Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Galectin-1 (Gal-1) (14 kDa laminin-binding protein) (HLBP14) (14 kDa lectin) (Beta-galactoside-binding lectin L-14-I) (Galaptin) (HBL) (HPL) (Lactose-binding lectin 1) (Lectin galactoside-binding soluble 1) (Putative MAPK-activating protein PM12) (S-Lac lectin 1)

 LEG1_HUMAN              Reviewed;         135 AA.
P09382; B2R5E8; Q9UDK5;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
23-MAY-2018, entry version 218.
RecName: Full=Galectin-1;
Short=Gal-1;
AltName: Full=14 kDa laminin-binding protein;
Short=HLBP14;
AltName: Full=14 kDa lectin;
AltName: Full=Beta-galactoside-binding lectin L-14-I;
AltName: Full=Galaptin;
AltName: Full=HBL;
AltName: Full=HPL;
AltName: Full=Lactose-binding lectin 1;
AltName: Full=Lectin galactoside-binding soluble 1;
AltName: Full=Putative MAPK-activating protein PM12;
AltName: Full=S-Lac lectin 1;
Name=LGALS1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
PubMed=2719964; DOI=10.1016/0167-4781(89)90173-5;
Hirabayashi J., Ayaki K., Soma G., Kasai K.;
"Cloning and nucleotide sequence of a full-length cDNA for human 14
kDa beta-galactoside-binding lectin.";
Biochim. Biophys. Acta 1008:85-91(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta, and Promyelocytic leukemia;
PubMed=2910856;
Couraud P.-O., Casentini-Borocz D., Bringman T.S., Griffith J.,
McGrogan M., Nedwin G.E.;
"Molecular cloning, characterization, and expression of a human 14-kDa
lectin.";
J. Biol. Chem. 264:1310-1316(1989).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Hepatoma;
PubMed=2719646; DOI=10.1042/bj2590291;
Abbott W.M., Feizi T.;
"Evidence that the 14 kDa soluble beta-galactoside-binding lectin in
man is encoded by a single gene.";
Biochem. J. 259:291-294(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Placenta;
PubMed=18824694; DOI=10.1073/pnas.0807606105;
Than N.G., Romero R., Erez O., Weckle A., Tarca A.L., Hotra J.,
Abbas A., Han Y.M., Kim S.S., Kusanovic J.P., Gotsch F., Hou Z.,
Santolaya-Forgas J., Benirschke K., Papp Z., Grossman L.I.,
Goodman M., Wildman D.E.;
"Emergence of hormonal and redox regulation of galectin-1 in placental
mammals: implication in maternal-fetal immune tolerance.";
Proc. Natl. Acad. Sci. U.S.A. 105:15819-15824(2008).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lymphocyte;
PubMed=1988031; DOI=10.1021/bi00215a013;
Gitt M.A., Barondes S.H.;
"Genomic sequence and organization of two members of a human lectin
gene family.";
Biochemistry 30:82-89(1991).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung fibroblast;
PubMed=12761501; DOI=10.1038/sj.onc.1206406;
Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
Sugano S.;
"Large-scale identification and characterization of human genes that
activate NF-kappaB and MAPK signaling pathways.";
Oncogene 22:3307-3318(2003).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thalamus;
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, and Skin;
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).
[13]
PROTEIN SEQUENCE OF 2-135.
TISSUE=Placenta;
PubMed=3065332;
Hirabayashi J., Kasai K.;
"Complete amino acid sequence of a beta-galactoside-binding lectin
from human placenta.";
J. Biochem. 104:1-4(1988).
[14]
PROTEIN SEQUENCE OF 2-135.
TISSUE=Brain;
Bladier D., le Caer J.-P., Joubert R., Caron M., Rossier J.;
"Beta-galactosidase soluble lectin from human brain: complete amino
acid sequence.";
Neurochem. Int. 18:275-281(1991).
[15]
PROTEIN SEQUENCE OF 2-19.
TISSUE=Platelet;
PubMed=12665801; DOI=10.1038/nbt810;
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A.,
Thomas G.R., Vandekerckhove J.;
"Exploring proteomes and analyzing protein processing by mass
spectrometric identification of sorted N-terminal peptides.";
Nat. Biotechnol. 21:566-569(2003).
[16]
PROTEIN SEQUENCE OF 38-49; 101-108 AND 113-128, AND IDENTIFICATION BY
MASS SPECTROMETRY.
TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
Lubec G., Vishwanath V., Chen W.-Q., Sun Y.;
Submitted (DEC-2008) to UniProtKB.
[17]
PROTEIN SEQUENCE OF 70-87 AND 122-133.
TISSUE=Placenta;
PubMed=3611046; DOI=10.1093/oxfordjournals.jbchem.a121968;
Hirabayashi J., Kawasaki H., Suzuki K., Kasai K.;
"Further characterization and structural studies on human placenta
lectin.";
J. Biochem. 101:987-995(1987).
[18]
PROTEIN SEQUENCE OF 20-29; 50-74 AND 132-135, AND INTERACTION WITH
LAMININ.
TISSUE=Melanoma;
PubMed=1386213; DOI=10.1016/0003-9861(92)90650-L;
Castronovo V., Luyten F., van den Brule F., Sobel M.E.;
"Identification of a 14-kDa laminin binding protein (HLBP14) in human
melanoma cells that is identical to the 14-kDa galactoside binding
lectin.";
Arch. Biochem. Biophys. 297:132-138(1992).
[19]
PARTIAL PROTEIN SEQUENCE.
TISSUE=Spleen;
PubMed=2383549; DOI=10.1021/bi00474a014;
Sharma A., Chemelli R., Allen H.J.;
"Human splenic galaptin: physicochemical characterization.";
Biochemistry 29:5309-5314(1990).
[20]
CHARACTERIZATION.
PubMed=7501023; DOI=10.1038/378736a0;
Perillo N.L., Pace K.E., Seilhamer J.J., Baum L.G.;
"Apoptosis of T cells mediated by galectin-1.";
Nature 378:736-739(1995).
[21]
CHARACTERIZATION.
TISSUE=Placenta;
PubMed=10369126; DOI=10.1016/S0165-2478(99)00012-7;
Walzel H., Schulz U., Neels P., Brock J.;
"Galectin-1, a natural ligand for the receptor-type protein tyrosine
phosphatase CD45.";
Immunol. Lett. 67:193-202(1999).
[22]
CHARACTERIZATION.
PubMed=10764829; DOI=10.1093/glycob/10.4.413;
Fouillit M., Joubert-Caron R., Poirier F., Bourin P., Monostori E.,
Levi-Strauss M., Raphael M., Bladier D., Caron M.;
"Regulation of CD45-induced signaling by galectin-1 in Burkitt
lymphoma B cells.";
Glycobiology 10:413-419(2000).
[23]
INTERACTION WITH LGALS3BP.
PubMed=11146440;
DOI=10.1002/1097-0215(200002)9999:9999<::AID-IJC1022>3.3.CO;2-Q;
Tinari N., Kuwabara I., Huflejt M.E., Shen P.F., Iacobelli S.,
Liu F.-T.;
"Glycoprotein 90K/MAC-2BP interacts with galectin-1 and mediates
galectin-1-induced cell aggregation.";
Int. J. Cancer 91:167-172(2001).
[24]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=14617626; DOI=10.1074/jbc.M311183200;
He J., Baum L.G.;
"Presentation of galectin-1 by extracellular matrix triggers T cell
death.";
J. Biol. Chem. 279:4705-4712(2004).
[25]
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Mammary cancer;
Ahamed M.E., Ahmed M.E., Eltoum A.M., Altahir G.O., Ahmed K.M.,
Harbi S.O., Stansalas J., Mohamed A.O.;
"Abnormal proteins in primary breast cancer tissues from 25 Sudanese
patients.";
Eur. J. Inflamm. 6:115-121(2008).
[26]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=19497882; DOI=10.1073/pnas.0903568106;
Than N.G., Romero R., Goodman M., Weckle A., Xing J., Dong Z., Xu Y.,
Tarquini F., Szilagyi A., Gal P., Hou Z., Tarca A.L., Kim C.J.,
Kim J.S., Haidarian S., Uddin M., Bohn H., Benirschke K.,
Santolaya-Forgas J., Grossman L.I., Erez O., Hassan S.S.,
Zavodszky P., Papp Z., Wildman D.E.;
"A primate subfamily of galectins expressed at the maternal-fetal
interface that promote immune cell death.";
Proc. Natl. Acad. Sci. U.S.A. 106:9731-9736(2009).
[27]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-29, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[28]
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).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22905912; DOI=10.1021/pr300539b;
Rosenow A., Noben J.P., Jocken J., Kallendrusch S.,
Fischer-Posovszky P., Mariman E.C., Renes J.;
"Resveratrol-induced changes of the human adipocyte secretion
profile.";
J. Proteome Res. 11:4733-4743(2012).
[30]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[31]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[32]
INTERACTION WITH SUSD2.
PubMed=23131994; DOI=10.1158/1541-7786.MCR-12-0501-T;
Watson A.P., Evans R.L., Egland K.A.;
"Multiple functions of sushi domain containing 2 (SUSD2) in breast
tumorigenesis.";
Mol. Cancer Res. 11:74-85(2013).
[33]
INTERACTION WITH CD6 AND ALCAM, AND FUNCTION.
PubMed=24945728; DOI=10.1016/j.febslet.2014.05.064;
Escoda-Ferran C., Carrasco E., Caballero-Banos M., Miro-Julia C.,
Martinez-Florensa M., Consuegra-Fernandez M., Martinez V.G., Liu F.T.,
Lozano F.;
"Modulation of CD6 function through interaction with galectin-1 and
-3.";
FEBS Lett. 588:2805-2813(2014).
[34]
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).
[35]
PHOSPHORYLATION AT SER-30.
PubMed=26091039; DOI=10.1016/j.cell.2015.05.028;
Tagliabracci V.S., Wiley S.E., Guo X., Kinch L.N., Durrant E., Wen J.,
Xiao J., Cui J., Nguyen K.B., Engel J.L., Coon J.J., Grishin N.,
Pinna L.A., Pagliarini D.J., Dixon J.E.;
"A single kinase generates the majority of the secreted
phosphoproteome.";
Cell 161:1619-1632(2015).
[36]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[37]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH CARBOHYDRATE,
AND SUBUNIT.
PubMed=15476813; DOI=10.1016/j.jmb.2004.08.078;
Lopez-Lucendo M.F., Solis D., Andre S., Hirabayashi J., Kasai K.,
Kaltner H., Gabius H.-J., Romero A.;
"Growth-regulatory human galectin-1: crystallographic characterisation
of the structural changes induced by single-site mutations and their
impact on the thermodynamics of ligand binding.";
J. Mol. Biol. 343:957-970(2004).
[38]
X-RAY CRYSTALLOGRAPHY (1.86 ANGSTROMS) OF 2-135 IN COMPLEX WITH
LACTOSE, INTERACTION WITH CD2; CD3; CD7; CD43 AND CD45, SUBUNIT, AND
FUNCTION.
PubMed=18796645; DOI=10.1093/glycob/cwn089;
Nishi N., Abe A., Iwaki J., Yoshida H., Itoh A., Shoji H.,
Kamitori S., Hirabayashi J., Nakamura T.;
"Functional and structural bases of a cysteine-less mutant as a long-
lasting substitute for galectin-1.";
Glycobiology 18:1065-1073(2008).
[39]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS).
PubMed=19128029; DOI=10.1021/bi801855g;
Di Lella S., Ma L., Ricci J.C., Rabinovich G.A., Asher S.A.,
Alvarez R.M.S.;
"Critical role of the solvent environment in galectin-1 binding to the
disaccharide lactose.";
Biochemistry 48:786-791(2009).
-!- FUNCTION: Lectin that binds beta-galactoside and a wide array of
complex carbohydrates. Plays a role in regulating apoptosis, cell
proliferation and cell differentiation. Inhibits CD45 protein
phosphatase activity and therefore the dephosphorylation of Lyn
kinase. Strong inducer of T-cell apoptosis.
{ECO:0000269|PubMed:14617626, ECO:0000269|PubMed:18796645,
ECO:0000269|PubMed:19497882, ECO:0000269|PubMed:24945728}.
-!- SUBUNIT: Homodimer. Binds LGALS3BP. Interacts with CD2, CD3, CD4,
CD6, CD7, CD43, ALCAM and CD45. Interacts with laminin (via poly-
N-acetyllactosamine). Interacts with SUSD2.
{ECO:0000269|PubMed:11146440, ECO:0000269|PubMed:1386213,
ECO:0000269|PubMed:15476813, ECO:0000269|PubMed:18796645,
ECO:0000269|PubMed:23131994, ECO:0000269|PubMed:24945728}.
-!- INTERACTION:
Q13740:ALCAM; NbExp=3; IntAct=EBI-1048875, EBI-1188108;
P30203:CD6; NbExp=2; IntAct=EBI-1048875, EBI-2873748;
P35968:KDR; NbExp=3; IntAct=EBI-1048875, EBI-1005487;
P08575:PTPRC; NbExp=2; IntAct=EBI-1048875, EBI-1341;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix {ECO:0000269|PubMed:14617626}.
-!- TISSUE SPECIFICITY: Expressed in placenta, maternal decidua and
fetal membranes. Within placenta, expressed in trophoblasts,
stromal cells, villous endothelium, syncytiotrophoblast apical
membrane and villous stroma. Within fetal membranes, expressed in
amnion, chorioamniotic mesenchyma and chorion (at protein level).
Expressed in cardiac, smooth, and skeletal muscle, neurons,
thymus, kidney and hematopoietic cells.
{ECO:0000269|PubMed:18824694, ECO:0000269|PubMed:19497882}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Galectin-1;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_hum_Stlect_00116";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X14829; CAA32938.1; -; mRNA.
EMBL; J04456; AAA36170.1; -; mRNA.
EMBL; X15256; CAA33328.1; -; mRNA.
EMBL; EU363770; ACA58297.1; -; mRNA.
EMBL; M57678; AAB00777.1; -; Genomic_DNA.
EMBL; AB097036; BAC77389.1; -; mRNA.
EMBL; CR456511; CAG30397.1; -; mRNA.
EMBL; AK312161; BAG35095.1; -; mRNA.
EMBL; BT006775; AAP35421.1; -; mRNA.
EMBL; Z83844; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471095; EAW60178.1; -; Genomic_DNA.
EMBL; BC001693; AAH01693.1; -; mRNA.
EMBL; BC020675; AAH20675.1; -; mRNA.
CCDS; CCDS13954.1; -.
PIR; A37134; LNHUGB.
RefSeq; NP_002296.1; NM_002305.3.
UniGene; Hs.445351; -.
PDB; 1GZW; X-ray; 1.70 A; A/B=2-135.
PDB; 1W6M; X-ray; 2.30 A; A/B=2-135.
PDB; 1W6N; X-ray; 1.65 A; A/B=2-135.
PDB; 1W6O; X-ray; 1.90 A; A/B=2-135.
PDB; 1W6P; X-ray; 1.80 A; A/B=2-135.
PDB; 1W6Q; X-ray; 2.10 A; A/B=2-135.
PDB; 2KM2; NMR; -; A/B=2-135.
PDB; 2ZKN; X-ray; 1.86 A; A/B=2-135.
PDB; 3OY8; X-ray; 2.19 A; A/B=2-135.
PDB; 3OYW; X-ray; 2.50 A; A/B=2-135.
PDB; 3T2T; X-ray; 1.90 A; A/B=1-135.
PDB; 3W58; X-ray; 1.58 A; A/B/C/D=2-135.
PDB; 3W59; X-ray; 2.10 A; A/B/C/D=2-135.
PDB; 4Q1P; X-ray; 1.46 A; A/B=1-135.
PDB; 4Q1R; X-ray; 1.47 A; A/B=1-135.
PDB; 4Q26; X-ray; 1.40 A; A/B/G/H=1-135.
PDB; 4Q27; X-ray; 1.20 A; A/B=1-135.
PDB; 4Q2F; X-ray; 1.40 A; A/B=1-135.
PDB; 4XBL; X-ray; 1.93 A; A/B=1-135.
PDB; 4Y1U; X-ray; 1.76 A; A/B=3-135.
PDB; 4Y1V; X-ray; 2.32 A; A/B=3-135.
PDB; 4Y1X; X-ray; 2.45 A; A/B=3-135.
PDB; 4Y1Y; X-ray; 1.86 A; A/B=4-135.
PDB; 4Y1Z; X-ray; 2.23 A; A/B=3-135.
PDB; 4Y20; X-ray; 2.20 A; A/B=3-135.
PDB; 4Y22; X-ray; 2.50 A; A/B=3-135.
PDB; 4Y24; X-ray; 2.32 A; A/B=3-135.
PDB; 5MWT; X-ray; 1.71 A; A/B=3-135.
PDB; 5MWX; X-ray; 1.29 A; A/B=3-135.
PDBsum; 1GZW; -.
PDBsum; 1W6M; -.
PDBsum; 1W6N; -.
PDBsum; 1W6O; -.
PDBsum; 1W6P; -.
PDBsum; 1W6Q; -.
PDBsum; 2KM2; -.
PDBsum; 2ZKN; -.
PDBsum; 3OY8; -.
PDBsum; 3OYW; -.
PDBsum; 3T2T; -.
PDBsum; 3W58; -.
PDBsum; 3W59; -.
PDBsum; 4Q1P; -.
PDBsum; 4Q1R; -.
PDBsum; 4Q26; -.
PDBsum; 4Q27; -.
PDBsum; 4Q2F; -.
PDBsum; 4XBL; -.
PDBsum; 4Y1U; -.
PDBsum; 4Y1V; -.
PDBsum; 4Y1X; -.
PDBsum; 4Y1Y; -.
PDBsum; 4Y1Z; -.
PDBsum; 4Y20; -.
PDBsum; 4Y22; -.
PDBsum; 4Y24; -.
PDBsum; 5MWT; -.
PDBsum; 5MWX; -.
ProteinModelPortal; P09382; -.
SMR; P09382; -.
BioGrid; 110147; 111.
CORUM; P09382; -.
DIP; DIP-46153N; -.
IntAct; P09382; 25.
MINT; P09382; -.
STRING; 9606.ENSP00000215909; -.
BindingDB; P09382; -.
ChEMBL; CHEMBL4915; -.
DrugBank; DB03345; Beta-Mercaptoethanol.
DrugBank; DB04396; Thiodigalactoside.
iPTMnet; P09382; -.
PhosphoSitePlus; P09382; -.
SwissPalm; P09382; -.
BioMuta; LGALS1; -.
DMDM; 126155; -.
DOSAC-COBS-2DPAGE; P09382; -.
REPRODUCTION-2DPAGE; IPI00219219; -.
REPRODUCTION-2DPAGE; P09382; -.
SWISS-2DPAGE; P09382; -.
UCD-2DPAGE; P09382; -.
EPD; P09382; -.
MaxQB; P09382; -.
PaxDb; P09382; -.
PeptideAtlas; P09382; -.
PRIDE; P09382; -.
TopDownProteomics; P09382; -.
DNASU; 3956; -.
Ensembl; ENST00000215909; ENSP00000215909; ENSG00000100097.
GeneID; 3956; -.
KEGG; hsa:3956; -.
UCSC; uc003atn.4; human.
CTD; 3956; -.
DisGeNET; 3956; -.
EuPathDB; HostDB:ENSG00000100097.11; -.
GeneCards; LGALS1; -.
HGNC; HGNC:6561; LGALS1.
HPA; CAB002157; -.
HPA; HPA000646; -.
HPA; HPA000687; -.
HPA; HPA001130; -.
MIM; 150570; gene.
neXtProt; NX_P09382; -.
OpenTargets; ENSG00000100097; -.
PharmGKB; PA30337; -.
eggNOG; KOG3587; Eukaryota.
eggNOG; ENOG4111EA0; LUCA.
GeneTree; ENSGT00440000034263; -.
HOGENOM; HOG000059539; -.
HOVERGEN; HBG006255; -.
InParanoid; P09382; -.
KO; K06830; -.
OMA; CNSKEDG; -.
OrthoDB; EOG091G0S7H; -.
PhylomeDB; P09382; -.
TreeFam; TF315551; -.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
SIGNOR; P09382; -.
ChiTaRS; LGALS1; human.
EvolutionaryTrace; P09382; -.
GeneWiki; Galectin-1; -.
GeneWiki; LGALS1; -.
GenomeRNAi; 3956; -.
PMAP-CutDB; P09382; -.
PRO; PR:P09382; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000100097; -.
CleanEx; HS_LGALS1; -.
ExpressionAtlas; P09382; baseline and differential.
Genevisible; P09382; HS.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; HDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0005622; C:intracellular; IDA:LIFEdb.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
GO; GO:0030395; F:lactose binding; IEA:Ensembl.
GO; GO:0043236; F:laminin binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0004871; F:signal transducer activity; HMP:UniProtKB.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0045445; P:myoblast differentiation; IEA:Ensembl.
GO; GO:0010812; P:negative regulation of cell-substrate adhesion; IEA:Ensembl.
GO; GO:0010977; P:negative regulation of neuron projection development; IEA:Ensembl.
GO; GO:0002317; P:plasma cell differentiation; IEA:Ensembl.
GO; GO:0034120; P:positive regulation of erythrocyte aggregation; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; HMP:UniProtKB.
GO; GO:0046598; P:positive regulation of viral entry into host cell; IDA:UniProtKB.
GO; GO:0043687; P:post-translational protein modification; TAS:Reactome.
GO; GO:0042981; P:regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0048678; P:response to axon injury; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0035900; P:response to isolation stress; IEA:Ensembl.
GO; GO:0031295; P:T cell costimulation; IEA:Ensembl.
CDD; cd00070; GLECT; 1.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR001079; Galectin_CRD.
Pfam; PF00337; Gal-bind_lectin; 1.
SMART; SM00908; Gal-bind_lectin; 1.
SMART; SM00276; GLECT; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS51304; GALECTIN; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Apoptosis; Complete proteome;
Direct protein sequencing; Extracellular matrix; Lectin;
Phosphoprotein; Reference proteome; Secreted.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:12665801,
ECO:0000269|PubMed:3065332,
ECO:0000269|Ref.14}.
CHAIN 2 135 Galectin-1.
/FTId=PRO_0000076917.
DOMAIN 4 135 Galectin. {ECO:0000255|PROSITE-
ProRule:PRU00639}.
REGION 45 49 Beta-galactoside binding.
REGION 69 72 Beta-galactoside binding.
BINDING 53 53 Beta-galactoside.
BINDING 62 62 Beta-galactoside.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712}.
MOD_RES 13 13 N6-acetyllysine.
{ECO:0000250|UniProtKB:P16045}.
MOD_RES 29 29 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 30 30 Phosphoserine; by FAM20C.
{ECO:0000269|PubMed:26091039}.
MOD_RES 108 108 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P16045}.
MOD_RES 108 108 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P16045}.
MOD_RES 128 128 N6-acetyllysine.
{ECO:0000250|UniProtKB:P16045}.
STRAND 3 12 {ECO:0000244|PDB:4Q27}.
STRAND 18 24 {ECO:0000244|PDB:4Q27}.
STRAND 30 38 {ECO:0000244|PDB:4Q27}.
STRAND 41 52 {ECO:0000244|PDB:4Q27}.
STRAND 55 65 {ECO:0000244|PDB:4Q27}.
STRAND 73 76 {ECO:0000244|PDB:4Y1U}.
STRAND 84 92 {ECO:0000244|PDB:4Q27}.
STRAND 94 100 {ECO:0000244|PDB:4Q27}.
HELIX 102 104 {ECO:0000244|PDB:4Q27}.
STRAND 106 110 {ECO:0000244|PDB:4Q27}.
STRAND 116 133 {ECO:0000244|PDB:4Q27}.
SEQUENCE 135 AA; 14716 MW; 2FBB8D7A1FC0F1F9 CRC64;
MACGLVASNL NLKPGECLRV RGEVAPDAKS FVLNLGKDSN NLCLHFNPRF NAHGDANTIV
CNSKDGGAWG TEQREAVFPF QPGSVAEVCI TFDQANLTVK LPDGYEFKFP NRLNLEAINY
MAADGDFKIK CVAFD


Related products :

Catalog number Product name Quantity
100-175 Galectin-1 Human Host: E. coli galectin-1; HBL; HPL; gal-1; HLBP14; galaptin; galectin 1; 14 kDa lectin; S-Lac lectin 1; lactose-binding lectin 1; 14 kDa laminin-binding protein; putative MAPK-activat 50
U0497m CLIA 35 kDa lectin,Carbohydrate-binding protein 35,CBP 35,Gal-3,Galactose-specific lectin 3,Galectin-3,IgE-binding protein,L-34 galactoside-binding lectin,Laminin-binding protein,Lectin L-29,Lgals3,Ma 96T
E0497m ELISA 35 kDa lectin,Carbohydrate-binding protein 35,CBP 35,Gal-3,Galactose-specific lectin 3,Galectin-3,IgE-binding protein,L-34 galactoside-binding lectin,Laminin-binding protein,Lectin L-29,Lgals3,M 96T
E0497m ELISA kit 35 kDa lectin,Carbohydrate-binding protein 35,CBP 35,Gal-3,Galactose-specific lectin 3,Galectin-3,IgE-binding protein,L-34 galactoside-binding lectin,Laminin-binding protein,Lectin L-29,Lga 96T
U0497h CLIA 35 kDa lectin,Carbohydrate-binding protein 35,CBP 35,Gal-3,Galactose-specific lectin 3,Galactoside-binding protein,GALBP,Galectin-3,Homo sapiens,Human,IgE-binding protein,L-31,Laminin-binding pro 96T
E0497h ELISA 35 kDa lectin,Carbohydrate-binding protein 35,CBP 35,Gal-3,Galactose-specific lectin 3,Galactoside-binding protein,GALBP,Galectin-3,Homo sapiens,Human,IgE-binding protein,L-31,Laminin-binding pr 96T
100-175 Galectin-1, Host: E. coli, Species: Human, Synonyms: 14 kDa lectin; beta-galactoside-binding lectin L-14-I; beta-galactoside-binding protein 14kDa; GBP, GAL1; LGALS1 50 ug
E0497h ELISA kit 35 kDa lectin,Carbohydrate-binding protein 35,CBP 35,Gal-3,Galactose-specific lectin 3,Galactoside-binding protein,GALBP,Galectin-3,Homo sapiens,Human,IgE-binding protein,L-31,Laminin-bindi 96T
U0497Rb CLIA 35 kDa lectin,Carbohydrate-binding protein 35,CBP 35,Gal-3,Galactose-specific lectin 3,Galectin-3,IgE-binding protein,Laminin-binding protein,Lectin L-29,LGALS3,Mac-2 antigen,Oryctolagus cuniculu 96T
U0497r CLIA 35 kDa lectin,Carbohydrate-binding protein 35,CBP 35,Gal-3,Galactose-specific lectin 3,Galectin-3,IgE-binding protein,Laminin-binding protein,Lectin L-29,Lgals3,Mac-2 antigen,Rat,Rattus norvegicu 96T
E0497Rb ELISA 35 kDa lectin,Carbohydrate-binding protein 35,CBP 35,Gal-3,Galactose-specific lectin 3,Galectin-3,IgE-binding protein,Laminin-binding protein,Lectin L-29,LGALS3,Mac-2 antigen,Oryctolagus cunicul 96T
E0497r ELISA 35 kDa lectin,Carbohydrate-binding protein 35,CBP 35,Gal-3,Galactose-specific lectin 3,Galectin-3,IgE-binding protein,Laminin-binding protein,Lectin L-29,Lgals3,Mac-2 antigen,Rat,Rattus norvegic 96T
E0497r ELISA kit 35 kDa lectin,Carbohydrate-binding protein 35,CBP 35,Gal-3,Galactose-specific lectin 3,Galectin-3,IgE-binding protein,Laminin-binding protein,Lectin L-29,Lgals3,Mac-2 antigen,Rat,Rattus nor 96T
E0497Rb ELISA kit 35 kDa lectin,Carbohydrate-binding protein 35,CBP 35,Gal-3,Galactose-specific lectin 3,Galectin-3,IgE-binding protein,Laminin-binding protein,Lectin L-29,LGALS3,Mac-2 antigen,Oryctolagus cu 96T
U0497c CLIA 35 kDa lectin,Canis familiaris,Canis lupus familiaris,Carbohydrate-binding protein 35,CBP 35,Dog,Gal-3,Galactose-specific lectin 3,Galectin-3,IgE-binding protein,Laminin-binding protein,Lectin L- 96T
E0497c ELISA 35 kDa lectin,Canis familiaris,Canis lupus familiaris,Carbohydrate-binding protein 35,CBP 35,Dog,Gal-3,Galactose-specific lectin 3,Galectin-3,IgE-binding protein,Laminin-binding protein,Lectin L 96T
20-321-175224 GALECTIN-3 - MONOCLONAL ANTIBODY TO HUMAN GALECTIN-3; Galactose-specific lectin 3; Mac-2 antigen; IgE-binding protein; 35 kDa lectin; Carbohydrate-binding protein 35; CBP 35; Laminin-binding protein; 0.1 mg
10-288-22418F Galectin-3-binding protein - Lectin galactoside-binding soluble 3-binding protein; Mac-2-binding protein; Mac-2 BP; MAC2BP; Tumor-associated antigen 90K 0.05 mg
10-288-22418F Galectin-3-binding protein - Lectin galactoside-binding soluble 3-binding protein; Mac-2-binding protein; Mac-2 BP; MAC2BP; Tumor-associated antigen 90K 0.1 mg
201-20-6669 LGALS3BP{lectin, galactoside-binding, soluble, 3 binding protein}mouse.mAb 0.2ml
E91766Hu ELISA Kit for Lectin Galactoside Binding, Soluble 3 Binding Protein (LGALS3BP) 96T/Kit
201-20-6670 LGALS3BP{lectin, galactoside-binding, soluble, 3 binding protein}mouse.mAb 0.2ml
201-20-3099 LGALS3BP{lectin, galactoside-binding, soluble, 3 binding protein}rabbit.pAb 0.2ml
LGALS7 LGALS3BP Gene lectin, galactoside-binding, soluble, 3 binding protein
E-EL-P1689 Porcine LGALS3BP (Lectin Galactoside Binding, Soluble 3 Binding Protein) ELISA Kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur