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O-GlcNAcase NagJ (EC 3.2.1.169) (Beta-N-acetylglucosaminidase) (Beta-N-acetylhexosaminidase) (Beta-hexosaminidase) (GH84C) (Hexosaminidase B) (N-acetyl-beta-D-glucosaminidase)

 OGA_CLOP1               Reviewed;        1001 AA.
Q0TR53;
31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
05-SEP-2006, sequence version 1.
12-SEP-2018, entry version 96.
RecName: Full=O-GlcNAcase NagJ;
EC=3.2.1.169 {ECO:0000269|PubMed:16541109, ECO:0000269|PubMed:18721751, ECO:0000269|PubMed:22365600};
AltName: Full=Beta-N-acetylglucosaminidase;
AltName: Full=Beta-N-acetylhexosaminidase;
AltName: Full=Beta-hexosaminidase;
AltName: Full=GH84C {ECO:0000303|PubMed:19193644};
AltName: Full=Hexosaminidase B;
AltName: Full=N-acetyl-beta-D-glucosaminidase;
Flags: Precursor;
Name=nagJ; OrderedLocusNames=CPF_1442;
Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 /
NCIMB 6125 / NCTC 8237 / Type A).
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=195103;
[1] {ECO:0000312|EMBL:ABG84519.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S
107 / Type A;
PubMed=16825665; DOI=10.1101/gr.5238106;
Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R.,
DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C.,
Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J.,
Sullivan S.A., Khouri H., Dimitrov G.I., Watkins K.L., Mulligan S.,
Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H.,
Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I.,
Melville S.B., Paulsen I.T.;
"Skewed genomic variability in strains of the toxigenic bacterial
pathogen, Clostridium perfringens.";
Genome Res. 16:1031-1040(2006).
[2] {ECO:0000305}
X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS) OF 31-624 IN COMPLEX WITH THE
SUBSTRATE ANALOG PUGNAC, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF
ASP-297; ASP-298; TYR-335; ASN-390; ASN-396; ASP-401 AND TRP-490,
FUNCTION, CATALYTIC ACTIVITY, AND ACTIVE SITE.
STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S
107 / Type A;
PubMed=16541109; DOI=10.1038/sj.emboj.7601026;
Rao F.V., Dorfmueller H.C., Villa F., Allwood M., Eggleston I.M.,
van Aalten D.M.;
"Structural insights into the mechanism and inhibition of eukaryotic
O-GlcNAc hydrolysis.";
EMBO J. 25:1569-1578(2006).
[3]
X-RAY CRYSTALLOGRAPHY (1.49 ANGSTROMS) OF 625-767 IN COMPLEX WITH
GALACTOSE AND N-ACETYL-ALPHA-D-GLUCOSAMINE, AND FUNCTION.
STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S
107 / Type A;
PubMed=16990278; DOI=10.1074/jbc.M606126200;
Ficko-Blean E., Boraston A.B.;
"The interaction of a carbohydrate-binding module from a Clostridium
perfringens N-acetyl-beta-hexosaminidase with its carbohydrate
receptor.";
J. Biol. Chem. 281:37748-37757(2006).
[4]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 31-624 IN COMPLEX WITH THE
SUBSTRATE ANALOG STREPTOZOTOCIN, CATALYTIC ACTIVITY, AND ACTIVITY
REGULATION.
STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S
107 / Type A;
PubMed=18721751; DOI=10.1016/j.chembiol.2008.06.010;
Pathak S., Dorfmueller H.C., Borodkin V.S., van Aalten D.M.;
"Chemical dissection of the link between streptozotocin, O-GlcNAc, and
pancreatic cell death.";
Chem. Biol. 15:799-807(2008).
[5]
X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 765-1001.
STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S
107 / Type A;
PubMed=19193644; DOI=10.1074/jbc.M808954200;
Ficko-Blean E., Gregg K.J., Adams J.J., Hehemann J.H., Czjzek M.,
Smith S.P., Boraston A.B.;
"Portrait of an enzyme, a complete structural analysis of a
multimodular {beta}-N-acetylglucosaminidase from Clostridium
perfringens.";
J. Biol. Chem. 284:9876-9884(2009).
[6]
X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 31-618 OF MUTANT ASN-298 IN
COMPLEX WITH N-ACETYL-D-GLUCOSAMINE, CATALYTIC ACTIVITY, AND
MUTAGENESIS OF ASP-298.
STRAIN=ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 / S
107 / Type A;
PubMed=22365600; DOI=10.1016/j.chembiol.2012.01.011;
Schimpl M., Borodkin V.S., Gray L.J., van Aalten D.M.;
"Synergy of peptide and sugar in O-GlcNAcase substrate recognition.";
Chem. Biol. 19:173-178(2012).
-!- FUNCTION: Binds carbohydrates (PubMed:16990278). Capable of
hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Can
bind and deglycosylate O-glycosylated peptides from mammals.
{ECO:0000269|PubMed:16541109, ECO:0000269|PubMed:16990278,
ECO:0000269|PubMed:18721751}.
-!- 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:16541109, ECO:0000269|PubMed:18721751,
ECO:0000269|PubMed:22365600}.
-!- 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:16541109,
ECO:0000269|PubMed:18721751, ECO:0000269|PubMed:22365600}.
-!- ACTIVITY REGULATION: Inhibited by O-(2-acetamido-2-deoxy-D-
glucopyranosylidene)amino-N-phenyl-carbamate (PUGNAc) and
streptozotocin. {ECO:0000269|PubMed:16541109,
ECO:0000269|PubMed:18721751}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=2.9 uM for 4-methylumbelliferyl-N-acetyl-beta-D-glucosaminide
(4MU-NAG) {ECO:0000269|PubMed:16541109};
-!- MISCELLANEOUS: Metal-binding observed in X-ray crystal structures
is artifactual. {ECO:0000305}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 84 family.
{ECO:0000255}.
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EMBL; CP000246; ABG84519.1; -; Genomic_DNA.
RefSeq; WP_003456570.1; NC_008261.1.
PDB; 2CBI; X-ray; 2.25 A; A/B=31-624.
PDB; 2CBJ; X-ray; 2.35 A; A/B=31-624.
PDB; 2J1A; X-ray; 1.49 A; A=625-767.
PDB; 2J1E; X-ray; 2.40 A; A=625-767.
PDB; 2J62; X-ray; 2.26 A; A/B=31-624.
PDB; 2J7M; X-ray; 2.30 A; A=625-767.
PDB; 2JH2; X-ray; 2.50 A; A/B/C=768-909.
PDB; 2O4E; NMR; -; A=768-909.
PDB; 2OZN; X-ray; 1.60 A; A=768-909.
PDB; 2V5C; X-ray; 2.10 A; A/B=31-624.
PDB; 2V5D; X-ray; 3.30 A; A=31-767.
PDB; 2VUR; X-ray; 2.20 A; A/B=31-624.
PDB; 2W1N; X-ray; 1.80 A; A=765-1001.
PDB; 2WB5; X-ray; 2.31 A; A/B=31-624.
PDB; 2X0Y; X-ray; 2.25 A; A/B=31-624.
PDB; 2XPK; X-ray; 2.40 A; A/B=31-624.
PDB; 2YDQ; X-ray; 2.60 A; A=31-618.
PDB; 2YDR; X-ray; 2.75 A; A=31-618.
PDB; 2YDS; X-ray; 2.55 A; A=31-618.
PDB; 4ZXL; X-ray; 2.60 A; A=39-617.
PDB; 5OXD; X-ray; 2.60 A; A=31-618.
PDBsum; 2CBI; -.
PDBsum; 2CBJ; -.
PDBsum; 2J1A; -.
PDBsum; 2J1E; -.
PDBsum; 2J62; -.
PDBsum; 2J7M; -.
PDBsum; 2JH2; -.
PDBsum; 2O4E; -.
PDBsum; 2OZN; -.
PDBsum; 2V5C; -.
PDBsum; 2V5D; -.
PDBsum; 2VUR; -.
PDBsum; 2W1N; -.
PDBsum; 2WB5; -.
PDBsum; 2X0Y; -.
PDBsum; 2XPK; -.
PDBsum; 2YDQ; -.
PDBsum; 2YDR; -.
PDBsum; 2YDS; -.
PDBsum; 4ZXL; -.
PDBsum; 5OXD; -.
ProteinModelPortal; Q0TR53; -.
SMR; Q0TR53; -.
STRING; 195103.CPF_1442; -.
CAZy; CBM32; Carbohydrate-Binding Module Family 32.
CAZy; GH84; Glycoside Hydrolase Family 84.
PRIDE; Q0TR53; -.
DNASU; 4202790; -.
EnsemblBacteria; ABG84519; ABG84519; CPF_1442.
GeneID; 29571445; -.
KEGG; cpf:CPF_1442; -.
eggNOG; ENOG4105CPE; Bacteria.
eggNOG; ENOG410XPBQ; LUCA.
HOGENOM; HOG000052598; -.
KO; K01197; -.
OMA; ARMEEAC; -.
OrthoDB; POG091H0IJT; -.
BRENDA; 3.2.1.169; 1503.
EvolutionaryTrace; Q0TR53; -.
Proteomes; UP000001823; Chromosome.
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; IDA:UniProtKB.
GO; GO:0030246; F:carbohydrate binding; IDA:UniProtKB.
GO; GO:0005975; P:carbohydrate metabolic process; IDA:UniProtKB.
GO; GO:0006517; P:protein deglycosylation; IMP:UniProtKB.
CDD; cd00063; FN3; 1.
Gene3D; 2.60.120.260; -; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.30.379.10; -; 1.
InterPro; IPR011496; Beta-N-acetylglucosaminidase.
InterPro; IPR008965; CBM2/CBM3_carb-bd_dom_sf.
InterPro; IPR000421; FA58C.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR029018; Hex-like_dom2.
InterPro; IPR015882; HEX_bac_N.
InterPro; IPR013783; Ig-like_fold.
Pfam; PF00754; F5_F8_type_C; 1.
Pfam; PF00041; fn3; 1.
Pfam; PF02838; Glyco_hydro_20b; 1.
Pfam; PF07555; NAGidase; 1.
SMART; SM00060; FN3; 1.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF49384; SSF49384; 1.
SUPFAM; SSF49785; SSF49785; 1.
SUPFAM; SSF51445; SSF51445; 1.
SUPFAM; SSF55545; SSF55545; 1.
PROSITE; PS50853; FN3; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Glycosidase; Hydrolase;
Signal.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 1001 O-GlcNAcase NagJ.
/FTId=PRO_0000257985.
DOMAIN 916 1001 Fibronectin type-III.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
REGION 179 469 Catalytic domain. {ECO:0000255}.
REGION 394 396 Substrate binding.
{ECO:0000269|PubMed:16541109}.
COILED 515 543 {ECO:0000255}.
COILED 573 597 {ECO:0000255}.
ACT_SITE 298 298 Proton donor.
{ECO:0000269|PubMed:16541109}.
BINDING 187 187 Substrate; via carbonyl oxygen.
{ECO:0000269|PubMed:16541109}.
BINDING 218 218 Substrate. {ECO:0000269|PubMed:16541109}.
BINDING 297 297 Substrate. {ECO:0000269|PubMed:16541109}.
BINDING 335 335 Substrate. {ECO:0000269|PubMed:16541109}.
BINDING 401 401 Substrate. {ECO:0000269|PubMed:16541109}.
BINDING 429 429 Substrate. {ECO:0000269|PubMed:16541109}.
MUTAGEN 297 297 D->A: 99% decrease in activity for 4MU-
NAG. {ECO:0000269|PubMed:16541109}.
MUTAGEN 298 298 D->N: 99% decrease in activity for 4MU-
NAG. {ECO:0000269|PubMed:16541109,
ECO:0000269|PubMed:22365600}.
MUTAGEN 335 335 Y->F: Strongly decreases affinity for
4MU-NAG. 99% decrease in activity for
4MU-NAG. {ECO:0000269|PubMed:16541109}.
MUTAGEN 390 390 N->A: No change in activity for 4MU-NAG.
{ECO:0000269|PubMed:16541109}.
MUTAGEN 396 396 N->A: Strongly decreases affinity for
4MU-NAG. 99% decrease in activity for
4MU-NAG. {ECO:0000269|PubMed:16541109}.
MUTAGEN 401 401 D->A: Strongly decreases affinity for
4MU-NAG. 99% decrease in activity for
4MU-NAG. {ECO:0000269|PubMed:16541109}.
MUTAGEN 490 490 W->A: Strongly decreases affinity for
4MU-NAG. 97% decrease in activity for
4MU-NAG. {ECO:0000269|PubMed:16541109}.
STRAND 51 55 {ECO:0000244|PDB:2V5C}.
STRAND 64 70 {ECO:0000244|PDB:2V5C}.
TURN 71 73 {ECO:0000244|PDB:2V5C}.
HELIX 76 88 {ECO:0000244|PDB:2V5C}.
STRAND 95 97 {ECO:0000244|PDB:2VUR}.
STRAND 101 108 {ECO:0000244|PDB:2V5C}.
STRAND 109 111 {ECO:0000244|PDB:2WB5}.
HELIX 114 120 {ECO:0000244|PDB:2V5C}.
STRAND 133 138 {ECO:0000244|PDB:2V5C}.
STRAND 141 148 {ECO:0000244|PDB:2V5C}.
HELIX 149 162 {ECO:0000244|PDB:2V5C}.
STRAND 164 168 {ECO:0000244|PDB:2V5D}.
STRAND 171 175 {ECO:0000244|PDB:2V5C}.
STRAND 178 185 {ECO:0000244|PDB:2V5C}.
STRAND 189 191 {ECO:0000244|PDB:2J62}.
HELIX 195 207 {ECO:0000244|PDB:2V5C}.
STRAND 212 215 {ECO:0000244|PDB:2V5C}.
HELIX 221 223 {ECO:0000244|PDB:2V5C}.
TURN 224 228 {ECO:0000244|PDB:2V5C}.
HELIX 233 235 {ECO:0000244|PDB:2V5C}.
HELIX 236 248 {ECO:0000244|PDB:2V5C}.
STRAND 252 257 {ECO:0000244|PDB:2V5C}.
HELIX 259 261 {ECO:0000244|PDB:2V5C}.
HELIX 268 285 {ECO:0000244|PDB:2V5C}.
TURN 286 288 {ECO:0000244|PDB:2V5C}.
STRAND 291 295 {ECO:0000244|PDB:2V5C}.
HELIX 304 317 {ECO:0000244|PDB:2V5C}.
HELIX 319 322 {ECO:0000244|PDB:2V5C}.
STRAND 323 325 {ECO:0000244|PDB:2X0Y}.
STRAND 329 331 {ECO:0000244|PDB:2V5C}.
HELIX 337 340 {ECO:0000244|PDB:2V5C}.
STRAND 341 346 {ECO:0000244|PDB:2V5D}.
HELIX 348 356 {ECO:0000244|PDB:2V5C}.
STRAND 361 365 {ECO:0000244|PDB:2V5C}.
STRAND 367 371 {ECO:0000244|PDB:2V5C}.
HELIX 377 387 {ECO:0000244|PDB:2V5C}.
STRAND 391 395 {ECO:0000244|PDB:2V5C}.
HELIX 419 421 {ECO:0000244|PDB:2V5C}.
STRAND 423 428 {ECO:0000244|PDB:2V5C}.
HELIX 434 449 {ECO:0000244|PDB:2V5C}.
HELIX 451 453 {ECO:0000244|PDB:2V5C}.
HELIX 456 468 {ECO:0000244|PDB:2V5C}.
HELIX 469 471 {ECO:0000244|PDB:2V5C}.
HELIX 472 479 {ECO:0000244|PDB:2V5C}.
STRAND 488 490 {ECO:0000244|PDB:2V5C}.
STRAND 492 495 {ECO:0000244|PDB:2V5C}.
HELIX 499 512 {ECO:0000244|PDB:2V5C}.
TURN 513 515 {ECO:0000244|PDB:2V5C}.
HELIX 519 542 {ECO:0000244|PDB:2V5C}.
HELIX 545 576 {ECO:0000244|PDB:2V5C}.
HELIX 580 599 {ECO:0000244|PDB:2V5C}.
TURN 606 608 {ECO:0000244|PDB:2V5C}.
HELIX 609 618 {ECO:0000244|PDB:2V5C}.
HELIX 621 623 {ECO:0000244|PDB:2V5C}.
STRAND 628 634 {ECO:0000244|PDB:2J1A}.
STRAND 639 641 {ECO:0000244|PDB:2J1A}.
HELIX 645 648 {ECO:0000244|PDB:2J1A}.
STRAND 649 651 {ECO:0000244|PDB:2J1A}.
STRAND 662 664 {ECO:0000244|PDB:2J1A}.
STRAND 671 688 {ECO:0000244|PDB:2J1A}.
STRAND 697 719 {ECO:0000244|PDB:2J1A}.
STRAND 722 725 {ECO:0000244|PDB:2J1A}.
STRAND 727 747 {ECO:0000244|PDB:2J1A}.
STRAND 749 752 {ECO:0000244|PDB:2V5D}.
TURN 754 756 {ECO:0000244|PDB:2J1A}.
STRAND 759 766 {ECO:0000244|PDB:2J1A}.
STRAND 776 782 {ECO:0000244|PDB:2OZN}.
STRAND 785 788 {ECO:0000244|PDB:2OZN}.
STRAND 792 804 {ECO:0000244|PDB:2OZN}.
STRAND 808 815 {ECO:0000244|PDB:2OZN}.
TURN 818 820 {ECO:0000244|PDB:2OZN}.
STRAND 821 827 {ECO:0000244|PDB:2OZN}.
STRAND 832 840 {ECO:0000244|PDB:2OZN}.
STRAND 843 854 {ECO:0000244|PDB:2OZN}.
STRAND 858 869 {ECO:0000244|PDB:2OZN}.
STRAND 873 886 {ECO:0000244|PDB:2OZN}.
STRAND 888 890 {ECO:0000244|PDB:2O4E}.
STRAND 892 894 {ECO:0000244|PDB:2OZN}.
STRAND 898 905 {ECO:0000244|PDB:2OZN}.
STRAND 918 925 {ECO:0000244|PDB:2W1N}.
STRAND 930 935 {ECO:0000244|PDB:2W1N}.
STRAND 943 950 {ECO:0000244|PDB:2W1N}.
STRAND 953 959 {ECO:0000244|PDB:2W1N}.
STRAND 964 967 {ECO:0000244|PDB:2W1N}.
STRAND 975 984 {ECO:0000244|PDB:2W1N}.
STRAND 993 998 {ECO:0000244|PDB:2W1N}.
SEQUENCE 1001 AA; 111080 MW; 3B918C7DB544A2DC CRC64;
MKRKMLKRLL TSAFACMFIA NGLITTTVRA VGPKTGEENQ VLVPNLNPTP ENLEVVGDGF
KITSSINLVG EEEADENAVN ALREFLTANN IEINSENDPN STTLIIGEVD DDIPELDEAL
NGTTAENLKE EGYALVSNDG KIAIEGKDGD GTFYGVQTFK QLVKESNIPE VNITDYPTVS
ARGIVEGFYG TPWTHQDRLD QIKFYGENKL NTYIYAPKDD PYHREKWREP YPESEMQRMQ
ELINASAENK VDFVFGISPG IDIRFDGDAG EEDFNHLITK AESLYDMGVR SFAIYWDDIQ
DKSAAKHAQV LNRFNEEFVK AKGDVKPLIT VPTEYDTGAM VSNGQPRAYT RIFAETVDPS
IEVMWTGPGV VTNEIPLSDA QLISGIYNRN MAVWWNYPVT DYFKGKLALG PMHGLDKGLN
QYVDFFTVNP MEHAELSKIS IHTAADYSWN MDNYDYDKAW NRAIDMLYGD LAEDMKVFAN
HSTRMDNKTW AKSGREDAPE LRAKMDELWN KLSSKEDASA LIEELYGEFA RMEEACNNLK
ANLPEVALEE CSRQLDELIT LAQGDKASLD MIVAQLNEDT EAYESAKEIA QNKLNTALSS
FAVISEKVAQ SFIQEALSFD LTLINPRTVK ITASSEETSG ENAPASFASD GDMNTFWHSK
WSSPAHEGPH HLTLELDNVY EINKVKYAPR QDSKNGRITG YKVSVSLDGE NFTEVKTGTL
EDNAAIKFIE FDSVDAKYVR LDVTDSVSDQ ANGRGKFATA AEVNVHGKLK ENAEVTGSVS
LEALEEVQVG ENLEVGVGID ELVNAEAFAY DFTLNYDENA FEYVEAISDD GVFVNAKKIE
DGKVRVLVSS LTGEPLPAKE VLAKVVLRAE AKAEGSNLSV TNSSVGDGEG LVHEIAGTEK
TVNIIEGTSP EIVVNPVRDF KASEINKKNV TVTWTEPETT EGLEGYILYK DGKKVAEIGK
DETSYTFKKL NRHTIYNFKI AAKYSNGEVS SKESLTLRTA R


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U0195b CLIA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Bos taurus,Bovine,HEXA,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha 96T
E0195b ELISA kit Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Bos taurus,Bovine,HEXA,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha 96T
U0195r CLIA Beta-hexosaminidase subunit alpha,Beta-N-acetylhexosaminidase subunit alpha,Hexa,Hexosaminidase subunit A,N-acetyl-beta-glucosaminidase subunit alpha,Rat,Rattus norvegicus 96T
'H00003074-B01P Beta-hexosaminidase beta _ HEXB antibody Host Mouse 50
CSB-EL010316HU Human Beta-hexosaminidase subunit beta(HEXB) ELISA kit SpeciesHuman 96T
CSB-EL010316MO Mouse Beta-hexosaminidase subunit beta(HEXB) ELISA kit SpeciesMouse 96T
'AP32247PU-N Beta-hexosaminidase beta HEXB (C-term) IgG antibody Ab host: Rabbit 50 Вµg
'GTX101182 Beta-hexosaminidase beta HEXB antibody Host rabbit 0.1 ml
CSB-EL010316CA Cat Beta-hexosaminidase subunit beta(HEXB) ELISA kit SpeciesCat 96T
'GTX101182 Beta-hexosaminidase beta _ HEXB antibody Host rabbit 0.1 ml
'C10295-2 Beta-hexosaminidase beta HEXB antibody Host rabbit 0.1 mg
CSB-EL010316MO Mouse Beta-hexosaminidase subunit beta(HEXB) ELISA kit 96T
'C10295-1 Beta-hexosaminidase beta HEXB antibody Host rabbit 50
CSB-EL010316HU Human Beta-hexosaminidase subunit beta(HEXB) ELISA kit 96T
GTX101182 Beta-hexosaminidase beta _ HEXB Rabbit antibody Ab Aff - Purified 0.1 ml
M1037 Resorufin beta-D-N-acetylgalactosamine, beta-Hexosaminidase Substrate, 10mg


 

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