {ECO:0000305|PubMed:16517082}.
BINDING 219 219 Substrate.
{ECO:0000250|UniProtKB:Q2CEE3}.
BINDING 285 285 Substrate.
{ECO:0000250|UniProtKB:Q2CEE3}.
BINDING 313 313 Substrate.
{ECO:0000250|UniProtKB:Q2CEE3}.
SITE 413 414 Cleavage; by caspase-3.
{ECO:0000250|UniProtKB:O60502}.
MOD_RES 364 364 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:21183079}.
VAR_SEQ 1 698 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020870.
VAR_SEQ 1 1 M -> MVRPRVWRSSRRVASQNGLRAFGPTDRGRRGAVAGG
RRM (in isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020871.
VAR_SEQ 699 725 NDLFFQPPPLTPTSKVYTIRPYFPKDE -> MYTTHSCLYS
FFLTFFLVCCLTRLYFQ (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_020872.
MUTAGEN 166 166 C->S: No change in substrate affinity but
60% reduction in O-GlcNAcase activity.
{ECO:0000269|PubMed:16517082}.
MUTAGEN 174 174 D->N: 2-fold increase in substrate
affinity and 77% reduction in O-GlcNAcase
activity. Regains appreciable level of
catalytic efficiency in the acidic pH
range. No recovery of activity in the
presence of sodium azide.
{ECO:0000269|PubMed:16517082}.
MUTAGEN 175 175 D->A: 3-fold increase in substrate
affinity and 90% reduction in O-GlcNAcase
activity. Regains appreciable level of
catalytic efficiency in the acidic pH
range. 70% recovery of activity in the
presence of sodium azide.
{ECO:0000269|PubMed:16517082}.
MUTAGEN 177 177 D->N: 2-fold decrease in substrate
affinity and 96% reduction in O-GlcNAcase
activity. Regains appreciable level of
catalytic efficiency in the acidic pH
range. 40% recovery of activity in the
presence of sodium azide.
{ECO:0000269|PubMed:16517082}.
MUTAGEN 878 878 C->S: No effect on O-GlcNAcase activity.
{ECO:0000269|PubMed:16517082}.
CONFLICT 6 6 S -> T (in Ref. 3; BAE26311).
{ECO:0000305}.
CONFLICT 52 53 GA -> RT (in Ref. 3; BAE26311).
{ECO:0000305}.
CONFLICT 742 742 F -> S (in Ref. 2; BAC97998).
{ECO:0000305}.
SEQUENCE 916 AA; 103162 MW; B2FAC6F10E03C5CA CRC64;
MVQKESQAAL EERESERNAN PAAASGASLE QSVAPAPGED NPSGAGAAAV VGAAGGARRF
LCGVVEGFYG RPWVMEQRKE LFRRLQKWEL NTYLYAPKDD YKHRMFWREM YSVEEAEQLM
TLISAAREYE IEFIYAISPG LDITFSNPKE VSTLKRKLDQ VSQFGCRSFA LLFDDIDHNM
CAADKEVFSS FAHAQVSITN EIYQYLGEPE TFLFCPTEYC GTFCYPNVSQ SPYLRTVGEK
LLPGIEVLWT GPKVVSKEIP VESIEEVSKI IKRAPVIWDN IHANDYDQKR LFLGPYKGRS
TELIPRLKGV LTNPNCEFEA NYVAIHTLAT WYKSNMNGVR KDVVMTDSED STVSIQIKLE
NEGSDEDIET DVLYSPQMAL KLALTEWLQE FGVPHQYSSR QVAHSGAKTS VVDGTPLVAA
PSLNATTVVT TVYQEPIMSQ GAALSGEPSV LTKEEEKKQP DEEPMDMVVE KQEEAEHKND
NQILTEIVEA KMAEELRPMD TDKESMAESK SPEMSMQEDC IPDVAPMQTD EQTQKEQFVP
GPNEKPLYTA EPVTLEDLQL LADLFYLPYE HGPKGAQMLR EFQWLRANSS VVSVNCKGKD
SEKIEEWRSR AAKFEEMCAL VMGMFTRLSN CANRTILYDM YSYVWDIKSI MSMVKSFVQW
LGCRSHSSAQ FLIGDQEPWA FRGGLAGEFQ RLLPIDGAND LFFQPPPLTP TSKVYTIRPY
FPKDEASVYK ICREMYDDGV GFPFQSQPDL IGDKLVGGLL SLSLDYCFVL EDEDGICGYA
LGTVDVTPFI KKCKISWIPF MQEKYTKPNG DKELSEAEKI MLSFHEEQEV LPETFLANFP
SLIKMDIHKK VTDPSVAKSM MACLLSSLKA NGSRGAFCEV RPDDKRILEF YSKLGCFEIA
KMEGFPKDVV ILGRSL


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E0195r ELISA kit Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Hexa,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha,Rat,Rattus norvegicus 96T
EIAAB26576 Bifunctional protein NCOAT,Hexc,Kiaa0679,Meningioma-expressed antigen 5,Mgea5,Mouse,Mus musculus,Nuclear cytoplasmic O-GlcNAcase and acetyltransferase
EIAAB26575 Bifunctional protein NCOAT,Hexc,Mea5,Meningioma-expressed antigen 5,Mgea5,Nuclear cytoplasmic O-GlcNAcase and acetyltransferase,Rat,Rattus norvegicus
EIAAB26577 Bifunctional protein NCOAT,HEXC,Homo sapiens,Human,KIAA0679,MEA5,Meningioma-expressed antigen 5,MGEA5,Nuclear cytoplasmic O-GlcNAcase and acetyltransferase
EM1225 N-Acetyl Beta-D-Glucosaminidase Elisa Kit 96T
EH3404 N-Acetyl Beta-D-Glucosaminidase Elisa Kit 96T
ER1177 N-Acetyl Beta-D-Glucosaminidase Elisa Kit 96T
E12411417 Rat N-Acetyl Beta D Glucosaminidase(NAG) ELISA Kit 1
E13812064 N-Acetyl beta-D-Glucosaminidase (NAG) ELISA Kit 1
E12531317 Mouse N-Acetyl Beta D Glucosaminidase(NAG) ELISA Kit 1
22842 Human N-Acetyl Beta D Glucosaminidase(NAG) ELISA Kit 96T
E-EL-R0647 Rat NAGase (N-Acetyl Beta-D-Glucosaminidase) ELISA Kit 96T
E15861270 Porcine N-Acetyl Beta D Glucosaminidase(NAG) ELISA Kit
E90069Ra ELISA Kit for N-Acetyl Beta D Glucosaminidase (NAGase) 96T/Kit


 

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