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

Insulin [Cleaved into: Insulin B chain; Insulin A chain]

 INS_PIG                 Reviewed;         108 AA.
P01315; Q9TSJ5;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
27-SEP-2017, entry version 153.
RecName: Full=Insulin;
Contains:
RecName: Full=Insulin B chain;
Contains:
RecName: Full=Insulin A chain;
Flags: Precursor;
Name=INS;
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE.
Han X.G., Tuch B.E.;
"Complete porcine preproinsulin cDNA sequence.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Large white;
PubMed=12140686; DOI=10.1007/s00335-001-3059-x;
Amarger V., Nguyen M., Van Laere A.-S., Braunschweig M., Nezer C.,
Georges M., Andersson L.;
"Comparative sequence analysis of the INS-IGF2-H19 gene cluster in
pigs.";
Mamm. Genome 13:388-398(2002).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=European wild boar, Hampshire, Japanese wild boar, Landrace,
Large white, Meishan, and Pietrain;
PubMed=14574411; DOI=10.1038/nature02064;
Van Laere A.-S., Nguyen M., Braunschweig M., Nezer C., Collette C.,
Moreau L., Archibald A.L., Haley C., Buys N., Tally M., Andersson G.,
Georges M., Andersson L.;
"A regulatory mutation in IGF2 causes a major QTL effect on muscle
growth in the pig.";
Nature 425:832-836(2003).
[4]
PROTEIN SEQUENCE OF 25-108.
PubMed=5657063; DOI=10.1126/science.161.3837.165;
Chance R.E., Ellis R.M., Bromer W.W.;
"Porcine proinsulin: characterization and amino acid sequence.";
Science 161:165-167(1968).
[5]
SEQUENCE REVISION TO 59.
Chance R.E.;
Submitted (JUL-1970) to the PIR data bank.
[6]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Blundell T.L., Dodson G.G., Hodgkin D., Mercola D.;
"Insulin. The structure in the crystal and its reflection in chemistry
and biology.";
Adv. Protein Chem. 26:279-402(1972).
[7]
X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS) OF 88-108 AND 25-54, AND
DISULFIDE BONDS.
Isaacs N.W., Agarwal R.C.;
"Experience with fast Fourier least squares in the refinement of the
crystal structure of rhombohedral 2-zinc insulin at 1.5-A
resolution.";
Acta Crystallogr. A 34:782-791(1978).
[8]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS).
PubMed=2905485; DOI=10.1098/rstb.1988.0058;
Baker E.N., Blundell T.L., Cutfield J.F., Cutfield S.M., Dodson E.J.,
Dodson G.G., Crowfoot Hodgkin D.M., Hubbard R.E., Isaacs N.W.,
Reynolds C.D., Sakabe K., Sakabe N., Vijayan N.M.;
"The structure of 2Zn pig insulin crystals at 1.5-A resolution.";
Philos. Trans. R. Soc. Lond., B, Biol. Sci. 319:369-456(1988).
[9]
X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 88-108 AND 25-54, AND
DISULFIDE BONDS.
PubMed=1772633; DOI=10.1107/S010876819100842X;
Balschmidt P., Hansen F.B., Dodson E., Dodson G., Korber F.;
"Structure of porcine insulin cocrystallized with clupeine Z.";
Acta Crystallogr. B 47:975-986(1991).
[10]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
PubMed=2025410; DOI=10.1107/S0108768190009570;
Badger J., Harris M.R., Reynolds C.D., Evans A.C., Dodson E.J.,
Dodson G.G., North A.C.T.;
"Structure of the pig insulin dimer in the cubic crystal.";
Acta Crystallogr. B 47:127-136(1991).
[11]
X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 88-108 AND 27-49, AND
DISULFIDE BONDS.
PubMed=15299880; DOI=10.1107/S0907444997004034;
Diao J.-S., Wan Z.-L., Chang W.-R., Liang D.-C.;
"Structure of monomeric porcine DesB1-B2 despentapeptide (B26-B30)
insulin at 1.65-A resolution.";
Acta Crystallogr. D 53:507-512(1997).
-!- FUNCTION: Insulin decreases blood glucose concentration. It
increases cell permeability to monosaccharides, amino acids and
fatty acids. It accelerates glycolysis, the pentose phosphate
cycle, and glycogen synthesis in liver.
-!- SUBUNIT: Heterodimer of a B chain and an A chain linked by two
disulfide bonds. {ECO:0000250|UniProtKB:P01308}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-8437944, EBI-8437944;
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the insulin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC77920.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Protein of the 20th
century - Issue 9 of April 2001;
URL="http://web.expasy.org/spotlight/back_issues/009";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF064555; AAC77920.1; ALT_INIT; mRNA.
EMBL; AY044828; AAL69550.1; -; Genomic_DNA.
EMBL; AY242098; AAQ00952.1; -; Genomic_DNA.
EMBL; AY242099; AAQ00954.1; -; Genomic_DNA.
EMBL; AY242100; AAQ00957.1; -; Genomic_DNA.
EMBL; AY242101; AAQ00960.1; -; Genomic_DNA.
EMBL; AY242102; AAQ00963.1; -; Genomic_DNA.
EMBL; AY242103; AAQ00966.1; -; Genomic_DNA.
EMBL; AY242104; AAQ00969.1; -; Genomic_DNA.
EMBL; AY242105; AAQ00972.1; -; Genomic_DNA.
EMBL; AY242106; AAQ00975.1; -; Genomic_DNA.
EMBL; AY242107; AAQ00978.1; -; Genomic_DNA.
EMBL; AY242108; AAQ00981.1; -; Genomic_DNA.
EMBL; AY242109; AAQ00983.1; -; Genomic_DNA.
EMBL; AY242110; AAQ00985.1; -; Genomic_DNA.
EMBL; AY242111; AAQ00987.1; -; Genomic_DNA.
EMBL; AY242112; AAQ00990.1; -; Genomic_DNA.
PIR; A01583; IPPG.
RefSeq; NP_001103242.1; NM_001109772.1.
UniGene; Ssc.583; -.
PDB; 1B17; X-ray; 1.70 A; A=88-108, B=25-54.
PDB; 1B18; X-ray; 1.80 A; A=88-108, B=25-54.
PDB; 1B19; X-ray; 1.80 A; A=88-108, B=25-54.
PDB; 1B2A; X-ray; 1.70 A; A=88-108, B=25-54.
PDB; 1B2B; X-ray; 1.80 A; A=88-108, B=25-54.
PDB; 1B2C; X-ray; 1.80 A; A=88-108, B=25-54.
PDB; 1B2D; X-ray; 1.70 A; A=88-108, B=25-54.
PDB; 1B2E; X-ray; 1.90 A; A=88-108, B=25-54.
PDB; 1B2F; X-ray; 1.90 A; A=88-108, B=25-54.
PDB; 1B2G; X-ray; 1.80 A; A=88-108, B=25-54.
PDB; 1DEI; X-ray; 1.60 A; A/C=88-108, B/D=25-47.
PDB; 1IZA; X-ray; 2.50 A; A/C=88-108, B/D=25-53.
PDB; 1IZB; X-ray; 2.00 A; A/C=88-108, B/D=25-53.
PDB; 1M5A; X-ray; 1.20 A; A/C=88-108, B/D=25-54.
PDB; 1MPJ; X-ray; 2.30 A; A/C=88-108, B/D=25-54.
PDB; 1SDB; X-ray; 1.65 A; A=88-108, B=27-49.
PDB; 1WAV; X-ray; 2.50 A; A/C/E/G/I/K=88-108, B/D/F/H/J/L=25-54.
PDB; 1ZEI; X-ray; 1.90 A; A/B/C/D/E/F=25-54, A/B/C/D/E/F=88-108.
PDB; 1ZNI; X-ray; 1.50 A; A/C=88-108, B/D=25-54.
PDB; 2EFA; Neutron; 2.70 A; A=88-108, B=25-54.
PDB; 2G4M; X-ray; 1.80 A; A=88-108, B=25-54.
PDB; 2TCI; X-ray; 1.80 A; A/C=88-108, B/D=25-54.
PDB; 2ZPP; Neutron; 2.50 A; A=88-108, B=25-54.
PDB; 3FHP; Neutron; 2.00 A; A/C=88-108, B/D=25-54.
PDB; 3GKY; X-ray; 1.80 A; A/C=88-108, B/D=25-54.
PDB; 3INS; X-ray; 1.50 A; A/C=88-108, B/D=25-54.
PDB; 3MTH; X-ray; 1.90 A; A/C=88-108, B/D=25-54.
PDB; 3RTO; X-ray; 1.80 A; A/C=88-108, B/D=25-54.
PDB; 3T2A; X-ray; 2.10 A; A=88-108, B=25-54.
PDB; 4A7E; X-ray; 1.86 A; A=88-108, B=25-54.
PDB; 4INS; X-ray; 1.50 A; A/C=88-108, B/D=25-54.
PDB; 5D52; X-ray; 1.80 A; A=88-108, B=25-54.
PDB; 5D53; X-ray; 1.50 A; A=88-108, B=25-54.
PDB; 5D54; X-ray; 1.50 A; A=88-108, B=25-54.
PDB; 5D5E; X-ray; 2.41 A; A=88-108, B=25-54.
PDB; 5FB6; X-ray; 1.90 A; A=88-108, B=25-54.
PDB; 5LIS; X-ray; 2.29 A; A=88-108, B=25-54.
PDB; 6INS; X-ray; 2.00 A; E/F=25-108.
PDB; 7INS; X-ray; 2.00 A; A/C/E=88-108, B/D/F=25-54.
PDB; 9INS; X-ray; 1.70 A; A=88-108, B=25-54.
PDBsum; 1B17; -.
PDBsum; 1B18; -.
PDBsum; 1B19; -.
PDBsum; 1B2A; -.
PDBsum; 1B2B; -.
PDBsum; 1B2C; -.
PDBsum; 1B2D; -.
PDBsum; 1B2E; -.
PDBsum; 1B2F; -.
PDBsum; 1B2G; -.
PDBsum; 1DEI; -.
PDBsum; 1IZA; -.
PDBsum; 1IZB; -.
PDBsum; 1M5A; -.
PDBsum; 1MPJ; -.
PDBsum; 1SDB; -.
PDBsum; 1WAV; -.
PDBsum; 1ZEI; -.
PDBsum; 1ZNI; -.
PDBsum; 2EFA; -.
PDBsum; 2G4M; -.
PDBsum; 2TCI; -.
PDBsum; 2ZPP; -.
PDBsum; 3FHP; -.
PDBsum; 3GKY; -.
PDBsum; 3INS; -.
PDBsum; 3MTH; -.
PDBsum; 3RTO; -.
PDBsum; 3T2A; -.
PDBsum; 4A7E; -.
PDBsum; 4INS; -.
PDBsum; 5D52; -.
PDBsum; 5D53; -.
PDBsum; 5D54; -.
PDBsum; 5D5E; -.
PDBsum; 5FB6; -.
PDBsum; 5LIS; -.
PDBsum; 6INS; -.
PDBsum; 7INS; -.
PDBsum; 9INS; -.
ProteinModelPortal; P01315; -.
SMR; P01315; -.
IntAct; P01315; 1.
MINT; MINT-1505666; -.
STRING; 9823.ENSSSCP00000025428; -.
Allergome; 2122; Sus s Insulin.
PaxDb; P01315; -.
GeneID; 397415; -.
KEGG; ssc:397415; -.
CTD; 3630; -.
eggNOG; ENOG410J0XC; Eukaryota.
eggNOG; ENOG4111VJB; LUCA.
HOVERGEN; HBG006137; -.
InParanoid; P01315; -.
KO; K04526; -.
EvolutionaryTrace; P01315; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0005615; C:extracellular space; ISS:AgBase.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005179; F:hormone activity; IMP:AgBase.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005158; F:insulin receptor binding; IEA:Ensembl.
GO; GO:0005159; F:insulin-like growth factor receptor binding; IMP:AgBase.
GO; GO:0002020; F:protease binding; IEA:Ensembl.
GO; GO:0032148; P:activation of protein kinase B activity; IEA:Ensembl.
GO; GO:0006953; P:acute-phase response; IEA:Ensembl.
GO; GO:0046631; P:alpha-beta T cell activation; IEA:Ensembl.
GO; GO:0055089; P:fatty acid homeostasis; IEA:Ensembl.
GO; GO:0007186; P:G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0042593; P:glucose homeostasis; IEA:Ensembl.
GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
GO; GO:0015758; P:glucose transport; IEA:Ensembl.
GO; GO:0009101; P:glycoprotein biosynthetic process; IMP:AgBase.
GO; GO:0008286; P:insulin receptor signaling pathway; IEA:Ensembl.
GO; GO:0019249; P:lactate biosynthetic process; IMP:AgBase.
GO; GO:0008610; P:lipid biosynthetic process; IMP:AgBase.
GO; GO:0042158; P:lipoprotein biosynthetic process; IMP:AgBase.
GO; GO:0000165; P:MAPK cascade; IEA:Ensembl.
GO; GO:0002674; P:negative regulation of acute inflammatory response; IEA:Ensembl.
GO; GO:0045922; P:negative regulation of fatty acid metabolic process; IEA:Ensembl.
GO; GO:2000252; P:negative regulation of feeding behavior; IEA:Ensembl.
GO; GO:0045721; P:negative regulation of gluconeogenesis; IMP:AgBase.
GO; GO:0045818; P:negative regulation of glycogen catabolic process; IEA:Ensembl.
GO; GO:0050995; P:negative regulation of lipid catabolic process; IEA:Ensembl.
GO; GO:0033861; P:negative regulation of NAD(P)H oxidase activity; IEA:Ensembl.
GO; GO:0042177; P:negative regulation of protein catabolic process; IEA:Ensembl.
GO; GO:0032460; P:negative regulation of protein oligomerization; IEA:Ensembl.
GO; GO:0050709; P:negative regulation of protein secretion; IEA:Ensembl.
GO; GO:0045861; P:negative regulation of proteolysis; IEA:Ensembl.
GO; GO:1903427; P:negative regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
GO; GO:0060266; P:negative regulation of respiratory burst involved in inflammatory response; IEA:Ensembl.
GO; GO:1990535; P:neuron projection maintenance; IEA:Ensembl.
GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
GO; GO:0008284; P:positive regulation of cell proliferation; IEA:Ensembl.
GO; GO:0050715; P:positive regulation of cytokine secretion; IEA:Ensembl.
GO; GO:1902952; P:positive regulation of dendritic spine maintenance; IEA:Ensembl.
GO; GO:0045740; P:positive regulation of DNA replication; IDA:BHF-UCL.
GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
GO; GO:0046326; P:positive regulation of glucose import; IEA:Ensembl.
GO; GO:0045725; P:positive regulation of glycogen biosynthetic process; IEA:Ensembl.
GO; GO:0045821; P:positive regulation of glycolytic process; IEA:Ensembl.
GO; GO:0046628; P:positive regulation of insulin receptor signaling pathway; IDA:BHF-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; IEA:Ensembl.
GO; GO:0045840; P:positive regulation of mitotic nuclear division; IEA:Ensembl.
GO; GO:0051092; P:positive regulation of NF-kappaB transcription factor activity; IEA:Ensembl.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IDA:BHF-UCL.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; IEA:Ensembl.
GO; GO:0031954; P:positive regulation of protein autophosphorylation; IDA:BHF-UCL.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:1900182; P:positive regulation of protein localization to nucleus; IEA:Ensembl.
GO; GO:0060267; P:positive regulation of respiratory burst; IEA:Ensembl.
GO; GO:0006521; P:regulation of cellular amino acid metabolic process; IEA:Ensembl.
GO; GO:1903076; P:regulation of protein localization to plasma membrane; IEA:Ensembl.
GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
GO; GO:1903576; P:response to L-arginine; ISS:AgBase.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 1.10.100.10; -; 1.
InterPro; IPR004825; Insulin.
InterPro; IPR016179; Insulin-like.
InterPro; IPR022353; Insulin_CS.
InterPro; IPR022352; Insulin_family.
Pfam; PF00049; Insulin; 1.
PRINTS; PR00277; INSULIN.
PRINTS; PR00276; INSULINFAMLY.
SMART; SM00078; IlGF; 1.
SUPFAM; SSF56994; SSF56994; 1.
PROSITE; PS00262; INSULIN; 1.
1: Evidence at protein level;
3D-structure; Carbohydrate metabolism;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disulfide bond; Glucose metabolism;
Hormone; Reference proteome; Secreted; Signal.
SIGNAL 1 24 {ECO:0000269|PubMed:5657063}.
PEPTIDE 25 54 Insulin B chain.
/FTId=PRO_0000015879.
PROPEP 57 85 C peptide.
/FTId=PRO_0000015880.
PEPTIDE 88 108 Insulin A chain.
/FTId=PRO_0000015881.
DISULFID 31 94 Interchain (between B and A chains).
{ECO:0000244|PDB:1SDB,
ECO:0000244|PDB:4INS,
ECO:0000244|PDB:7INS,
ECO:0000269|PubMed:15299880,
ECO:0000269|PubMed:1772633,
ECO:0000269|PubMed:2905485}.
DISULFID 43 107 Interchain (between B and A chains).
{ECO:0000244|PDB:1SDB,
ECO:0000244|PDB:4INS,
ECO:0000244|PDB:7INS,
ECO:0000269|PubMed:15299880,
ECO:0000269|PubMed:1772633,
ECO:0000269|PubMed:2905485}.
DISULFID 93 98 {ECO:0000244|PDB:1SDB,
ECO:0000244|PDB:4INS,
ECO:0000244|PDB:7INS,
ECO:0000269|PubMed:15299880,
ECO:0000269|PubMed:1772633,
ECO:0000269|PubMed:2905485}.
HELIX 33 43 {ECO:0000244|PDB:1M5A}.
HELIX 44 46 {ECO:0000244|PDB:1M5A}.
STRAND 48 50 {ECO:0000244|PDB:1M5A}.
HELIX 89 95 {ECO:0000244|PDB:1M5A}.
HELIX 100 103 {ECO:0000244|PDB:1M5A}.
HELIX 104 106 {ECO:0000244|PDB:1M5A}.
SEQUENCE 108 AA; 11672 MW; CB4491B429858EBE CRC64;
MALWTRLLPL LALLALWAPA PAQAFVNQHL CGSHLVEALY LVCGERGFFY TPKARREAEN
PQAGAVELGG GLGGLQALAL EGPPQKRGIV EQCCTSICSL YQLENYCN


Related products :

Catalog number Product name Quantity
orb80481 Human Insulin protein Insulin Human Recombinant produced in E.coli is two chain, non-glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5807 Dalton. Insulin is pur 25 mg
orb80483 Porcine Insulin protein Insulin Porcine is two chain, glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5777 Dalton. The and chains are joined by two interchain d 25 mg
orb80482 Human Insulin Yeast protein Insulin Human Recombinant produced in Yeast is two chain, glycosylated polypeptide chain containing 51 amino acids and having a molecular mass of 5807 Dalton. Zinc content 2 mg
630-01461 Insulin ELISA, Porcine Porcine Insulin ELISA Kit to quantify Insulin using a sandwich enzyme immunoassay. In less than 4 hours, the Porcine Insulin ELISA Kit measures insulin quantities in as little 96tests
SCH-5329-4102 SYNTHETIC HUMAN INSULIN B CHAIN, Product Type Purified Protein, Specificity INSULIN, Target Species Human, Host N_A, Format Purified, Isotypes , Applications E, Clone 5 mg
5329-4102 SYNTHETIC HUMAN INSULIN B CHAIN, Product Type Purified Protein, Specificity INSULIN, Target Species Human, Host N_A, Format Purified, Isotypes , Applications E, Clone 5 mg
637-07113 Insulin Standard Solution, Rabbit (10ng_ml) Insulin is a hormone that is central to regulating carbohydrate and fat metabolism in the body. Insulin causes cells in the liver, muscle, and fat tissue t 5X500UL
630-07103 Insulin Standard Solution, Humster (10ng_ml) Insulin is a hormone that is central to regulating carbohydrate and fat metabolism in the body. Insulin causes cells in the liver, muscle, and fat tissue 5X500UL
637-01471 Insulin (T_type) ELISA, Rat Rat Insulin ELISA Kit is a reagent kit for quantitation of Insulin by sandwich  technique of enzyme immunoassay.   96tests
orb21787 Guinea Pig IgG Against Swine Insulin Polyclonal Purified IgG fraction of polyclonal guinea pig antiserum to swine insulin. Insulin is a hormone produced by the beta cells of the islets of Langerhans i 10 mg
orb21788 Guinea Pig IgG Against Swine Insulin Polyclonal Fluorescein isothiocyanate-conjugated IgG fraction of polyclonal guinea pig antiserum to swine insulin. Insulin is a hormone produced by the beta cells 1 ml
2I1-C7C9 Insulin (beta chain) 1 mg
KP1016 Insulin β Chain Peptide (15 - 23) 1 mg
RP20501 Insulin alpha-chain (1-13) 1,0mg
BMA1025 Insulin B chain, Monoclonal antibody 100 μg
RP21067 Insulin beta Chain Peptide (15-23)
10-783-79566 SYNTHETIC HUMAN INSULIN B CHAIN - 5 mg
SP2656a Insulin-like 6 (INSL 6) _ RIF-1 B-Chain, human
BMA1025 Insulin B chain Monoclonal Antibodie 100 μg
BPA1067 Insulin (B chain) Polyclonal Antibodie 100 μg
Y103558 Insulin (human) beta chain 1 mg
SP2656b Insulin-like 6 (INSL 6) _ RIF-1 B-Chain, human
ABS2556 SYNTHETIC HUMAN INSULIN B CHAIN 5 mg
SP2656a Insulin-like 6 (INSL 6) _ RIF-1 B-Chain, human 0.1 mg
SP2656b Insulin-like 6 (INSL 6) _ RIF-1 B-Chain, human 0.5 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