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Cytosolic beta-glucosidase (EC 3.2.1.21) (Cytosolic beta-glucosidase-like protein 1)

 GBA3_HUMAN              Reviewed;         469 AA.
Q9H227; Q32LY7; Q3MIH4; Q53GG8; Q6NSF4; Q8NHT8; Q9H3T4; Q9H4C6;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 2.
12-SEP-2018, entry version 146.
RecName: Full=Cytosolic beta-glucosidase;
EC=3.2.1.21;
AltName: Full=Cytosolic beta-glucosidase-like protein 1;
Name=GBA3; Synonyms=CBG, CBGL1;
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 TISSUE SPECIFICITY.
TISSUE=Fetal liver;
PubMed=11043382; DOI=10.1007/s001090000131;
Yahata K., Mori K., Arai H., Koide S., Ogawa Y., Mukoyama M.,
Sugawara A., Ozaki S., Tanaka I., Nabeshima Y., Nakao K.;
"Molecular cloning and expression of a novel klotho-related protein.";
J. Mol. Med. 78:389-394(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ACTIVITY REGULATION, AND
BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Liver;
PubMed=11389701; DOI=10.1042/0264-6021:3560907;
de Graaf M., van Veen I.C., van der Meulen-Muileman I.H.,
Gerritsen W.R., Pinedo H.M., Haisma H.J.;
"Cloning and characterization of human liver cytosolic beta-
glycosidase.";
Biochem. J. 356:907-910(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, BLOCKAGE OF
N-TERMINUS, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Liver;
PubMed=11784319; DOI=10.1046/j.0014-2956.2001.02641.x;
Berrin J.-G., McLauchlan W.R., Needs P., Williamson G., Puigserver A.,
Kroon P.A., Juge N.;
"Functional expression of human liver cytosolic beta-glucosidase in
Pichia pastoris. Insights into its role in the metabolism of dietary
glucosides.";
Eur. J. Biochem. 269:249-258(2002).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Liver;
Hays W.S., VanderJagt D.J., Glew R.H., Johnston D.E.;
Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Small intestine;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Kidney, and Liver;
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).
[7]
MUTAGENESIS OF VAL-168; PHE-225 AND TYR-308.
PubMed=12667141; DOI=10.1042/BJ20021876;
Berrin J.-G., Czjzek M., Kroon P.A., McLauchlan W.R., Puigserver A.,
Williamson G., Juge N.;
"Substrate (aglycone) specificity of human cytosolic beta-
glucosidase.";
Biochem. J. 373:41-48(2003).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12594539; DOI=10.1007/s00394-003-0397-3;
Nemeth K., Plumb G.W., Berrin J.-G., Juge N., Jacob R., Naim H.Y.,
Williamson G., Swallow D.M., Kroon P.A.;
"Deglycosylation by small intestinal epithelial cell beta-glucosidases
is a critical step in the absorption and metabolism of dietary
flavonoid glycosides in humans.";
Eur. J. Nutr. 42:29-42(2003).
[9]
X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH GLUCOSE AND
GALACTOSE, FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF GLU-165
AND GLU-373.
PubMed=17595169; DOI=10.1074/jbc.M700832200;
Hayashi Y., Okino N., Kakuta Y., Shikanai T., Tani M., Narimatsu H.,
Ito M.;
"Klotho-related protein is a novel cytosolic neutral beta-
glycosylceramidase.";
J. Biol. Chem. 282:30889-30900(2007).
[10]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
PubMed=17555766; DOI=10.1016/j.jmb.2007.05.034;
Tribolo S., Berrin J.G., Kroon P.A., Czjzek M., Juge N.;
"The crystal structure of human cytosolic beta-glucosidase unravels
the substrate aglycone specificity of a family 1 glycoside
hydrolase.";
J. Mol. Biol. 370:964-975(2007).
[11]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH GLUCOSE, AND
MUTAGENESIS OF GLU-165.
PubMed=18662675; DOI=10.1016/j.bbrc.2008.07.089;
Noguchi J., Hayashi Y., Baba Y., Okino N., Kimura M., Ito M.,
Kakuta Y.;
"Crystal structure of the covalent intermediate of human cytosolic
beta-glucosidase.";
Biochem. Biophys. Res. Commun. 374:549-552(2008).
[12]
VARIANT ASN-106.
PubMed=15322500; DOI=10.1016/j.lab.2004.03.013;
Beutler E., Beutler L., West C.;
"Mutations in the gene encoding cytosolic beta-glucosidase in Gaucher
disease.";
J. Lab. Clin. Med. 144:65-68(2004).
-!- FUNCTION: Glycosidase probably involved in the intestinal
absorption and metabolism of dietary flavonoid glycosides. Able to
hydrolyze a broad variety of glycosides including phytoestrogens,
flavonols, flavones, flavanones and cyanogens. Possesses beta-
glycosylceramidase activity and may be involved in a nonlysosomal
catabolic pathway of glycosylceramide.
{ECO:0000269|PubMed:11784319, ECO:0000269|PubMed:12594539,
ECO:0000269|PubMed:17595169}.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal, non-reducing beta-D-
glucosyl residues with release of beta-D-glucose.
-!- ACTIVITY REGULATION: Inhibited by 2,4-dinitrophenyl-2-fluoro-2-
deoxy-beta-D-glucopyranoside and sodium taurocholate.
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=40 uM for 4-methylumbelliferyl-beta-D-glucopyranoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
KM=50 uM for 4-methylumbelliferyl-beta-D-galactopyranoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
KM=370 uM for 4-nitrophenyl-beta-D-fucopyranoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
KM=570 uM for 4-nitrophenyl-alpha-D-arabinopyranoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
KM=1.76 mM for 4-nitrophenyl-beta-D-glucopyranoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
KM=3.14 mM for 4-nitrophenyl-beta-D-galactopyranoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
KM=1.58 mM for 4-nitrophenyl-beta-D-xylopyranoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
KM=52.6 mM for 4-nitrophenyl-beta-L-arabinopyranoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
KM=35 uM for genistein-7-glucoside {ECO:0000269|PubMed:11389701,
ECO:0000269|PubMed:11784319};
KM=118 uM for daidzein-7-glucoside {ECO:0000269|PubMed:11389701,
ECO:0000269|PubMed:11784319};
KM=31.8 uM for quercetin-4'-glucoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
KM=42.2 uM for quercetin-7-glucoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
KM=21.5 uM for apigenin-7-glucoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
KM=10 uM for luteolin-4'-glucoside {ECO:0000269|PubMed:11389701,
ECO:0000269|PubMed:11784319};
KM=50 uM for luteolin-7-glucoside {ECO:0000269|PubMed:11389701,
ECO:0000269|PubMed:11784319};
KM=432 uM for naringenin-7-glucoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
KM=253 uM for eriodictyol-7-glucoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
Vmax=10 umol/min/mg enzyme toward 4-nitrophenyl-beta-D-
glucopyranoside {ECO:0000269|PubMed:11389701,
ECO:0000269|PubMed:11784319};
Vmax=1.73 umol/min/mg enzyme toward genistein-7-glucoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
Vmax=2.75 umol/min/mg enzyme toward daidzein-7-glucoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
Vmax=1.19 umol/min/mg enzyme toward quercetin-4'-glucoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
Vmax=0.77 umol/min/mg enzyme toward quercetin-7-glucoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
Vmax=1.30 umol/min/mg enzyme toward apigenin-7-glucoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
Vmax=1.30 umol/min/mg enzyme toward luteolin-4'-glucoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
Vmax=2.85 umol/min/mg enzyme toward luteolin-7-glucoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
Vmax=0.93 umol/min/mg enzyme toward naringenin-7-glucoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
Vmax=0.90 umol/min/mg enzyme toward eriodictyol-7-glucoside
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
pH dependence:
Optimum pH is 6.5. Active from pH 5 to 7.5. Activity decreases
sharply with increasing acidity and is less than 4% at pH 4.
{ECO:0000269|PubMed:11389701, ECO:0000269|PubMed:11784319};
Temperature dependence:
Optimum temperature is 50 degrees Celsius. Stable more than 24
hours at 37 degrees Celsius. Loses activity at 58 degrees
Celsius. {ECO:0000269|PubMed:11389701,
ECO:0000269|PubMed:11784319};
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:12594539, ECO:0000269|PubMed:17595169}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H227-1; Sequence=Displayed;
Name=2;
IsoId=Q9H227-2; Sequence=VSP_015835;
-!- TISSUE SPECIFICITY: Present in small intestine (at protein level).
Expressed in liver, small intestine, colon, spleen and kidney.
Down-regulated in renal cell carcinomas and hepatocellular
carcinomas. {ECO:0000269|PubMed:11043382,
ECO:0000269|PubMed:12594539}.
-!- PTM: The N-terminus is blocked.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. Klotho
subfamily. {ECO:0000305}.
-!- CAUTION: GBA3 is both a gene and a pseudogene in the human
population, the reference genome corresponding currently to the
non-functional allele with a stop codon at position 456. The
reference genome allele is the major one in at least one human
population and should therefore not be changed to the functional
allele of the gene by the Genome Reference Consortium (GRC). The
sequence shown here with a Tyr at that position is the one of the
functional protein. {ECO:0000305}.
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EMBL; AB017913; BAB18741.1; -; mRNA.
EMBL; AJ278964; CAC08178.1; -; mRNA.
EMBL; AF317840; AAG39217.1; -; mRNA.
EMBL; AF323990; AAL37305.1; -; mRNA.
EMBL; AK222963; BAD96683.1; -; mRNA.
EMBL; BC029362; AAH29362.1; -; mRNA.
EMBL; BC070188; AAH70188.1; -; mRNA.
EMBL; BC101829; AAI01830.1; -; mRNA.
EMBL; BC109377; AAI09378.1; -; mRNA.
RefSeq; NP_001121904.1; NM_001128432.2. [Q9H227-2]
RefSeq; NP_001264154.1; NM_001277225.1.
RefSeq; NP_066024.1; NM_020973.4. [Q9H227-1]
UniGene; Hs.653107; -.
PDB; 2E9L; X-ray; 1.60 A; A=1-469.
PDB; 2E9M; X-ray; 1.80 A; A=1-469.
PDB; 2JFE; X-ray; 2.70 A; X=1-469.
PDB; 2ZOX; X-ray; 1.90 A; A=1-469.
PDB; 3VKK; X-ray; 2.00 A; A=1-469.
PDBsum; 2E9L; -.
PDBsum; 2E9M; -.
PDBsum; 2JFE; -.
PDBsum; 2ZOX; -.
PDBsum; 3VKK; -.
ProteinModelPortal; Q9H227; -.
SMR; Q9H227; -.
BioGrid; 121753; 7.
IntAct; Q9H227; 2.
STRING; 9606.ENSP00000471397; -.
BindingDB; Q9H227; -.
ChEMBL; CHEMBL3865; -.
CAZy; GH1; Glycoside Hydrolase Family 1.
iPTMnet; Q9H227; -.
PhosphoSitePlus; Q9H227; -.
DMDM; 77416427; -.
PaxDb; Q9H227; -.
PeptideAtlas; Q9H227; -.
PRIDE; Q9H227; -.
ProteomicsDB; 80477; -.
ProteomicsDB; 80478; -. [Q9H227-2]
DNASU; 57733; -.
GeneID; 57733; -.
KEGG; hsa:57733; -.
CTD; 57733; -.
DisGeNET; 57733; -.
GeneCards; GBA3; -.
HGNC; HGNC:19069; GBA3.
MIM; 606619; gene.
neXtProt; NX_Q9H227; -.
PharmGKB; PA134861643; -.
eggNOG; KOG0626; Eukaryota.
eggNOG; COG2723; LUCA.
HOVERGEN; HBG053101; -.
InParanoid; Q9H227; -.
KO; K05350; -.
PhylomeDB; Q9H227; -.
BioCyc; MetaCyc:HS11014-MONOMER; -.
BRENDA; 3.2.1.21; 2681.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
SABIO-RK; Q9H227; -.
EvolutionaryTrace; Q9H227; -.
GeneWiki; GBA3; -.
GenomeRNAi; 57733; -.
PRO; PR:Q9H227; -.
Proteomes; UP000005640; Unplaced.
CleanEx; HS_GBA3; -.
GO; GO:1902494; C:catalytic complex; IDA:CAFA.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0004565; F:beta-galactosidase activity; IDA:UniProtKB.
GO; GO:0008422; F:beta-glucosidase activity; IDA:UniProtKB.
GO; GO:0004348; F:glucosylceramidase activity; TAS:Reactome.
GO; GO:0017042; F:glycosylceramidase activity; IDA:UniProtKB.
GO; GO:0102483; F:scopolin beta-glucosidase activity; IEA:UniProtKB-EC.
GO; GO:0051692; P:cellular oligosaccharide catabolic process; IDA:CAFA.
GO; GO:0016139; P:glycoside catabolic process; IDA:UniProtKB.
GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
GO; GO:0046477; P:glycosylceramide catabolic process; IMP:UniProtKB.
GO; GO:1903017; P:positive regulation of exo-alpha-sialidase activity; IDA:CAFA.
GO; GO:0050821; P:protein stabilization; IDA:CAFA.
InterPro; IPR001360; Glyco_hydro_1.
InterPro; IPR033132; Glyco_hydro_1_N_CS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR10353; PTHR10353; 2.
Pfam; PF00232; Glyco_hydro_1; 1.
PRINTS; PR00131; GLHYDRLASE1.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Glycosidase; Hydrolase; Polymorphism; Reference proteome.
CHAIN 1 469 Cytosolic beta-glucosidase.
/FTId=PRO_0000063908.
REGION 424 425 Substrate binding. {ECO:0000250}.
ACT_SITE 165 165 Proton donor. {ECO:0000255}.
ACT_SITE 373 373 Nucleophile. {ECO:0000255}.
BINDING 17 17 Substrate.
BINDING 120 120 Substrate.
BINDING 164 164 Substrate.
BINDING 309 309 Substrate.
BINDING 417 417 Substrate.
VAR_SEQ 95 401 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_015835.
VARIANT 106 106 D -> N (rare polymorphism).
{ECO:0000269|PubMed:15322500}.
/FTId=VAR_023587.
VARIANT 172 172 M -> I (in dbSNP:rs36090352).
/FTId=VAR_049298.
VARIANT 213 213 R -> P (in dbSNP:rs17612341).
/FTId=VAR_023588.
VARIANT 354 354 C -> R (in dbSNP:rs16873108).
/FTId=VAR_023589.
MUTAGEN 165 165 E->D: Reduces catalytic activity 2-fold.
{ECO:0000269|PubMed:17595169,
ECO:0000269|PubMed:18662675}.
MUTAGEN 165 165 E->Q: Loss of catalytic activity.
{ECO:0000269|PubMed:17595169,
ECO:0000269|PubMed:18662675}.
MUTAGEN 168 168 V->Y: No change in temperature or pH
dependence. Decrease in specific
activity. {ECO:0000269|PubMed:12667141}.
MUTAGEN 225 225 F->S: Decrease in specific activity.
{ECO:0000269|PubMed:12667141}.
MUTAGEN 308 308 Y->F,A: Decrease in specific activity.
{ECO:0000269|PubMed:12667141}.
MUTAGEN 373 373 E->D: Reduces catalytic activity 2-fold.
{ECO:0000269|PubMed:17595169}.
MUTAGEN 373 373 E->Q: Loss of catalytic activity.
{ECO:0000269|PubMed:17595169}.
CONFLICT 29 29 P -> L (in Ref. 6; AAH70188).
{ECO:0000305}.
CONFLICT 134 134 L -> W (in Ref. 3; AAG39217).
{ECO:0000305}.
CONFLICT 309 309 Y -> C (in Ref. 5; BAD96683).
{ECO:0000305}.
CONFLICT 321 321 K -> R (in Ref. 5; BAD96683).
{ECO:0000305}.
CONFLICT 326 326 I -> T (in Ref. 2; CAC08178).
{ECO:0000305}.
STRAND 8 12 {ECO:0000244|PDB:2E9L}.
HELIX 15 18 {ECO:0000244|PDB:2E9L}.
HELIX 24 26 {ECO:0000244|PDB:2E9L}.
HELIX 31 38 {ECO:0000244|PDB:2E9L}.
STRAND 40 43 {ECO:0000244|PDB:2E9L}.
HELIX 44 46 {ECO:0000244|PDB:2E9L}.
STRAND 49 51 {ECO:0000244|PDB:2E9L}.
TURN 55 57 {ECO:0000244|PDB:2E9L}.
HELIX 59 69 {ECO:0000244|PDB:2E9L}.
STRAND 72 77 {ECO:0000244|PDB:2E9L}.
HELIX 80 83 {ECO:0000244|PDB:2E9L}.
HELIX 94 109 {ECO:0000244|PDB:2E9L}.
STRAND 113 121 {ECO:0000244|PDB:2E9L}.
HELIX 125 129 {ECO:0000244|PDB:2E9L}.
HELIX 132 134 {ECO:0000244|PDB:2E9L}.
HELIX 138 153 {ECO:0000244|PDB:2E9L}.
TURN 154 156 {ECO:0000244|PDB:2E9L}.
STRAND 159 164 {ECO:0000244|PDB:2E9L}.
HELIX 166 174 {ECO:0000244|PDB:2E9L}.
TURN 186 188 {ECO:0000244|PDB:2E9L}.
HELIX 189 211 {ECO:0000244|PDB:2E9L}.
HELIX 213 216 {ECO:0000244|PDB:2E9L}.
STRAND 219 221 {ECO:0000244|PDB:2E9L}.
STRAND 223 233 {ECO:0000244|PDB:2E9L}.
HELIX 237 250 {ECO:0000244|PDB:2E9L}.
HELIX 252 259 {ECO:0000244|PDB:2E9L}.
HELIX 266 278 {ECO:0000244|PDB:2E9L}.
HELIX 291 297 {ECO:0000244|PDB:2E9L}.
STRAND 302 316 {ECO:0000244|PDB:2E9L}.
HELIX 326 330 {ECO:0000244|PDB:2E9L}.
STRAND 332 335 {ECO:0000244|PDB:2E9L}.
HELIX 351 363 {ECO:0000244|PDB:2E9L}.
STRAND 369 374 {ECO:0000244|PDB:2E9L}.
STRAND 378 381 {ECO:0000244|PDB:2E9L}.
HELIX 387 405 {ECO:0000244|PDB:2E9L}.
STRAND 411 417 {ECO:0000244|PDB:2E9L}.
HELIX 425 430 {ECO:0000244|PDB:2E9L}.
STRAND 435 438 {ECO:0000244|PDB:2E9L}.
STRAND 442 444 {ECO:0000244|PDB:2JFE}.
STRAND 447 449 {ECO:0000244|PDB:2E9L}.
HELIX 451 462 {ECO:0000244|PDB:2E9L}.
SEQUENCE 469 AA; 53696 MW; 9036455485CE2E2F CRC64;
MAFPAGFGWA AATAAYQVEG GWDADGKGPC VWDTFTHQGG ERVFKNQTGD VACGSYTLWE
EDLKCIKQLG LTHYRFSLSW SRLLPDGTTG FINQKGIDYY NKIIDDLLKN GVTPIVTLYH
FDLPQTLEDQ GGWLSEAIIE SFDKYAQFCF STFGDRVKQW ITINEANVLS VMSYDLGMFP
PGIPHFGTGG YQAAHNLIKA HARSWHSYDS LFRKKQKGMV SLSLFAVWLE PADPNSVSDQ
EAAKRAITFH LDLFAKPIFI DGDYPEVVKS QIASMSQKQG YPSSRLPEFT EEEKKMIKGT
ADFFAVQYYT TRLIKYQENK KGELGILQDA EIEFFPDPSW KNVDWIYVVP WGVCKLLKYI
KDTYNNPVIY ITENGFPQSD PAPLDDTQRW EYFRQTFQEL FKAIQLDKVN LQVYCAWSLL
DNFEWNQGYS SRFGLFHVDF EDPARPRVPY TSAKEYAKII RNNGLEAHL


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CSB-EL009291GU Guinea pig glucosidase, beta, acid 3 (cytosolic) (GBA3) ELISA kit, Species Guinea pig, Sample Type serum, plasma 96T
AS09 449 Antibody: GLUC | beta-glucosidase, Immunogen: native beta- glucosidase purified from almonds, Host: rabbit, polyclonal, Confirmed reactivity: Prunus dulcis 10 mg
AS09 450 Antibody: GLUC | beta-glucosidase, Biotin conjugated, Immunogen: native beta- glucosidase purified from almonds, Host: rabbit, polyclonal, Confirmed reactivity: Prunus dulcis 1 ml
CSB-PA009291GA01HU Rabbit anti-human glucosidase, beta, acid 3 (cytosolic) polyclonal Antibody Primary antibody Host:Rabbit IgG 50ul
CSB-PA009291GA01HU Rabbit anti-human glucosidase, beta, acid 3 (cytosolic) polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul
AS09 451 Antibody: GLUC | beta-glucosidase, Affinity purified, Immunogen: native beta- glucosidase purified from almonds, Host: rabbit, polyclonal, Confirmed reactivity: Prunus dulcis 1 mg
EIAAB25109 Gcs1,Glucosidase 1,Glycoprotein-processing glucosidase I,Mannosyl-oligosaccharide glucosidase,Mogs,Mouse,Mus musculus
M0569 Resorufin beta-D-glucopyranoside, beta-Glucosidase Substrate, 10mg
M0881 Fluorescein di-beta-D-glucopyranoside (FDGlu), beta-Glucosidase Substrate, 5mg
M0065 Fluorescein mono-beta-D-glucopyranoside, Highly fluorescent beta-glucosidase probe, 10mg


 

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