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Beta-galactosidase (EC 3.2.1.23) (Acid beta-galactosidase) (Lactase) (Elastin receptor 1)

 BGAL_HUMAN              Reviewed;         677 AA.
P16278; B2R7H8; B7Z6B0; P16279;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 2.
25-APR-2018, entry version 203.
RecName: Full=Beta-galactosidase;
EC=3.2.1.23;
AltName: Full=Acid beta-galactosidase;
Short=Lactase;
AltName: Full=Elastin receptor 1;
Flags: Precursor;
Name=GLB1; Synonyms=ELNR1;
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=Placenta;
PubMed=3143362; DOI=10.1016/S0006-291X(88)80038-X;
Oshima A., Tsuji A., Nagao Y., Sakuraba H., Suzuki Y.;
"Cloning, sequencing, and expression of cDNA for human beta-
galactosidase.";
Biochem. Biophys. Res. Commun. 157:238-244(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PARTIAL PROTEIN
SEQUENCE, AND VARIANT LEU-10.
TISSUE=Testis;
PubMed=2511208;
Morreau H., Galjart N.J., Gillemans N., Willemsen R.,
van der Horst G.T.J., D'Azzo A.;
"Alternative splicing of beta-galactosidase mRNA generates the classic
lysosomal enzyme and a beta-galactosidase-related protein.";
J. Biol. Chem. 264:20655-20663(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-10.
PubMed=2111707; DOI=10.1089/dna.1990.9.119;
Yamamoto Y., Hake C.A., Martin B.M., Kretz K.A., Ahern-Rindell A.J.,
Naylor S.L., Mudd M., O'Brien J.S.;
"Isolation, characterization, and mapping of a human acid beta-
galactosidase cDNA.";
DNA Cell Biol. 9:119-127(1990).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
LEU-10.
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LEU-10.
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT CYS-521.
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LEU-10.
TISSUE=Colon;
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).
[8]
DOMAIN ELASTIN/LAMININ BINDING.
PubMed=8383699; DOI=10.1172/JCI116280;
Hinek A., Rabinovitch M., Keeley F., Okamura-Oho Y., Callahan J.;
"The 67-kD elastin/laminin-binding protein is related to an
enzymatically inactive, alternatively spliced form of beta-
galactosidase.";
J. Clin. Invest. 91:1198-1205(1993).
[9]
FUNCTION (ISOFORM 2).
PubMed=8922281;
Hinek A.;
"Biological roles of the non-integrin elastin/laminin receptor.";
Biol. Chem. 377:471-480(1996).
[10]
IDENTITY OF BETA-GALACTOSIDASE-RELATED PROTEIN WITH EBP.
PubMed=9497360; DOI=10.1074/jbc.273.11.6319;
Privitera S., Prody C.A., Callahan J.W., Hinek A.;
"The 67-kDa enzymatically inactive alternatively spliced variant of
beta-galactosidase is identical to the elastin/laminin-binding
protein.";
J. Biol. Chem. 273:6319-6326(1998).
[11]
REVIEW.
PubMed=10571006; DOI=10.1016/S0925-4439(99)00075-7;
Callahan J.W.;
"Molecular basis of GM1 gangliosidosis and Morquio disease, type B.
Structure-function studies of lysosomal beta-galactosidase and the
non-lysosomal beta-galactosidase-like protein.";
Biochim. Biophys. Acta 1455:85-103(1999).
[12]
ELASTIC-FIBER ASSEMBLY STUDIES.
PubMed=10841810; DOI=10.1086/302968;
Hinek A., Zhang S., Smith A.C., Callahan J.W.;
"Impaired elastic-fiber assembly by fibroblasts from patients with
either Morquio B disease or infantile GM1-gangliosidosis is linked to
deficiency in the 67-kD spliced variant of beta-galactosidase.";
Am. J. Hum. Genet. 67:23-36(2000).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-464.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-464 AND ASN-555.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[15]
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).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
VARIANTS MPS4B LEU-273; HIS-482 AND CYS-509, AND VARIANT GM1G1
CYS-494.
PubMed=1928092;
Oshima A., Yoshida K., Shimmoto M., Fukuhara Y., Sakuraba H.,
Suzuki Y.;
"Human beta-galactosidase gene mutations in morquio B disease.";
Am. J. Hum. Genet. 49:1091-1093(1991).
[19]
VARIANT GM1G1 CYS-49, VARIANT GM1G3 THR-51, AND VARIANT GM1G2 CYS-201.
PubMed=1909089;
Nishimoto J., Nanba E., Inui K., Okada S., Suzuki K.;
"GM1-gangliosidosis (genetic beta-galactosidase deficiency):
identification of four mutations in different clinical phenotypes
among Japanese patients.";
Am. J. Hum. Genet. 49:566-574(1991).
[20]
VARIANTS GM1G3 THR-51 AND GLN-457, VARIANTS GM1G1 ARG-123 AND CYS-316,
AND VARIANT GM1G2 CYS-201.
PubMed=1907800;
Yoshida K., Oshima A., Shimmoto M., Fukuhara Y., Sakuraba H.,
Yanagisawa N., Suzuki Y.;
"Human beta-galactosidase gene mutations in GM1-gangliosidosis: a
common mutation among Japanese adult/chronic cases.";
Am. J. Hum. Genet. 49:435-442(1991).
[21]
VARIANT GM1G1 HIS-482.
PubMed=1487238; DOI=10.1007/BF00220071;
Mosna G., Fattore S., Tubiello G., Brocca S., Trubia M., Gianazza E.,
Gatti R., Danesino C., Minelli A., Piantanida M.;
"A homozygous missense arginine to histidine substitution at position
482 of the beta-galactosidase in an Italian infantile GM1-
gangliosidosis patient.";
Hum. Genet. 90:247-250(1992).
[22]
VARIANTS GM1G1 CYS-208 AND ARG-578, AND VARIANTS GM1G2 HIS-590 AND
GLY-632.
PubMed=8213816;
Boustany R.-M.N., Qian W.-H., Suzuki K.;
"Mutations in acid beta-galactosidase cause GM1-gangliosidosis in
American patients.";
Am. J. Hum. Genet. 53:881-888(1993).
[23]
VARIANT GM1G3 MET-82.
PubMed=8198123;
Chakraborty S., Rafi M.A., Wenger D.A.;
"Mutations in the lysosomal beta-galactosidase gene that cause the
adult form of GM1 gangliosidosis.";
Am. J. Hum. Genet. 54:1004-1013(1994).
[24]
VARIANTS GM1G1 SER-148 AND ALA-216, VARIANT GM1G3 TYR-214, AND VARIANT
GLY-532.
Hilson W.L., Okamura-Oho Y., Zhang S., Clarke J.T.R., Mahuran D.,
Callahan J.W.;
"Novel missense mutations in beta-galactosidase that result in GM1-
gangliosidosis.";
Am. J. Hum. Genet. 55:A223-A223(1994).
[25]
VARIANTS MPS4B HIS-83 AND CYS-482.
PubMed=7586649;
Ishii N., Oohira T., Oshima A., Sakuraba H., Endo F., Matsuda I.,
Sukegawa K., Orii T., Suzuki Y.;
"Clinical and molecular analysis of a Japanese boy with Morquio B
disease.";
Clin. Genet. 48:103-108(1995).
[26]
VARIANT GM1G3 SER-263.
Suzuki Y., Sakuraba H., Oshima A.;
"Beta-galactosidase deficiency (beta-galactosidosis): GM1
gangliosidosis and Morquio B disease.";
(In) Scriver C.R., Beaudet A.L., Sly W.S., Valle D. (eds.);
The metabolic and molecular bases of inherited disease, pp.2787-2823,
McGraw-Hill Publishing Co., New York (1995).
[27]
VARIANTS GM1G1 HIS-59; ASN-591 AND CYS-591.
Morrone A., Bardelli T., Donati M.A., Giorgi M., Di Rocco R.,
Gatti R., Taddeucci G., Ricci R., D'Azzo A., Zammarchi E.;
"Identification of new mutations in six Italian patients affected by a
variant form of infantile GM1-gangliosidosis with severe
cardiomyopathy.";
Am. J. Hum. Genet. 61:A258-A258(1997).
[28]
VARIANTS SLOWLY PROGRESSIVE GM1-GANGLIOSIDOSIS HIS-201; SER-266 AND
CYS-509.
PubMed=9203065; DOI=10.1177/088307389701200404;
Kaye E.M., Shalish C., Livermore J., Taylor H.A., Stevenson R.E.,
Breakefield X.O.;
"Beta-Galactosidase gene mutations in patients with slowly progressive
GM1 gangliosidosis.";
J. Child Neurol. 12:242-247(1997).
[29]
VARIANTS MPS4B GLU-438; LYS-484 AND ALA-500.
PubMed=12393180; DOI=10.1016/S0925-4439(02)00172-2;
Bagshaw R.D., Zhang S., Hinek A., Skomorowski M.-A., Whelan D.,
Clarke J.T.R., Callahan J.W.;
"Novel mutations (Asn 484 Lys, Thr 500 Ala, Gly 438 Glu) in Morquio B
disease.";
Biochim. Biophys. Acta 1588:247-253(2002).
[30]
VARIANTS GM1G1 HIS-59; SER-121; CYS-208; MET-240 AND ASN-491, AND
VARIANTS LEU-10; CYS-521 AND GLY-532.
PubMed=10338095;
DOI=10.1002/(SICI)1098-1004(1999)13:5<401::AID-HUMU9>3.0.CO;2-N;
Silva C.M.D., Severini M.H., Sopelsa A., Coelho J.C., Zaha A.,
d'Azzo A., Giugliani R.;
"Six novel beta-galactosidase gene mutations in Brazilian patients
with GM1-gangliosidosis.";
Hum. Mutat. 13:401-409(1999).
[31]
VARIANTS GM1G1 SER-148 AND ASN-332, VARIANT GLY-532, AND
CHARACTERIZATION OF VARIANT GLY-532.
PubMed=10839995; DOI=10.1042/bj3480621;
Zhang S., Bagshaw R., Hilson W., Oho Y., Hinek A., Clarke J.T.R.,
Hinek A., Callahan J.W.;
"Characterization of beta-galactosidase mutations Asp332-->Asn and
Arg148-->Ser, and a polymorphism, Ser532-->Gly, in a case of GM1
gangliosidosis.";
Biochem. J. 348:621-632(2000).
[32]
VARIANTS GM1G1 HIS-59; HIS-482; ASN-591 AND CYS-591, AND VARIANTS
GM1G2 HIS-201 AND ASP-579.
PubMed=10737981;
DOI=10.1002/(SICI)1098-1004(200004)15:4<354::AID-HUMU8>3.0.CO;2-L;
Morrone A., Bardelli T., Donati M.A., Giorgi M., Di Rocco M.,
Gatti R., Parini R., Ricci R., Taddeucci G., D'Azzo A., Zammarchi E.;
"Beta-galactosidase gene mutations affecting the lysosomal enzyme and
the elastin-binding protein in GM1-gangliosidosis patients with
cardiac involvement.";
Hum. Mutat. 15:354-366(2000).
[33]
VARIANTS MPS4B LEU-273; PRO-408 AND ALA-500, VARIANTS GM1G3 MET-82;
ASP-270 AND TYR-281, AND VARIANT LEU-10.
PubMed=11511921; DOI=10.1007/s004390100570;
Paschke E., Milos I., Kreimer-Erlacher H., Hoefler G., Beck M.,
Hoeltzenbein M., Kleijer W., Levade T., Michelakakis H., Radeva B.;
"Mutation analyses in 17 patients with deficiency in acid beta-
galactosidase: three novel point mutations and high correlation of
mutation W273L with Morquio disease type B.";
Hum. Genet. 109:159-166(2001).
[34]
VARIANTS GM1G2 TRP-68 AND CYS-201, CHARACTERIZATION OF VARIANTS GM1G2
TRP-68 AND CYS-201, VARIANT PHE-436, AND MODULATING ACTION OF VARIANT
PHE-436.
PubMed=12644936; DOI=10.1007/s00439-003-0930-8;
Caciotti A., Bardelli T., Cunningham J., D'Azzo A., Zammarchi E.,
Morrone A.;
"Modulating action of the new polymorphism L436F detected in the GLB1
gene of a type-II GM1 gangliosidosis patient.";
Hum. Genet. 113:44-50(2003).
[35]
VARIANT GM1G1 TYR-151, AND CHARACTERIZATION OF VARIANT GM1G1 TYR-151.
PubMed=15365997; DOI=10.1002/humu.9279;
Georgiou T., Drousiotou A., Campos Y., Caciotti A., Sztriha L.,
Gururaj A., Ozand P., Zammarchi E., Morrone A., D'Azzo A.;
"Four novel mutations in patients from the Middle East with the
infantile form of GM1-gangliosidosis.";
Hum. Mutat. 24:352-352(2004).
[36]
ERRATUM.
Georgiou T., Drousiotou A., Campos Y., Caciotti A., Sztriha L.,
Gururaj A., Ozand P., Zammarchi E., Morrone A., D'Azzo A.;
Hum. Mutat. 24:536-537(2004).
[37]
VARIANTS GM1G1 HIS-59; CYS-59; CYS-208; MET-239; TYR-281; HIS-482;
ASP-579; ASN-591 AND CYS-591, VARIANT GM1G2 HIS-201, VARIANT CYS-521,
CHARACTERIZATION OF VARIANTS GM1G1 HIS-59; CYS-59; CYS-208; MET-239;
TYR-281; HIS-482; ASP-579; ASN-591 AND CYS-591, CHARACTERIZATION OF
VARIANT GM1G2 HIS-201, AND CHARACTERIZATION OF VARIANT CYS-521.
PubMed=15714521; DOI=10.1002/humu.20147;
Caciotti A., Donati M.A., Boneh A., d'Azzo A., Federico A., Parini R.,
Antuzzi D., Bardelli T., Nosi D., Kimonis V., Zammarchi E.,
Morrone A.;
"Role of beta-galactosidase and elastin binding protein in lysosomal
and nonlysosomal complexes of patients with GM1-gangliosidosis.";
Hum. Mutat. 25:285-292(2005).
[38]
VARIANTS GM1G1 LEU-10 AND TYR-151.
PubMed=15791924;
Gururaj A., Sztriha L., Hertecant J., Johansen J.G., Georgiou T.,
Campos Y., Drousiotou A., d'Azzo A.;
"Magnetic resonance imaging findings and novel mutations in GM1
gangliosidosis.";
J. Child Neurol. 20:57-60(2005).
[39]
VARIANTS GM1G3 HIS-49; GLU-73; CYS-148 AND GLU-438.
PubMed=15986423; DOI=10.1002/mds.20593;
Roze E., Paschke E., Lopez N., Eck T., Yoshida K., Maurel-Ollivier A.,
Doummar D., Caillaud C., Galanaud D., Billette de Villemeur T.,
Vidailhet M., Roubergue A.;
"Dystonia and parkinsonism in GM1 type 3 gangliosidosis.";
Mov. Disord. 20:1366-1369(2005).
[40]
VARIANTS GM1G1 CYS-59; HIS-59; SER-136; VAL-151; PRO-173; CYS-199;
ASP-272; ASN-346; CYS-347; PRO-420; ARG-422; ASN-441 AND CYS-590,
VARIANT GM1G2 SER-264, VARIANTS GM1G3 HIS-201 AND LYS-420, VARIANTS
MPS4B CYS-83; CYS-444; SER-494 AND ALA-500, AND VARIANTS PHE-436;
CYS-521 AND GLY-532.
PubMed=16941474; DOI=10.1002/humu.9451;
Santamaria R., Chabas A., Coll M.J., Miranda C.S., Vilageliu L.,
Grinberg D.;
"Twenty-one novel mutations in the GLB1 gene identified in a large
group of GM1-gangliosidosis and Morquio B patients: possible common
origin for the prevalent p.R59H mutation among Gypsies.";
Hum. Mutat. 27:1060-1060(2006).
[41]
VARIANTS MPS4B LEU-273; HIS-482 AND CYS-509, AND VARIANTS GM1G1
CYS-201; HIS-201 AND HIS-318.
PubMed=16538002; DOI=10.2152/jmi.53.103;
Tatano Y., Takeuchi N., Kuwahara J., Sakuraba H., Takahashi T.,
Takada G., Itoh K.;
"Elastogenesis in cultured dermal fibroblasts from patients with
lysosomal beta-galactosidase, protective protein/cathepsin A and
neuraminidase-1 deficiencies.";
J. Med. Invest. 53:103-112(2006).
[42]
VARIANTS GM1G1 CYS-59; HIS-59; VAL-134; LEU-147 DEL; SER-162; CYS-208;
ASP-272; 377-VAL--LYS-381 DEL; TYR-491; LEU-549 AND CYS-590, VARIANT
GM1G2 HIS-201, VARIANT GM1G3 ARG-155, AND VARIANTS GM1-GANGLIOSIDOSIS
LEU-434 AND GLU-554.
PubMed=17309651; DOI=10.1111/j.1399-0004.2007.00767.x;
Santamaria R., Blanco M., Chabas A., Grinberg D., Vilageliu L.;
"Identification of 14 novel GLB1 mutations, including five deletions,
in 19 patients with GM1 gangliosidosis from South America.";
Clin. Genet. 71:273-279(2007).
[43]
VARIANT TRP-595, AND CHARACTERIZATION OF VARIANT TRP-595.
PubMed=17661814; DOI=10.1111/j.1399-0004.2007.00843.x;
Gort L., Santamaria R., Grinberg D., Vilageliu L., Chabas A.;
"Identification of a novel pseudodeficiency allele in the GLB1 gene in
a carrier of GM1 gangliosidosis.";
Clin. Genet. 72:109-111(2007).
[44]
CHARACTERIZATION OF VARIANTS GM1G1 HIS-59; SER-162; PRO-173; HIS-201;
PRO-420; ASN-441; CYS-521 AND CYS-590, CHARACTERIZATION OF VARIANTS
MPS4B CYS-83; CYS-444 AND SER-494, CHARACTERIZATION OF VARIANT GM1G3
LYS-420, AND CHARACTERIZATION OF VARIANT GLY-532.
PubMed=17664528; DOI=10.1194/jlr.M700308-JLR200;
Santamaria R., Chabas A., Callahan J.W., Grinberg D., Vilageliu L.;
"Expression and characterization of 14 GLB1 mutant alleles found in
GM1-gangliosidosis and Morquio B patients.";
J. Lipid Res. 48:2275-2282(2007).
[45]
VARIANTS GM1G1 HIS-59; THR-132; ARG-184; ASP-190; CYS-201; HIS-201;
MET-239; HIS-255; ILE-329; GLU-332; ASN-346; GLN-442 AND SER-597,
VARIANTS GM1G2 GLN-68; ARG-155 AND HIS-333, VARIANTS GM1G3 MET-82;
ASP-270 AND GLU-438, VARIANTS MPS4B PHE-149; TYR-198; LEU-273;
ALA-397; PRO-408 AND ALA-500, CHARACTERIZATION OF VARIANTS GM1G1
THR-132; ARG-184; ASP-190; CYS-201; HIS-201; HIS-255; ILE-329; GLU-332
AND SER-597, CHARACTERIZATION OF VARIANTS GM1G2 GLN-68; ARG-155 AND
HIS-333, CHARACTERIZATION OF VARIANTS GM1G3 ASP-270 AND GLU-438, AND
CHARACTERIZATION OF VARIANTS MPS4B PHE-149; TYR-198; LEU-273; ALA-397;
PRO-408 AND ALA-500.
PubMed=19472408; DOI=10.1002/humu.21031;
Hofer D., Paul K., Fantur K., Beck M., Buerger F., Caillaud C.,
Fumic K., Ledvinova J., Lugowska A., Michelakakis H., Radeva B.,
Ramaswami U., Plecko B., Paschke E.;
"GM1 gangliosidosis and Morquio B disease: expression analysis of
missense mutations affecting the catalytic site of acid beta-
galactosidase.";
Hum. Mutat. 30:1214-1221(2009).
[46]
VARIANTS GM1G2 CYS-49; ARG-134; CYS-148; GLU-262; LEU-314; PRO-337;
VAL-414; ASN-493; LEU-597 AND ILE-600, CHARACTERIZATION OF VARIANTS
GM1G2 CYS-49; GLU-262; LEU-314; PRO-337; VAL-414; ASN-493; LEU-597 AND
ILE-600, VARIANTS GM1G1 TRP-68; ARG-123; PRO-236; CYS-331; ASN-332;
PRO-337; HIS-482 AND PRO-514, CHARACTERIZATION OF VARIANTS GM1G1
TRP-68; ARG-123; PRO-236; ASN-332; PRO-337; HIS-482 AND PRO-514,
VARIANT GM1G3 PHE-297, CHARACTERIZATION OF VARIANT GM1G3 PHE-297, AND
VARIANTS GLN-129 AND CYS-521.
PubMed=25936995; DOI=10.1016/j.gene.2015.04.078;
Bidchol A.M., Dalal A., Trivedi R., Shukla A., Nampoothiri S.,
Sankar V.H., Danda S., Gupta N., Kabra M., Hebbar S.A., Bhat R.Y.,
Matta D., Ekbote A.V., Puri R.D., Phadke S.R., Gowrishankar K.,
Aggarwal S., Ranganath P., Sharda S., Kamate M., Datar C.A., Bhat K.,
Kamath N., Shah H., Krishna S., Gopinath P.M., Verma I.C.,
Nagarajaram H.A., Satyamoorthy K., Girisha K.M.;
"Recurrent and novel GLB1 mutations in India.";
Gene 567:173-181(2015).
-!- FUNCTION: Cleaves beta-linked terminal galactosyl residues from
gangliosides, glycoproteins, and glycosaminoglycans.
-!- FUNCTION: Isoform 2 has no beta-galactosidase catalytic activity,
but plays functional roles in the formation of extracellular
elastic fibers (elastogenesis) and in the development of
connective tissue. Seems to be identical to the elastin-binding
protein (EBP), a major component of the non-integrin cell surface
receptor expressed on fibroblasts, smooth muscle cells,
chondroblasts, leukocytes, and certain cancer cell types. In
elastin producing cells, associates with tropoelastin
intracellularly and functions as a recycling molecular chaperone
which facilitates the secretions of tropoelastin and its assembly
into elastic fibers.
-!- CATALYTIC ACTIVITY: Hydrolysis of terminal non-reducing beta-D-
galactose residues in beta-D-galactosides.
-!- SUBCELLULAR LOCATION: Isoform 1: Lysosome.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm, perinuclear region.
Note=Localized to the perinuclear area of the cytoplasm but not to
lysosomes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P16278-1; Sequence=Displayed;
Name=2; Synonyms=Beta-galactosidase-related protein,
Beta-galactosidase-like protein, S-Gal, Elastin-binding protein,
EBP;
IsoId=P16278-2, P16279-1;
Sequence=VSP_031241;
Name=3;
IsoId=P16278-3; Sequence=VSP_039974;
Note=No experimental confirmation available.;
-!- DISEASE: GM1-gangliosidosis 1 (GM1G1) [MIM:230500]: An autosomal
recessive lysosomal storage disease marked by the accumulation of
GM1 gangliosides, glycoproteins and keratan sulfate primarily in
neurons of the central nervous system. GM1-gangliosidosis type 1
is characterized by onset within the first three months of life,
central nervous system degeneration, coarse facial features,
hepatosplenomegaly, skeletal dysmorphology reminiscent of Hurler
syndrome, and rapidly progressive psychomotor deterioration.
Urinary oligosaccharide levels are high. It leads to death usually
between the first and second year of life.
{ECO:0000269|PubMed:10338095, ECO:0000269|PubMed:10737981,
ECO:0000269|PubMed:10839995, ECO:0000269|PubMed:1487238,
ECO:0000269|PubMed:15365997, ECO:0000269|PubMed:15714521,
ECO:0000269|PubMed:15791924, ECO:0000269|PubMed:16538002,
ECO:0000269|PubMed:16941474, ECO:0000269|PubMed:17309651,
ECO:0000269|PubMed:17664528, ECO:0000269|PubMed:1907800,
ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:1928092,
ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:25936995,
ECO:0000269|PubMed:8213816, ECO:0000269|Ref.24,
ECO:0000269|Ref.27}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: GM1-gangliosidosis 2 (GM1G2) [MIM:230600]: A
gangliosidosis characterized by onset between ages 1 and 5. The
main symptom is locomotor ataxia, ultimately leading to a state of
decerebration with epileptic seizures. Patients do not display the
skeletal changes associated with the infantile form, but they
nonetheless excrete elevated amounts of beta-linked galactose-
terminal oligosaccharides. Inheritance is autosomal recessive.
{ECO:0000269|PubMed:10737981, ECO:0000269|PubMed:12644936,
ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:1907800,
ECO:0000269|PubMed:1909089, ECO:0000269|PubMed:19472408,
ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8213816}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: GM1-gangliosidosis 3 (GM1G3) [MIM:230650]: A
gangliosidosis with a variable phenotype. Patients show mild
skeletal abnormalities, dysarthria, gait disturbance, dystonia and
visual impairment. Visceromegaly is absent. Intellectual deficit
can initially be mild or absent but progresses over time.
Inheritance is autosomal recessive. {ECO:0000269|PubMed:11511921,
ECO:0000269|PubMed:15986423, ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17309651, ECO:0000269|PubMed:17664528,
ECO:0000269|PubMed:1907800, ECO:0000269|PubMed:1909089,
ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:25936995,
ECO:0000269|PubMed:8198123, ECO:0000269|Ref.24,
ECO:0000269|Ref.26}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Mucopolysaccharidosis 4B (MPS4B) [MIM:253010]: A form of
mucopolysaccharidosis type 4, an autosomal recessive lysosomal
storage disease characterized by intracellular accumulation of
keratan sulfate and chondroitin-6-sulfate. Key clinical features
include short stature, skeletal dysplasia, dental anomalies, and
corneal clouding. Intelligence is normal and there is no direct
central nervous system involvement, although the skeletal changes
may result in neurologic complications. There is variable
severity, but patients with the severe phenotype usually do not
survive past the second or third decade of life.
{ECO:0000269|PubMed:11511921, ECO:0000269|PubMed:12393180,
ECO:0000269|PubMed:16538002, ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17664528, ECO:0000269|PubMed:1928092,
ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:7586649}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 35 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Beta-galactosidase entry;
URL="https://en.wikipedia.org/wiki/Beta-galactosidase";
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; M22590; AAA51822.1; -; mRNA.
EMBL; M27507; AAA51819.1; -; mRNA.
EMBL; M27508; AAA35599.1; -; mRNA.
EMBL; M34423; AAA51823.1; -; mRNA.
EMBL; AK300021; BAH13196.1; -; mRNA.
EMBL; AK312988; BAG35825.1; -; mRNA.
EMBL; BT007147; AAP35811.1; -; mRNA.
EMBL; AC112211; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC007493; AAH07493.1; -; mRNA.
CCDS; CCDS43061.1; -. [P16278-1]
CCDS; CCDS43062.1; -. [P16278-3]
CCDS; CCDS46785.1; -. [P16278-2]
PIR; A32688; A32611.
PIR; B32688; B32688.
RefSeq; NP_000395.2; NM_000404.3. [P16278-1]
RefSeq; NP_001073279.1; NM_001079811.2. [P16278-3]
RefSeq; NP_001129074.1; NM_001135602.2. [P16278-2]
RefSeq; NP_001303969.1; NM_001317040.1.
UniGene; Hs.443031; -.
PDB; 3THC; X-ray; 1.80 A; A/B/C/D=24-677.
PDB; 3THD; X-ray; 1.79 A; A/B/C/D=24-677.
PDB; 3WEZ; X-ray; 2.11 A; A/B/C/D=24-677.
PDB; 3WF0; X-ray; 2.20 A; A/B/C/D=24-677.
PDB; 3WF1; X-ray; 2.00 A; A/B/C/D=24-677.
PDB; 3WF2; X-ray; 2.30 A; A/B/C/D=24-677.
PDB; 3WF3; X-ray; 2.15 A; A/B/C/D=24-677.
PDB; 3WF4; X-ray; 2.30 A; A/B/C/D=24-677.
PDBsum; 3THC; -.
PDBsum; 3THD; -.
PDBsum; 3WEZ; -.
PDBsum; 3WF0; -.
PDBsum; 3WF1; -.
PDBsum; 3WF2; -.
PDBsum; 3WF3; -.
PDBsum; 3WF4; -.
ProteinModelPortal; P16278; -.
SMR; P16278; -.
BioGrid; 108984; 49.
CORUM; P16278; -.
IntAct; P16278; 21.
MINT; P16278; -.
STRING; 9606.ENSP00000306920; -.
BindingDB; P16278; -.
ChEMBL; CHEMBL2522; -.
CAZy; GH35; Glycoside Hydrolase Family 35.
iPTMnet; P16278; -.
PhosphoSitePlus; P16278; -.
SwissPalm; P16278; -.
BioMuta; GLB1; -.
DMDM; 215273939; -.
EPD; P16278; -.
MaxQB; P16278; -.
PaxDb; P16278; -.
PeptideAtlas; P16278; -.
PRIDE; P16278; -.
DNASU; 2720; -.
Ensembl; ENST00000307363; ENSP00000306920; ENSG00000170266.
Ensembl; ENST00000399402; ENSP00000382333; ENSG00000170266.
Ensembl; ENST00000445488; ENSP00000393377; ENSG00000170266.
GeneID; 2720; -.
KEGG; hsa:2720; -.
UCSC; uc003cfh.2; human. [P16278-1]
CTD; 2720; -.
DisGeNET; 2720; -.
EuPathDB; HostDB:ENSG00000170266.15; -.
GeneCards; GLB1; -.
GeneReviews; GLB1; -.
HGNC; HGNC:4298; GLB1.
HPA; CAB008382; -.
HPA; HPA040610; -.
HPA; HPA069503; -.
MalaCards; GLB1; -.
MIM; 230500; phenotype.
MIM; 230600; phenotype.
MIM; 230650; phenotype.
MIM; 253010; phenotype.
MIM; 611458; gene.
neXtProt; NX_P16278; -.
Orphanet; 79255; GM1 gangliosidosis type 1.
Orphanet; 79256; GM1 gangliosidosis type 2.
Orphanet; 79257; GM1 gangliosidosis type 3.
Orphanet; 309310; Mucopolysaccharidosis type 4B.
PharmGKB; PA28709; -.
eggNOG; KOG0496; Eukaryota.
eggNOG; COG1874; LUCA.
HOGENOM; HOG000221607; -.
HOVERGEN; HBG004841; -.
InParanoid; P16278; -.
KO; K12309; -.
OrthoDB; EOG091G006X; -.
PhylomeDB; P16278; -.
TreeFam; TF314816; -.
Reactome; R-HSA-1660662; Glycosphingolipid metabolism.
Reactome; R-HSA-2022857; Keratan sulfate degradation.
Reactome; R-HSA-2024096; HS-GAG degradation.
Reactome; R-HSA-2206308; MPS IV - Morquio syndrome B.
Reactome; R-HSA-4085001; Sialic acid metabolism.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SABIO-RK; P16278; -.
ChiTaRS; GLB1; human.
GeneWiki; GLB1; -.
GenomeRNAi; 2720; -.
PRO; PR:P16278; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000170266; -.
CleanEx; HS_GLB1; -.
ExpressionAtlas; P16278; baseline and differential.
Genevisible; P16278; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:1904813; C:ficolin-1-rich granule lumen; TAS:Reactome.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005773; C:vacuole; IBA:GO_Central.
GO; GO:0004565; F:beta-galactosidase activity; IDA:BHF-UCL.
GO; GO:0004308; F:exo-alpha-sialidase activity; TAS:Reactome.
GO; GO:0016936; F:galactoside binding; IEA:Ensembl.
GO; GO:0044262; P:cellular carbohydrate metabolic process; IDA:BHF-UCL.
GO; GO:0019388; P:galactose catabolic process; IEA:Ensembl.
GO; GO:0006027; P:glycosaminoglycan catabolic process; TAS:Reactome.
GO; GO:0006687; P:glycosphingolipid metabolic process; TAS:Reactome.
GO; GO:0042340; P:keratan sulfate catabolic process; TAS:Reactome.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0051413; P:response to cortisone; IEA:Ensembl.
GO; GO:1904016; P:response to Thyroglobulin triiodothyronine; IEA:Ensembl.
Gene3D; 2.60.120.260; -; 3.
InterPro; IPR026283; B-gal_1-like.
InterPro; IPR025300; BetaGal_jelly_roll_dom.
InterPro; IPR008979; Galactose-bd-like_sf.
InterPro; IPR031330; Gly_Hdrlase_35_cat.
InterPro; IPR019801; Glyco_hydro_35_CS.
InterPro; IPR001944; Glycoside_Hdrlase_35.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR23421; PTHR23421; 1.
Pfam; PF13364; BetaGal_dom4_5; 1.
Pfam; PF01301; Glyco_hydro_35; 1.
PIRSF; PIRSF006336; B-gal; 1.
PRINTS; PR00742; GLHYDRLASE35.
SUPFAM; SSF49785; SSF49785; 2.
SUPFAM; SSF51445; SSF51445; 1.
PROSITE; PS01182; GLYCOSYL_HYDROL_F35; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; Cytoplasm;
Direct protein sequencing; Disease mutation; Gangliosidosis;
Glycoprotein; Glycosidase; Hydrolase; Lysosome; Mucopolysaccharidosis;
Polymorphism; Reference proteome; Signal; Zymogen.
SIGNAL 1 23
PROPEP 24 28
/FTId=PRO_0000012185.
CHAIN 29 677 Beta-galactosidase.
/FTId=PRO_0000012186.
ACT_SITE 188 188 Proton donor. {ECO:0000255}.
ACT_SITE 268 268 Nucleophile. {ECO:0000255}.
CARBOHYD 26 26 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 247 247 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 464 464 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:19159218}.
CARBOHYD 498 498 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 542 542 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 545 545 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 555 555 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
VAR_SEQ 1 30 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_039974.
VAR_SEQ 83 244 YVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPG
PYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGV
LLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQK
RFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGT
-> LPGSCGQVVGSPSAQDEASPLSEWRASYNSA (in
isoform 2). {ECO:0000303|PubMed:2511208}.
/FTId=VSP_031241.
VARIANT 10 10 P -> L (in GM1G1; dbSNP:rs7637099).
{ECO:0000269|PubMed:10338095,
ECO:0000269|PubMed:11511921,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:15791924,
ECO:0000269|PubMed:2111707,
ECO:0000269|PubMed:2511208,
ECO:0000269|Ref.5}.
/FTId=VAR_008671.
VARIANT 49 49 R -> C (in GM1G1 and GM1G2; decrease in
galactosidase activity).
{ECO:0000269|PubMed:1909089,
ECO:0000269|PubMed:25936995}.
/FTId=VAR_003329.
VARIANT 49 49 R -> H (in GM1G3).
{ECO:0000269|PubMed:15986423}.
/FTId=VAR_062340.
VARIANT 51 51 I -> T (in GM1G3).
{ECO:0000269|PubMed:1907800,
ECO:0000269|PubMed:1909089}.
/FTId=VAR_003330.
VARIANT 59 59 R -> C (in GM1G1; loss of galactosidase
activity; severe mutation).
{ECO:0000269|PubMed:15714521,
ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17309651}.
/FTId=VAR_026129.
VARIANT 59 59 R -> H (in GM1G1; with cardiac
involvement in some patients; loss of
galactosidase activity; severe mutation).
{ECO:0000269|PubMed:10338095,
ECO:0000269|PubMed:10737981,
ECO:0000269|PubMed:15714521,
ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17309651,
ECO:0000269|PubMed:17664528,
ECO:0000269|PubMed:19472408,
ECO:0000269|Ref.27}.
/FTId=VAR_008672.
VARIANT 68 68 R -> Q (in GM1G2; 7.4% of wild-type
galactosidase activity).
{ECO:0000269|PubMed:19472408}.
/FTId=VAR_062341.
VARIANT 68 68 R -> W (in GM1G2 and GM1G1; loss of
galactosidase activity).
{ECO:0000269|PubMed:12644936,
ECO:0000269|PubMed:25936995}.
/FTId=VAR_026130.
VARIANT 73 73 K -> E (in GM1G3).
{ECO:0000269|PubMed:15986423}.
/FTId=VAR_062342.
VARIANT 82 82 T -> M (in GM1G3; mild phenotype).
{ECO:0000269|PubMed:11511921,
ECO:0000269|PubMed:19472408,
ECO:0000269|PubMed:8198123}.
/FTId=VAR_008673.
VARIANT 83 83 Y -> C (in MPS4B; decrease in
galactosidase activity).
{ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17664528}.
/FTId=VAR_062343.
VARIANT 83 83 Y -> H (in MPS4B; 2-5% of wild-type
galactosidase activity).
{ECO:0000269|PubMed:7586649}.
/FTId=VAR_008674.
VARIANT 109 109 R -> W (in dbSNP:rs35289681).
/FTId=VAR_053875.
VARIANT 121 121 R -> S (in GM1G1).
{ECO:0000269|PubMed:10338095}.
/FTId=VAR_008675.
VARIANT 123 123 G -> R (in GM1G1; decrease in
galactosidase activity).
{ECO:0000269|PubMed:1907800,
ECO:0000269|PubMed:25936995}.
/FTId=VAR_003331.
VARIANT 129 129 E -> Q. {ECO:0000269|PubMed:25936995}.
/FTId=VAR_074054.
VARIANT 132 132 M -> T (in GM1G1; 4.3% of wild-type
galactosidase activity).
{ECO:0000269|PubMed:19472408}.
/FTId=VAR_062344.
VARIANT 134 134 G -> R (in GM1G2; unknown pathological
significance).
{ECO:0000269|PubMed:25936995}.
/FTId=VAR_074055.
VARIANT 134 134 G -> V (in GM1G1).
{ECO:0000269|PubMed:17309651}.
/FTId=VAR_037937.
VARIANT 136 136 P -> S (in GM1G1).
{ECO:0000269|PubMed:16941474}.
/FTId=VAR_062345.
VARIANT 147 147 Missing (in GM1G1).
{ECO:0000269|PubMed:17309651}.
/FTId=VAR_037938.
VARIANT 148 148 R -> C (in GM1G3 and GM1G2).
{ECO:0000269|PubMed:15986423,
ECO:0000269|PubMed:25936995}.
/FTId=VAR_062346.
VARIANT 148 148 R -> S (in GM1G1).
{ECO:0000269|PubMed:10839995,
ECO:0000269|Ref.24}.
/FTId=VAR_013541.
VARIANT 149 149 S -> F (in MPS4B; 2.0% of wild-type
galactosidase activity).
{ECO:0000269|PubMed:19472408}.
/FTId=VAR_062347.
VARIANT 151 151 D -> V (in GM1G1).
{ECO:0000269|PubMed:16941474}.
/FTId=VAR_062348.
VARIANT 151 151 D -> Y (in GM1G1; complete lack of
protein; loss of galactosidase activity).
{ECO:0000269|PubMed:15365997,
ECO:0000269|PubMed:15791924}.
/FTId=VAR_026131.
VARIANT 155 155 L -> R (in GM1G2 and GM1G3; 6.7% of wild-
type galactosidase activity).
{ECO:0000269|PubMed:17309651,
ECO:0000269|PubMed:19472408}.
/FTId=VAR_037939.
VARIANT 162 162 L -> S (in GM1G1; loss of galactosidase
activity). {ECO:0000269|PubMed:17309651,
ECO:0000269|PubMed:17664528}.
/FTId=VAR_037940.
VARIANT 173 173 L -> P (in GM1G1; loss of galactosidase
activity). {ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17664528}.
/FTId=VAR_062349.
VARIANT 184 184 Q -> R (in GM1G1; loss of galactosidase
activity). {ECO:0000269|PubMed:19472408}.
/FTId=VAR_062350.
VARIANT 190 190 G -> D (in GM1G1; 3.4% of wild-type
galactosidase activity).
{ECO:0000269|PubMed:19472408}.
/FTId=VAR_062351.
VARIANT 198 198 D -> Y (in MPS4B; 17.4% of wild-type
galactosidase activity).
{ECO:0000269|PubMed:19472408}.
/FTId=VAR_062352.
VARIANT 199 199 Y -> C (in GM1G1).
{ECO:0000269|PubMed:16941474}.
/FTId=VAR_062353.
VARIANT 201 201 R -> C (in GM1G1 and GM1G2; 8.4% of wild-
type galactosidase activity; activity
severely reduced in transfection with the
F-436 polymorphism).
{ECO:0000269|PubMed:12644936,
ECO:0000269|PubMed:16538002,
ECO:0000269|PubMed:1907800,
ECO:0000269|PubMed:1909089,
ECO:0000269|PubMed:19472408}.
/FTId=VAR_003332.
VARIANT 201 201 R -> H (in GM1G1 and GM1G2; also in a
patient with a slowly progressive GM1-
gangliosidosis form; 36.2% of wild-type
galactosidase activity).
{ECO:0000269|PubMed:10737981,
ECO:0000269|PubMed:15714521,
ECO:0000269|PubMed:16538002,
ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17309651,
ECO:0000269|PubMed:17664528,
ECO:0000269|PubMed:19472408,
ECO:0000269|PubMed:9203065}.
/FTId=VAR_013542.
VARIANT 208 208 R -> C (in GM1G1).
{ECO:0000269|PubMed:10338095,
ECO:0000269|PubMed:15714521,
ECO:0000269|PubMed:17309651,
ECO:0000269|PubMed:8213816}.
/FTId=VAR_008676.
VARIANT 214 214 D -> Y (in GM1G3). {ECO:0000269|Ref.24}.
/FTId=VAR_013543.
VARIANT 216 216 V -> A (in GM1G1). {ECO:0000269|Ref.24}.
/FTId=VAR_013544.
VARIANT 236 236 L -> P (in GM1G1; decrease in
galactosidase activity).
{ECO:0000269|PubMed:25936995}.
/FTId=VAR_074056.
VARIANT 239 239 T -> M (in GM1G1; loss of galactosidase
activity; severe mutation; causes a rapid
degradation of the protein precursor).
{ECO:0000269|PubMed:15714521,
ECO:0000269|PubMed:19472408}.
/FTId=VAR_026132.
VARIANT 240 240 V -> M (in GM1G1).
{ECO:0000269|PubMed:10338095}.
/FTId=VAR_008677.
VARIANT 255 255 Q -> H (in GM1G1; 2.4% of wild-type
galactosidase activity).
{ECO:0000269|PubMed:19472408}.
/FTId=VAR_062354.
VARIANT 262 262 G -> E (in GM1G2; decrease in
galactosidase activity).
{ECO:0000269|PubMed:25936995}.
/FTId=VAR_074057.
VARIANT 263 263 P -> S (in GM1G3). {ECO:0000269|Ref.26}.
/FTId=VAR_013545.
VARIANT 264 264 L -> S (in GM1G2).
{ECO:0000269|PubMed:16941474}.
/FTId=VAR_062355.
VARIANT 266 266 N -> S (in GM1G3).
{ECO:0000269|PubMed:9203065}.
/FTId=VAR_013546.
VARIANT 270 270 Y -> D (in GM1G3; originally classified
as Morquio syndrome).
{ECO:0000269|PubMed:11511921,
ECO:0000269|PubMed:19472408}.
/FTId=VAR_013547.
VARIANT 272 272 G -> D (in GM1G1).
{ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17309651}.
/FTId=VAR_038346.
VARIANT 273 273 W -> L (in MPS4B; decreased galactosidase
activity). {ECO:0000269|PubMed:11511921,
ECO:0000269|PubMed:16538002,
ECO:0000269|PubMed:1928092,
ECO:0000269|PubMed:19472408}.
/FTId=VAR_003333.
VARIANT 281 281 H -> Y (in GM1G1 and GM1G3).
{ECO:0000269|PubMed:11511921,
ECO:0000269|PubMed:15714521}.
/FTId=VAR_013548.
VARIANT 297 297 L -> F (in GM1G3; decrease in
galactosidase activity).
{ECO:0000269|PubMed:25936995}.
/FTId=VAR_074058.
VARIANT 314 314 F -> L (in GM1G2; decrease in
galactosidase activity).
{ECO:0000269|PubMed:25936995}.
/FTId=VAR_074059.
VARIANT 316 316 Y -> C (in GM1G1).
{ECO:0000269|PubMed:1907800}.
/FTId=VAR_003334.
VARIANT 318 318 N -> H (in GM1G1; unknown pathological
significance).
{ECO:0000269|PubMed:16538002}.
/FTId=VAR_062356.
VARIANT 329 329 T -> I (in GM1G1; 5.0% of wild-type
galactosidase activity).
{ECO:0000269|PubMed:19472408}.
/FTId=VAR_062357.
VARIANT 331 331 Y -> C (in GM1G1; unknown pathological
significance).
{ECO:0000269|PubMed:25936995}.
/FTId=VAR_074060.
VARIANT 332 332 D -> E (in GM1G1; 2.3% of wild-type
galactosidase activity).
{ECO:0000269|PubMed:19472408}.
/FTId=VAR_062358.
VARIANT 332 332 D -> N (in GM1G1; decrease in
galactosidase activity).
{ECO:0000269|PubMed:10839995,
ECO:0000269|PubMed:25936995}.
/FTId=VAR_013549.
VARIANT 333 333 Y -> H (in GM1G2; 3.0% of wild-type
galactosidase activity; the mutant
protein is localized in the lysosomal-
endosomal compartment).
{ECO:0000269|PubMed:19472408}.
/FTId=VAR_062359.
VARIANT 337 337 L -> P (in GM1G1 and GM1G2; loss of
galactosidase activity).
{ECO:0000269|PubMed:25936995}.
/FTId=VAR_074061.
VARIANT 346 346 K -> N (in GM1G1).
{ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:19472408}.
/FTId=VAR_062360.
VARIANT 347 347 Y -> C (in GM1G1).
{ECO:0000269|PubMed:16941474}.
/FTId=VAR_062361.
VARIANT 377 381 Missing (in GM1G1).
{ECO:0000269|PubMed:17309651}.
/FTId=VAR_037941.
VARIANT 397 397 P -> A (in MPS4B; 24.0% of wild-type
galactosidase activity).
{ECO:0000269|PubMed:19472408}.
/FTId=VAR_062362.
VARIANT 408 408 Q -> P (in MPS4B; 1.1% of wild-type
galactosidase activity).
{ECO:0000269|PubMed:11511921,
ECO:0000269|PubMed:19472408}.
/FTId=VAR_013550.
VARIANT 414 414 G -> V (in GM1G2; decrease in
galactosidase activity).
{ECO:0000269|PubMed:25936995}.
/FTId=VAR_074062.
VARIANT 420 420 T -> K (in GM1G3; decrease in
galactosidase activity).
{ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17664528}.
/FTId=VAR_062363.
VARIANT 420 420 T -> P (in GM1G1; loss of galactosidase
activity). {ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17664528}.
/FTId=VAR_062364.
VARIANT 422 422 L -> R (in GM1G1).
{ECO:0000269|PubMed:16941474}.
/FTId=VAR_062365.
VARIANT 434 434 S -> L (in GM1-gangliosidosis;
unclassified clinical type).
{ECO:0000269|PubMed:17309651}.
/FTId=VAR_037942.
VARIANT 436 436 L -> F (seems to have a modulating action
in the expression of the severity of
other mutations; dbSNP:rs34421970).
{ECO:0000269|PubMed:12644936,
ECO:0000269|PubMed:16941474}.
/FTId=VAR_026133.
VARIANT 438 438 G -> E (in GM1G3 and MPS4B; mild form;
5.7% of wild-type galactosidase
activity). {ECO:0000269|PubMed:12393180,
ECO:0000269|PubMed:15986423,
ECO:0000269|PubMed:19472408}.
/FTId=VAR_013551.
VARIANT 441 441 D -> N (in GM1G1; loss of galactosidase
activity). {ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17664528}.
/FTId=VAR_062366.
VARIANT 442 442 R -> Q (in GM1G1).
{ECO:0000269|PubMed:19472408}.
/FTId=VAR_062367.
VARIANT 444 444 Y -> C (in MPS4B; loss of galactosidase
activity). {ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17664528}.
/FTId=VAR_062368.
VARIANT 457 457 R -> Q (in GM1G3).
{ECO:0000269|PubMed:1907800}.
/FTId=VAR_003335.
VARIANT 482 482 R -> C (in MPS4B; loss of galactosidase
activity). {ECO:0000269|PubMed:7586649}.
/FTId=VAR_008678.
VARIANT 482 482 R -> H (in MPS4B and GM1G1; severe
decrease in galactosidase activity).
{ECO:0000269|PubMed:10737981,
ECO:0000269|PubMed:1487238,
ECO:0000269|PubMed:15714521,
ECO:0000269|PubMed:16538002,
ECO:0000269|PubMed:1928092,
ECO:0000269|PubMed:25936995}.
/FTId=VAR_003336.
VARIANT 484 484 N -> K (in MPS4B; mild form; fibroblasts
from MPS4B compound heterozygotes for K-
484 and A-500 have 1.9% of wild-type
galactosidase activity).
{ECO:0000269|PubMed:12393180}.
/FTId=VAR_013552.
VARIANT 491 491 D -> N (in GM1G1).
{ECO:0000269|PubMed:10338095}.
/FTId=VAR_008679.
VARIANT 491 491 D -> Y (in GM1G1).
{ECO:0000269|PubMed:17309651}.
/FTId=VAR_037943.
VARIANT 493 493 K -> N (in GM1G2; decrease in
galactosidase activity).
{ECO:0000269|PubMed:25936995}.
/FTId=VAR_074063.
VARIANT 494 494 G -> C (in GM1G1).
{ECO:0000269|PubMed:1928092}.
/FTId=VAR_013553.
VARIANT 494 494 G -> S (in MPS4B; loss of galactosidase
activity). {ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17664528}.
/FTId=VAR_062369.
VARIANT 500 500 T -> A (in MPS4B; mild form; 2.1% of
wild-type galactosidase activity).
{ECO:0000269|PubMed:11511921,
ECO:0000269|PubMed:12393180,
ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:19472408}.
/FTId=VAR_013554.
VARIANT 509 509 W -> C (in MPS4B; also in a patient with
a slowly progressive form of GM1-
gangisidosis; loss of galactosidase
activity). {ECO:0000269|PubMed:16538002,
ECO:0000269|PubMed:1928092,
ECO:0000269|PubMed:9203065}.
/FTId=VAR_003337.
VARIANT 514 514 L -> P (in GM1G1; decrease in
galactosidase activity).
{ECO:0000269|PubMed:25936995}.
/FTId=VAR_074064.
VARIANT 521 521 R -> C (in GM1G1; mild phenotype; unknown
pathological significance; reduction of
galactosidase activity; dbSNP:rs4302331).
{ECO:0000269|PubMed:10338095,
ECO:0000269|PubMed:15714521,
ECO:0000269|PubMed:16641997,
ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17664528,
ECO:0000269|PubMed:25936995}.
/FTId=VAR_008680.
VARIANT 532 532 S -> G (polymorphism; results in near-
normal activity corresponding to 60%-100%
of the wild-type depending on the
expression system).
{ECO:0000269|PubMed:10338095,
ECO:0000269|PubMed:10839995,
ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17664528,
ECO:0000269|Ref.24}.
/FTId=VAR_008681.
VARIANT 549 549 P -> L (in GM1G1).
{ECO:0000269|PubMed:17309651}.
/FTId=VAR_037944.
VARIANT 554 554 G -> E (in GM1-gangliosidosis;
unclassified clinical type).
{ECO:0000269|PubMed:17309651}.
/FTId=VAR_037945.
VARIANT 578 578 K -> R (in GM1G1).
{ECO:0000269|PubMed:8213816}.
/FTId=VAR_008682.
VARIANT 579 579 G -> D (in GM1G1 and GM1G2; loss of
galactosidase activity; severe mutation).
{ECO:0000269|PubMed:10737981,
ECO:0000269|PubMed:15714521}.
/FTId=VAR_013555.
VARIANT 590 590 R -> C (in GM1G1; loss of galactosidase
activity). {ECO:0000269|PubMed:16941474,
ECO:0000269|PubMed:17309651,
ECO:0000269|PubMed:17664528}.
/FTId=VAR_037946.
VARIANT 590 590 R -> H (in GM1G2).
{ECO:0000269|PubMed:8213816}.
/FTId=VAR_008683.
VARIANT 591 591 Y -> C (in GM1G1; with cardiac
involvement in some patients; loss of
galactosidase activity; severe mutation;
causes a rapid degradation of the protein
precursor). {ECO:0000269|PubMed:10737981,
ECO:0000269|PubMed:15714521,
ECO:0000269|Ref.27}.
/FTId=VAR_008684.
VARIANT 591 591 Y -> N (in GM1G1; with cardiac
involvement in some patients; loss of
galactosidase activity; severe mutation;
causes a rapid degradation of the protein
precursor). {ECO:0000269|PubMed:10737981,
ECO:0000269|PubMed:15714521,
ECO:0000269|Ref.27}.
/FTId=VAR_008685.
VARIANT 595 595 R -> W (reduction of galactosidase
activity). {ECO:0000269|PubMed:17661814}.
/FTId=VAR_037947.
VARIANT 597 597 P -> L (in GM1G2; decrease in
galactosidase activity).
{ECO:0000269|PubMed:25936995}.
/FTId=VAR_074065.
VARIANT 597 597 P -> S (in GM1G1; 2.1% of wild-type
galactosidase activity).
{ECO:0000269|PubMed:19472408}.
/FTId=VAR_062370.
VARIANT 600 600 T -> I (in GM1G2; decrease in
galactosidase activity).
{ECO:0000269|PubMed:25936995}.
/FTId=VAR_074066.
VARIANT 632 632 E -> G (in GM1G2).
{ECO:0000269|PubMed:8213816}.
/FTId=VAR_008686.
CONFLICT 89 89 H -> Y (in Ref. 4; BAH13196).
{ECO:0000305}.
CONFLICT 201 201 R -> A (in Ref. 1; AAA51822).
{ECO:0000305}.
STRAND 32 35 {ECO:0000244|PDB:3THD}.
TURN 36 39 {ECO:0000244|PDB:3THD}.
STRAND 40 43 {ECO:0000244|PDB:3THD}.
STRAND 46 48 {ECO:0000244|PDB:3THD}.
STRAND 51 54 {ECO:0000244|PDB:3THD}.
HELIX 57 59 {ECO:0000244|PDB:3THD}.
HELIX 62 64 {ECO:0000244|PDB:3THD}.
HELIX 65 74 {ECO:0000244|PDB:3THD}.
STRAND 78 83 {ECO:0000244|PDB:3THD}.
HELIX 86 89 {ECO:0000244|PDB:3THD}.
HELIX 100 102 {ECO:0000244|PDB:3THD}.
HELIX 104 113 {ECO:0000244|PDB:3THD}.
STRAND 117 121 {ECO:0000244|PDB:3THD}.
HELIX 131 134 {ECO:0000244|PDB:3THD}.
HELIX 137 141 {ECO:0000244|PDB:3THD}.
STRAND 147 149 {ECO:0000244|PDB:3THD}.
HELIX 152 169 {ECO:0000244|PDB:3THD}.
HELIX 170 172 {ECO:0000244|PDB:3THD}.
HELIX 174 176 {ECO:0000244|PDB:3THD}.
STRAND 178 184 {ECO:0000244|PDB:3THD}.
STRAND 186 188 {ECO:0000244|PDB:3WF0}.
HELIX 189 191 {ECO:0000244|PDB:3THD}.
HELIX 197 211 {ECO:0000244|PDB:3THD}.
STRAND 213 224 {ECO:0000244|PDB:3THD}.
HELIX 225 231 {ECO:0000244|PDB:3THD}.
STRAND 236 241 {ECO:0000244|PDB:3THD}.
HELIX 248 258 {ECO:0000244|PDB:3THD}.
STRAND 260 262 {ECO:0000244|PDB:3THD}.
STRAND 265 272 {ECO:0000244|PDB:3THD}.
HELIX 286 298 {ECO:0000244|PDB:3THD}.
STRAND 302 306 {ECO:0000244|PDB:3THD}.
TURN 322 324 {ECO:0000244|PDB:3THD}.
HELIX 345 354 {ECO:0000244|PDB:3THD}.
TURN 355 357 {ECO:0000244|PDB:3THD}.
STRAND 375 378 {ECO:0000244|PDB:3THD}.
STRAND 380 384 {ECO:0000244|PDB:3THD}.
TURN 385 388 {ECO:0000244|PDB:3THD}.
HELIX 389 392 {ECO:0000244|PDB:3THD}.
STRAND 398 402 {ECO:0000244|PDB:3THD}.
HELIX 407 409 {ECO:0000244|PDB:3THD}.
STRAND 413 421 {ECO:0000244|PDB:3THD}.
STRAND 426 433 {ECO:0000244|PDB:3THD}.
STRAND 439 447 {ECO:0000244|PDB:3THD}.
STRAND 450 456 {ECO:0000244|PDB:3THD}.
TURN 457 459 {ECO:0000244|PDB:3THD}.
STRAND 462 467 {ECO:0000244|PDB:3THD}.
STRAND 472 478 {ECO:0000244|PDB:3THD}.
HELIX 487 489 {ECO:0000244|PDB:3THD}.
STRAND 509 513 {ECO:0000244|PDB:3THD}.
HELIX 516 521 {ECO:0000244|PDB:3THD}.
TURN 522 527 {ECO:0000244|PDB:3THD}.
STRAND 550 556 {ECO:0000244|PDB:3THD}.
STRAND 568 572 {ECO:0000244|PDB:3THD}.
STRAND 578 583 {ECO:0000244|PDB:3THD}.
STRAND 586 591 {ECO:0000244|PDB:3THD}.
TURN 593 595 {ECO:0000244|PDB:3THD}.
STRAND 601 603 {ECO:0000244|PDB:3THD}.
HELIX 605 607 {ECO:0000244|PDB:3THD}.
STRAND 610 612 {ECO:0000244|PDB:3THD}.
STRAND 614 622 {ECO:0000244|PDB:3THD}.
STRAND 627 629 {ECO:0000244|PDB:3THD}.
HELIX 631 633 {ECO:0000244|PDB:3THD}.
STRAND 634 641 {ECO:0000244|PDB:3THD}.
SEQUENCE 677 AA; 76075 MW; 74421586B1BCFECA CRC64;
MPGFLVRILP LLLVLLLLGP TRGLRNATQR MFEIDYSRDS FLKDGQPFRY ISGSIHYSRV
PRFYWKDRLL KMKMAGLNAI QTYVPWNFHE PWPGQYQFSE DHDVEYFLRL AHELGLLVIL
RPGPYICAEW EMGGLPAWLL EKESILLRSS DPDYLAAVDK WLGVLLPKMK PLLYQNGGPV
ITVQVENEYG SYFACDFDYL RFLQKRFRHH LGDDVVLFTT DGAHKTFLKC GALQGLYTTV
DFGTGSNITD AFLSQRKCEP KGPLINSEFY TGWLDHWGQP HSTIKTEAVA SSLYDILARG
ASVNLYMFIG GTNFAYWNGA NSPYAAQPTS YDYDAPLSEA GDLTEKYFAL RNIIQKFEKV
PEGPIPPSTP KFAYGKVTLE KLKTVGAALD ILCPSGPIKS LYPLTFIQVK QHYGFVLYRT
TLPQDCSNPA PLSSPLNGVH DRAYVAVDGI PQGVLERNNV ITLNITGKAG ATLDLLVENM
GRVNYGAYIN DFKGLVSNLT LSSNILTDWT IFPLDTEDAV RSHLGGWGHR DSGHHDEAWA
HNSSNYTLPA FYMGNFSIPS GIPDLPQDTF IQFPGWTKGQ VWINGFNLGR YWPARGPQLT
LFVPQHILMT SAPNTITVLE LEWAPCSSDD PELCAVTFVD RPVIGSSVTY DHPSKPVEKR
LMPPPPQKNK DSWLDHV


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