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

Immunoglobulin lambda variable 1-51 (Ig lambda chain V-I region BL2) (Ig lambda chain V-I region EPS) (Ig lambda chain V-I region NEW) (Ig lambda chain V-I region NIG-64)

 LV151_HUMAN             Reviewed;         117 AA.
P01701; A0A075B6I5; P01702; P06316; P06888;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
07-SEP-2016, sequence version 2.
27-SEP-2017, entry version 99.
RecName: Full=Immunoglobulin lambda variable 1-51 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.7};
AltName: Full=Ig lambda chain V-I region BL2 {ECO:0000305|PubMed:6095199};
AltName: Full=Ig lambda chain V-I region EPS {ECO:0000305|PubMed:3929803};
AltName: Full=Ig lambda chain V-I region NEW {ECO:0000305|PubMed:4177823};
AltName: Full=Ig lambda chain V-I region NIG-64 {ECO:0000305|PubMed:6404900};
Flags: Precursor;
Name=IGLV1-51 {ECO:0000303|PubMed:11872955, ECO:0000303|Ref.7};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=6095199; DOI=10.1093/nar/12.22.8407;
Tsujimoto Y., Croce C.M.;
"Molecular cloning of a human immunoglobulin lambda chain variable
sequence.";
Nucleic Acids Res. 12:8407-8414(1984).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (IMGT ALLELE
IGLV1-51*01).
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).
[3]
PROTEIN SEQUENCE OF 20-117, AND PYROGLUTAMATE FORMATION AT GLN-20.
PubMed=4177823;
Langer B., Steinmetz-Kayne M., Hilschmann N.;
"The complete amino acid sequence of Bence Jones protein New (lambda-
type). Subgroups in the variable part of immunoglobulin L-chains of
the lambda-type.";
Hoppe-Seyler's Z. Physiol. Chem. 349:945-951(1968).
[4]
PROTEIN SEQUENCE OF 20-117, AND PYROGLUTAMATE FORMATION AT GLN-20.
PubMed=6404900;
Kametani F., Takayasu T., Suzuki S., Shinoda T., Okuyama T.,
Shimizu A.;
"Comparative studies on the structure of the light chains of human
immunoglobulins. IV. Assignment of a subsubgroup.";
J. Biochem. 93:421-429(1983).
[5]
PROTEIN SEQUENCE OF 20-117.
PubMed=3929803;
Toft K.G., Sletten K., Husby G.;
"The amino-acid sequence of the variable region of a carbohydrate-
containing amyloid fibril protein EPS (immunoglobulin light chain,
type lambda).";
Biol. Chem. Hoppe-Seyler 366:617-625(1985).
[6]
NOMEMCLATURE.
PubMed=11872955;
Lefranc M.P.;
"Nomenclature of the human immunoglobulin lambda (IGL) genes.";
Exp. Clin. Immunogenet. 18:242-254(2001).
[7]
NOMENCLATURE.
Lefranc M.P., Lefranc G.;
"The Immunoglobulin FactsBook.";
(In) Lefranc M.P., Lefranc G. (eds.);
The Immunoglobulin FactsBook., pp.1-458, Academic Press, London.
(2001).
[8]
REVIEW ON SOMATIC HYPERMUTATION.
PubMed=17576170; DOI=10.1146/annurev.genet.41.110306.130340;
Teng G., Papavasiliou F.N.;
"Immunoglobulin somatic hypermutation.";
Annu. Rev. Genet. 41:107-120(2007).
[9]
REVIEW ON IMMUNOGLOBULINS.
PubMed=20176268; DOI=10.1016/j.jaci.2009.09.046;
Schroeder H.W. Jr., Cavacini L.;
"Structure and function of immunoglobulins.";
J. Allergy Clin. Immunol. 125:S41-S52(2010).
[10]
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).
[11]
REVIEW ON FUNCTION.
PubMed=22158414; DOI=10.1038/nri3128;
McHeyzer-Williams M., Okitsu S., Wang N., McHeyzer-Williams L.;
"Molecular programming of B cell memory.";
Nat. Rev. Immunol. 12:24-34(2012).
[12]
NOMENCLATURE.
PubMed=24600447; DOI=10.3389/fimmu.2014.00022;
Lefranc M.P.;
"Immunoglobulin and T Cell Receptor Genes: IMGT((R)) and the Birth and
Rise of Immunoinformatics.";
Front. Immunol. 5:22-22(2014).
-!- FUNCTION: V region of the variable domain of immunoglobulin light
chains that participates in the antigen recognition
(PubMed:24600447). Immunoglobulins, also known as antibodies, are
membrane-bound or secreted glycoproteins produced by B
lymphocytes. In the recognition phase of humoral immunity, the
membrane-bound immunoglobulins serve as receptors which, upon
binding of a specific antigen, trigger the clonal expansion and
differentiation of B lymphocytes into immunoglobulins-secreting
plasma cells. Secreted immunoglobulins mediate the effector phase
of humoral immunity, which results in the elimination of bound
antigens (PubMed:20176268, PubMed:22158414). The antigen binding
site is formed by the variable domain of one heavy chain, together
with that of its associated light chain. Thus, each immunoglobulin
has two antigen binding sites with remarkable affinity for a
particular antigen. The variable domains are assembled by a
process called V-(D)-J rearrangement and can then be subjected to
somatic hypermutations which, after exposure to antigen and
selection, allow affinity maturation for a particular antigen
(PubMed:17576170, PubMed:20176268). {ECO:0000303|PubMed:17576170,
ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414,
ECO:0000303|PubMed:24600447}.
-!- SUBUNIT: Immunoglobulins are composed of two identical heavy
chains and two identical light chains; disulfide-linked.
{ECO:0000303|PubMed:20176268}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000303|PubMed:20176268,
ECO:0000303|PubMed:22158414}. Cell membrane
{ECO:0000303|PubMed:20176268, ECO:0000303|PubMed:22158414}.
-!- POLYMORPHISM: There are several alleles. The sequence shown is
that of IMGT allele IGLV1-51*01.
-!- CAUTION: For an example of a full-length immunoglobulin lambda
light chain see AC P0DOX8. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAA25598.1; Type=Miscellaneous discrepancy; Note=Chimeric mRNA corresponding to regions V and J of immunoglobulin kappa light chain.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X01147; CAA25598.1; ALT_SEQ; mRNA.
EMBL; AC245060; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; A01964; L1HUNW.
PIR; A01965; L1HUNG.
PIR; A01966; L1HUBL.
PIR; A24656; L1HUEP.
ProteinModelPortal; P01701; -.
SMR; P01701; -.
IMGT_GENE-DB; IGLV1-51; -.
DMDM; 126541; -.
DMDM; 126543; -.
DMDM; 126548; -.
DMDM; 126550; -.
EPD; P01701; -.
PeptideAtlas; P01701; -.
PRIDE; P01701; -.
Ensembl; ENST00000390290; ENSP00000374825; ENSG00000211644.
UCSC; uc062cbm.1; human.
EuPathDB; HostDB:ENSG00000211644.2; -.
GeneCards; IGLV1-51; -.
HGNC; HGNC:5882; IGLV1-51.
neXtProt; NX_P01701; -.
OpenTargets; ENSG00000211644; -.
GeneTree; ENSGT00780000121842; -.
HOVERGEN; HBG018013; -.
Reactome; R-HSA-166663; Initial triggering of complement.
Reactome; R-HSA-173623; Classical antibody-mediated complement activation.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-202733; Cell surface interactions at the vascular wall.
Reactome; R-HSA-2029481; FCGR activation.
Reactome; R-HSA-2029482; Regulation of actin dynamics for phagocytic cup formation.
Reactome; R-HSA-2029485; Role of phospholipids in phagocytosis.
Reactome; R-HSA-2168880; Scavenging of heme from plasma.
Reactome; R-HSA-2454202; Fc epsilon receptor (FCERI) signaling.
Reactome; R-HSA-2730905; Role of LAT2/NTAL/LAB on calcium mobilization.
Reactome; R-HSA-2871796; FCERI mediated MAPK activation.
Reactome; R-HSA-2871809; FCERI mediated Ca+2 mobilization.
Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
Reactome; R-HSA-5690714; CD22 mediated BCR regulation.
Reactome; R-HSA-977606; Regulation of Complement cascade.
Reactome; R-HSA-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
PRO; PR:P01701; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000211644; -.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0003823; F:antigen binding; NAS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0006956; P:complement activation; TAS:Reactome.
GO; GO:0006958; P:complement activation, classical pathway; TAS:Reactome.
GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; TAS:Reactome.
GO; GO:0006955; P:immune response; NAS:UniProtKB.
GO; GO:0050900; P:leukocyte migration; TAS:Reactome.
GO; GO:0006898; P:receptor-mediated endocytosis; TAS:Reactome.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SMART; SM00406; IGv; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing;
Disulfide bond; Immunoglobulin domain; Immunoglobulin V region;
Membrane; Polymorphism; Pyrrolidone carboxylic acid;
Reference proteome; Secreted; Signal.
SIGNAL 1 19 {ECO:0000269|PubMed:3929803,
ECO:0000269|PubMed:4177823,
ECO:0000269|PubMed:6404900}.
CHAIN 20 117 Immunoglobulin lambda variable 1-51.
{ECO:0000269|PubMed:3929803,
ECO:0000269|PubMed:4177823,
ECO:0000269|PubMed:6404900}.
/FTId=PRO_0000059824.
DOMAIN 20 >117 Ig-like. {ECO:0000255|PROSITE-
ProRule:PRU00114}.
MOD_RES 20 20 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:4177823,
ECO:0000269|PubMed:6404900}.
DISULFID 41 108 {ECO:0000255|PROSITE-ProRule:PRU00114}.
CONFLICT 29 29 V -> L (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 36 38 KVT -> RVS (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 36 36 K -> E (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 44 46 SSS -> GST (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 50 54 NNYVS -> KNYVD (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 50 52 NNY -> DNF (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 51 51 N -> D (in Ref. 1; CAA25598).
{ECO:0000305}.
CONFLICT 56 58 YQQ -> HQH (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 59 59 L -> V (in Ref. 1; CAA25598).
{ECO:0000305}.
CONFLICT 69 70 YD -> FN (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 70 71 DN -> ED (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 82 84 FSG -> ISA (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 99 99 Q -> R (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 105 105 D -> I (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 109 109 G -> A (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 112 117 DSSLSA -> NNSLSG (in Ref. 1; CAA25598).
{ECO:0000305}.
CONFLICT 113 117 SSLSA -> NRRSV (in Ref. 5; AA sequence).
{ECO:0000305}.
CONFLICT 116 116 S -> N (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 117 117 A -> V (in Ref. 4; AA sequence).
{ECO:0000305}.
NON_TER 117 117
SEQUENCE 117 AA; 12249 MW; 46700D34C2882B7F CRC64;
MTCSPLLLTL LIHCTGSWAQ SVLTQPPSVS AAPGQKVTIS CSGSSSNIGN NYVSWYQQLP
GTAPKLLIYD NNKRPSGIPD RFSGSKSGTS ATLGITGLQT GDEADYYCGT WDSSLSA


Related products :

Catalog number Product name Quantity
E0119p Human ELISA Kit FOR Ig lambda-7 chain C region 96T
GATA_HUMAN Human ELISA Kit FOR Ig lambda-7 chain C region 96T
ZN384_HUMAN Human ELISA Kit FOR Ig lambda-7 chain C region 96T
CSB-EL011458HU Human Ig lambda-7 chain C region(IGLC7) ELISA kit 96T
CSB-EL011457HU Human Ig lambda-6 chain C region(IGLC6) ELISA kit 96T
orb81941 Human Anti-Human (lambda chain) (L) antibody Lambda Light Chain is a purified human immunoglobulin. 1 mg
CSB-EL011458HU Human Ig lambda-7 chain C region(IGLC7) ELISA kit SpeciesHuman 96T
CSB-EL011457HU Human Ig lambda-6 chain C region(IGLC6) ELISA kit SpeciesHuman 96T
orb82193 Human Anti-Human IgE ((kappa chain) chain) and (lambda chain) antibody IgE, kappa and lambda is a purified human immunoglobulin. 100
1107NF-V7076 Monoclonal Antibodies: Human Ig lambda-chain; reactive species: Human; Clone: B468; Isotype: IgG1; Specificity: Human Ig lambda-chain 0.5/ml
RANT-203B Ig Lambda Mouse Anti Human Ig Lambda Light Chain 1mg
RANT-203A Ig Lambda Mouse Anti Human Ig Lambda Light Chain 500µg
orb81198 Human Lambda Light Chain protein Human Lambda light chain produced in Pooled Bence Jones urine having a molecular mass of 23 kDa. For research use only. 200
AM08021AP-N Mouse Lambda (lambda light chain specific) 1.0 ml
AM08021RP-S Mouse Lambda (lambda light chain specific) 0.1 mg
ant-203 Mouse Anti Human Ig Lambda Light Chain Ig Lambda 1mg
AM08021AP-N Mouse Lambda (lambda light chain specific) 1.0 ml
ant-203 Mouse Anti Human Ig Lambda Light Chain Ig Lambda 500
AM08021BT-N Mouse Lambda (lambda light chain specific) 0.5 mg
AM08021FC-N Mouse Lambda (lambda light chain specific) 0.5 mg
AM08021HR-N Mouse Lambda (lambda light chain specific) 1.0 ml
AM08021PU-N Mouse Lambda (lambda light chain specific) 0.5 mg
AM08021RP-N Mouse Lambda (lambda light chain specific) 0.2 mg
AM08021FC-N Mouse Lambda (lambda light chain specific) 0.5 mg
AM08021RP-N Mouse Lambda (lambda light chain specific) 0.2 mg


 

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