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Interleukin-2 (IL-2) (T-cell growth factor) (TCGF) (Aldesleukin)

 IL2_HUMAN               Reviewed;         153 AA.
P60568; P01585;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
27-SEP-2017, entry version 157.
RecName: Full=Interleukin-2;
Short=IL-2;
AltName: Full=T-cell growth factor;
Short=TCGF;
AltName: INN=Aldesleukin;
Flags: Precursor;
Name=IL2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6312994; DOI=10.1016/S0006-291X(83)80040-0;
Maeda S., Nishino N., Obaru K., Mita S., Nomiyama H., Shimada K.,
Fujimoto K., Teranishi T., Hirano T., Onoue K.;
"Cloning of interleukin 2 mRNAs from human tonsils.";
Biochem. Biophys. Res. Commun. 115:1040-1047(1983).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
PubMed=6403867; DOI=10.1038/302305a0;
Taniguchi T., Matsui H., Fujita T., Takaoka C., Kashima N.,
Yoshimoto R., Hamuro J.;
"Structure and expression of a cloned cDNA for human interleukin-2.";
Nature 302:305-310(1983).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6306584; DOI=10.1093/nar/11.13.4307;
Devos R., Plaetinck G., Cheroutre H., Simons G., Degrave W.,
Tavernier J., Remaut E., Fiers W.;
"Molecular cloning of human interleukin 2 cDNA and its expression in
E. coli.";
Nucleic Acids Res. 11:4307-4323(1983).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6324170; DOI=10.1073/pnas.80.24.7437;
Fujita T., Takaoka C., Matsui H., Taniguchi T.;
"Structure of the human interleukin 2 gene.";
Proc. Natl. Acad. Sci. U.S.A. 80:7437-7441(1983).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6330695; DOI=10.1093/nar/12.12.5005;
Holbrook N.J., Lieber M., Crabtree G.R.;
"DNA sequence of the 5' flanking region of the human interleukin 2
gene: homologies with adult T-cell leukemia virus.";
Nucleic Acids Res. 12:5005-5013(1984).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6608729; DOI=10.1073/pnas.81.6.1634;
Holbrook N.J., Smith K.A., Fornace A.J. Jr., Comeau C.M.,
Wiskocil R.L., Crabtree G.R.;
"T-cell growth factor: complete nucleotide sequence and organization
of the gene in normal and malignant cells.";
Proc. Natl. Acad. Sci. U.S.A. 81:1634-1638(1984).
[7]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7722480;
Eizenberg O., Faber-Elman A., Lotan M., Schwartz M.;
"Interleukin-2 transcripts in human and rodent brains: possible
expression by astrocytes.";
J. Neurochem. 64:1928-1936(1995).
[8]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Placenta;
PubMed=8824916;
DOI=10.1002/(SICI)1098-2795(199602)43:2<180::AID-MRD7>3.0.CO;2-N;
Chernicky C.L., Tan H., Burfeind P., Ilan J., Ilan J.;
"Sequence of interleukin-2 isolated from human placental poly A+ RNA:
possible role in maintenance of fetal allograft.";
Mol. Reprod. Dev. 43:180-186(1996).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
SeattleSNPs variation discovery resource;
Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Blood;
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).
[11]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-68.
Nishino N., Obaru K., Maeda S., Shimada K., Onoue K.;
"Organization of the DNA regions flanking the human interleukin 2
gene.";
Biomed. Res. 6:197-205(1985).
[12]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-69.
PubMed=3491296; DOI=10.1128/MCB.6.9.3042;
Siebenlist U., Durand D.B., Bressler P., Holbrook N.J., Norris C.A.,
Kamoun M., Kant J.A., Crabtree G.R.;
"Promoter region of interleukin-2 gene undergoes chromatin structure
changes and confers inducibility on chloramphenicol acetyltransferase
gene during activation of T cells.";
Mol. Cell. Biol. 6:3042-3049(1986).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 21-153.
PubMed=3264184; DOI=10.1021/bi00418a034;
Weir M.P., Chaplin M.A., Wallace D.M., Dykes C.W., Hobden A.N.;
"Structure-activity relationships of recombinant human interleukin
2.";
Biochemistry 27:6883-6892(1988).
[14]
PROTEIN SEQUENCE OF 21-153, DISULFIDE BOND, AND GLYCOSYLATION AT
THR-23.
PubMed=6333684; DOI=10.1073/pnas.81.20.6486;
Robb R.J., Kutny R.M., Panico M., Morris H.R., Chowdhry V.;
"Amino acid sequence and post-translational modification of human
interleukin 2.";
Proc. Natl. Acad. Sci. U.S.A. 81:6486-6490(1984).
[15]
GLYCOSYLATION AT THR-23.
PubMed=2793860;
Conradt H.S., Nimtz M., Dittmar K.E.J., Lindenmaier W., Hoppe J.,
Hauser H.;
"Expression of human interleukin-2 in recombinant baby hamster kidney,
Ltk-, and Chinese hamster ovary cells. Structure of O-linked
carbohydrate chains and their location within the polypeptide.";
J. Biol. Chem. 264:17368-17373(1989).
[16]
CHROMOSOMAL TRANSLOCATION WITH TNFRSF17.
PubMed=1396583;
Laabi Y., Gras M.P., Carbonnel F., Brouet J.C., Berger R.,
Larsen C.-J., Tsapis A.;
"A new gene, BCM, on chromosome 16 is fused to the interleukin 2 gene
by a t(4;16)(q26;p13) translocation in a malignant T cell lymphoma.";
EMBO J. 11:3897-3904(1992).
[17]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=3500515; DOI=10.1126/science.3500515;
Brandhuber B.J., Boone T., Kenney W.C., McKay D.B.;
"Three-dimensional structure of interleukin-2.";
Science 238:1707-1709(1987).
[18]
COMPARISON OF X-RAY STRUCTURES.
PubMed=1631562; DOI=10.1126/science.1631562;
Bazan J.F.;
"Unraveling the structure of IL-2.";
Science 257:410-412(1992).
[19]
RESPONSE TO PUBMED:1631562.
McKay D.B.;
Science 257:412-413(1992).
[20]
STRUCTURE BY NMR.
PubMed=1510960; DOI=10.1021/bi00148a040;
Mott H.R., Driscoll P.C., Boyd J., Cooke R.M., Weir M.P.,
Campbell I.D.;
"Secondary structure of human interleukin 2 from 3D heteronuclear NMR
experiments.";
Biochemistry 31:7741-7744(1992).
[21]
3D-STRUCTURE MODELING.
PubMed=7529123; DOI=10.1016/S0969-2126(94)00085-9;
Bamborough P., Hedgecock C.J., Richards W.G.;
"The interleukin-2 and interleukin-4 receptors studied by molecular
modelling.";
Structure 2:839-851(1994).
[22]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-153 IN COMPLEX WITH IL2RA;
IL2RB AND IL2RC.
PubMed=16293754; DOI=10.1126/science.1117893;
Wang X., Rickert M., Garcia K.C.;
"Structure of the quaternary complex of interleukin-2 with its alpha,
beta, and gammac receptors.";
Science 310:1159-1163(2005).
[23]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 21-153 IN COMPLEX WITH IL2RA;
IL2RB AND IL2RC, AND DISULFIDE BOND.
PubMed=16477002; DOI=10.1073/pnas.0511161103;
Stauber D.J., Debler E.W., Horton P.A., Smith K.A., Wilson I.A.;
"Crystal structure of the IL-2 signaling complex: paradigm for a
heterotrimeric cytokine receptor.";
Proc. Natl. Acad. Sci. U.S.A. 103:2788-2793(2006).
-!- FUNCTION: Produced by T-cells in response to antigenic or
mitogenic stimulation, this protein is required for T-cell
proliferation and other activities crucial to regulation of the
immune response. Can stimulate B-cells, monocytes, lymphokine-
activated killer cells, natural killer cells, and glioma cells.
-!- SUBCELLULAR LOCATION: Secreted.
-!- DISEASE: Note=A chromosomal aberration involving IL2 is found in a
form of T-cell acute lymphoblastic leukemia (T-ALL). Translocation
t(4;16)(q26;p13) with involves TNFRSF17.
{ECO:0000269|PubMed:1396583}.
-!- PHARMACEUTICAL: Available under the name Proleukin (Chiron). Used
in patients with renal cell carcinoma or metastatic melanoma.
-!- SIMILARITY: Belongs to the IL-2 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA59140.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=Interleukin-2 entry;
URL="https://en.wikipedia.org/wiki/Interleukin_2";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il2/";
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=IL2";
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EMBL; X00695; CAA25292.1; -; Genomic_DNA.
EMBL; V00564; CAA23827.1; -; mRNA.
EMBL; X01586; CAA25742.1; -; mRNA.
EMBL; J00264; AAD48509.1; -; Genomic_DNA.
EMBL; K02056; AAA98792.1; -; Genomic_DNA.
EMBL; S77834; AAD14263.2; -; mRNA.
EMBL; S82692; AAB46883.1; -; mRNA.
EMBL; AF359939; AAK26665.1; -; Genomic_DNA.
EMBL; BC066255; AAH66255.1; -; mRNA.
EMBL; BC066257; AAH66257.1; -; mRNA.
EMBL; BC070338; AAH70338.1; -; mRNA.
EMBL; M33199; AAA59139.1; -; Genomic_DNA.
EMBL; M13879; AAA59141.1; -; Genomic_DNA.
EMBL; M22005; AAA59140.1; ALT_INIT; Genomic_DNA.
CCDS; CCDS3726.1; -.
PIR; A01849; ICHU2.
RefSeq; NP_000577.2; NM_000586.3.
UniGene; Hs.89679; -.
PDB; 1ILM; Model; -; 2=26-153.
PDB; 1ILN; Model; -; 2=26-153.
PDB; 1IRL; NMR; -; A=21-153.
PDB; 1M47; X-ray; 1.99 A; A=21-153.
PDB; 1M48; X-ray; 1.95 A; A/B=21-153.
PDB; 1M49; X-ray; 2.00 A; A/B=21-153.
PDB; 1M4A; X-ray; 2.18 A; A=21-153.
PDB; 1M4B; X-ray; 2.15 A; A=21-153.
PDB; 1M4C; X-ray; 2.40 A; A/B=21-153.
PDB; 1NBP; X-ray; 2.20 A; A=21-153.
PDB; 1PW6; X-ray; 2.60 A; A/B=21-153.
PDB; 1PY2; X-ray; 2.80 A; A/B/C/D=21-152.
PDB; 1QVN; X-ray; 2.70 A; A/B/C/D=21-152.
PDB; 1Z92; X-ray; 2.80 A; A=21-153.
PDB; 2B5I; X-ray; 2.30 A; A=21-153.
PDB; 2ERJ; X-ray; 3.00 A; D/H=21-153.
PDB; 3INK; X-ray; 2.50 A; C/D=21-153.
PDB; 3QAZ; X-ray; 3.80 A; A/D/G/J/M/P/S/V/Y/b/e/h=21-153.
PDB; 3QB1; X-ray; 3.10 A; A/B/C/D/E/F/G/H=21-153.
PDB; 4NEJ; X-ray; 1.92 A; A=24-153.
PDB; 4NEM; X-ray; 1.93 A; A=24-153.
PDB; 5LQB; X-ray; 1.95 A; A=22-153.
PDB; 5M5E; X-ray; 2.30 A; D=8-153.
PDBsum; 1ILM; -.
PDBsum; 1ILN; -.
PDBsum; 1IRL; -.
PDBsum; 1M47; -.
PDBsum; 1M48; -.
PDBsum; 1M49; -.
PDBsum; 1M4A; -.
PDBsum; 1M4B; -.
PDBsum; 1M4C; -.
PDBsum; 1NBP; -.
PDBsum; 1PW6; -.
PDBsum; 1PY2; -.
PDBsum; 1QVN; -.
PDBsum; 1Z92; -.
PDBsum; 2B5I; -.
PDBsum; 2ERJ; -.
PDBsum; 3INK; -.
PDBsum; 3QAZ; -.
PDBsum; 3QB1; -.
PDBsum; 4NEJ; -.
PDBsum; 4NEM; -.
PDBsum; 5LQB; -.
PDBsum; 5M5E; -.
ProteinModelPortal; P60568; -.
SMR; P60568; -.
BioGrid; 109773; 2.
CORUM; P60568; -.
DIP; DIP-475N; -.
MINT; MINT-1522299; -.
STRING; 9606.ENSP00000226730; -.
BindingDB; P60568; -.
ChEMBL; CHEMBL5880; -.
DrugBank; DB03455; (1H-indol-3-yl)-(2-mercapto-ethoxyimino)-acetic acid.
DrugBank; DB04278; 2-[2-(2-Cyclohexyl-2-Guanidino-Acetylamino)-Acetylamino]-N-(3-Mercapto-Propyl)-Propionamide.
DrugBank; DB05676; Apremilast.
DrugBank; DB05299; keyhole limpet hemocyanin.
DrugBank; DB00852; Pseudoephedrine.
DrugBank; DB03957; SP2456.
DrugBank; DB02555; SP4160.
DrugBank; DB05304; WX-G250.
iPTMnet; P60568; -.
PhosphoSitePlus; P60568; -.
UniCarbKB; P60568; -.
BioMuta; IL2; -.
DMDM; 45593462; -.
PaxDb; P60568; -.
PeptideAtlas; P60568; -.
PRIDE; P60568; -.
DNASU; 3558; -.
Ensembl; ENST00000226730; ENSP00000226730; ENSG00000109471.
GeneID; 3558; -.
KEGG; hsa:3558; -.
CTD; 3558; -.
DisGeNET; 3558; -.
EuPathDB; HostDB:ENSG00000109471.4; -.
GeneCards; IL2; -.
HGNC; HGNC:6001; IL2.
HPA; CAB010310; -.
MIM; 147680; gene.
neXtProt; NX_P60568; -.
OpenTargets; ENSG00000109471; -.
PharmGKB; PA195; -.
eggNOG; ENOG410J049; Eukaryota.
eggNOG; ENOG41119SF; LUCA.
GeneTree; ENSGT00390000003555; -.
HOVERGEN; HBG007496; -.
InParanoid; P60568; -.
KO; K05429; -.
OMA; KWITFCQ; -.
OrthoDB; EOG091G0VTZ; -.
PhylomeDB; P60568; -.
TreeFam; TF338200; -.
Reactome; R-HSA-114604; GPVI-mediated activation cascade.
Reactome; R-HSA-392451; G beta:gamma signalling through PI3Kgamma.
Reactome; R-HSA-451927; Interleukin-2 family signaling.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-8877330; RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs).
Reactome; R-HSA-912526; Interleukin receptor SHC signaling.
SignaLink; P60568; -.
SIGNOR; P60568; -.
ChiTaRS; IL2; human.
EvolutionaryTrace; P60568; -.
GeneWiki; Interleukin_2; -.
GenomeRNAi; 3558; -.
PRO; PR:P60568; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000109471; -.
CleanEx; HS_IL2; -.
ExpressionAtlas; P60568; baseline and differential.
Genevisible; P60568; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0030246; F:carbohydrate binding; IEA:Ensembl.
GO; GO:0005125; F:cytokine activity; IDA:MGI.
GO; GO:0043208; F:glycosphingolipid binding; IEA:Ensembl.
GO; GO:0008083; F:growth factor activity; TAS:UniProtKB.
GO; GO:0005134; F:interleukin-2 receptor binding; IDA:MGI.
GO; GO:0031851; F:kappa-type opioid receptor binding; IEA:Ensembl.
GO; GO:0019209; F:kinase activator activity; TAS:UniProtKB.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0007155; P:cell adhesion; TAS:UniProtKB.
GO; GO:0007267; P:cell-cell signaling; TAS:UniProtKB.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0006955; P:immune response; TAS:UniProtKB.
GO; GO:0002366; P:leukocyte activation involved in immune response; IDA:UniProtKB.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0030101; P:natural killer cell activation; TAS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0002903; P:negative regulation of B cell apoptotic process; IDA:MGI.
GO; GO:0045822; P:negative regulation of heart contraction; IEA:Ensembl.
GO; GO:0050728; P:negative regulation of inflammatory response; IEA:Ensembl.
GO; GO:0050672; P:negative regulation of lymphocyte proliferation; IEA:Ensembl.
GO; GO:0001933; P:negative regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:2000320; P:negative regulation of T-helper 17 cell differentiation; IEA:Ensembl.
GO; GO:0042104; P:positive regulation of activated T cell proliferation; IDA:MGI.
GO; GO:0030890; P:positive regulation of B cell proliferation; IDA:MGI.
GO; GO:0030307; P:positive regulation of cell growth; TAS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; TAS:UniProtKB.
GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IEA:Ensembl.
GO; GO:0060999; P:positive regulation of dendritic spine development; IEA:Ensembl.
GO; GO:0051024; P:positive regulation of immunoglobulin secretion; IEA:Ensembl.
GO; GO:0050729; P:positive regulation of inflammatory response; IC:BHF-UCL.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0032740; P:positive regulation of interleukin-17 production; IDA:BHF-UCL.
GO; GO:0048304; P:positive regulation of isotype switching to IgG isotypes; IEA:Ensembl.
GO; GO:0045591; P:positive regulation of regulatory T cell differentiation; IEA:Ensembl.
GO; GO:0034105; P:positive regulation of tissue remodeling; IC:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IDA:BHF-UCL.
GO; GO:0007205; P:protein kinase C-activating G-protein coupled receptor signaling pathway; IEA:Ensembl.
GO; GO:0045589; P:regulation of regulatory T cell differentiation; TAS:Reactome.
GO; GO:0046013; P:regulation of T cell homeostatic proliferation; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0030217; P:T cell differentiation; TAS:UniProtKB.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR000779; IL-2.
InterPro; IPR030477; IL-2_CS.
PANTHER; PTHR10078:SF32; PTHR10078:SF32; 1.
Pfam; PF00715; IL2; 1.
PRINTS; PR00265; INTERLEUKIN2.
ProDom; PD003649; Interleukin-2; 1.
SMART; SM00189; IL2; 1.
SUPFAM; SSF47266; SSF47266; 1.
PROSITE; PS00424; INTERLEUKIN_2; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Chromosomal rearrangement;
Complete proteome; Cytokine; Direct protein sequencing;
Disulfide bond; Glycoprotein; Growth factor; Immunity; Pharmaceutical;
Proto-oncogene; Reference proteome; Secreted; Signal.
SIGNAL 1 20 {ECO:0000269|PubMed:6333684}.
CHAIN 21 153 Interleukin-2.
/FTId=PRO_0000015484.
CARBOHYD 23 23 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:2793860,
ECO:0000269|PubMed:6333684}.
/FTId=CAR_000051.
DISULFID 78 125 {ECO:0000269|PubMed:16477002,
ECO:0000269|PubMed:6333684}.
VARIANT 21 21 Missing (in FT-IL2-A and FT-IL2-B).
/FTId=VAR_003967.
VARIANT 22 22 Missing (in FT-IL2-B).
/FTId=VAR_003968.
HELIX 25 49 {ECO:0000244|PDB:4NEJ}.
HELIX 53 59 {ECO:0000244|PDB:4NEJ}.
HELIX 60 62 {ECO:0000244|PDB:1IRL}.
STRAND 64 68 {ECO:0000244|PDB:3INK}.
HELIX 73 76 {ECO:0000244|PDB:4NEJ}.
HELIX 77 93 {ECO:0000244|PDB:4NEJ}.
TURN 95 97 {ECO:0000244|PDB:1M48}.
STRAND 98 100 {ECO:0000244|PDB:3INK}.
HELIX 105 117 {ECO:0000244|PDB:4NEJ}.
HELIX 120 122 {ECO:0000244|PDB:5LQB}.
STRAND 127 132 {ECO:0000244|PDB:3INK}.
HELIX 134 149 {ECO:0000244|PDB:4NEJ}.
TURN 150 152 {ECO:0000244|PDB:4NEJ}.
SEQUENCE 153 AA; 17628 MW; 59E2F40F25860F84 CRC64;
MYRMQLLSCI ALSLALVTNS APTSSSTKKT QLQLEHLLLD LQMILNGINN YKNPKLTRML
TFKFYMPKKA TELKHLQCLE EELKPLEEVL NLAQSKNFHL RPRDLISNIN VIVLELKGSE
TTFMCEYADE TATIVEFLNR WITFCQSIIS TLT


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10-288-22461 Interleukin-2 (IL-2) Human Recombinant Protein. E. coli - IL-2; T-cell growth factor; TCGF; Aldesleukin 0.05 mg
10-288-22461 Interleukin-2 (IL-2) Human Recombinant Protein. E. coli - IL-2; T-cell growth factor; TCGF; Aldesleukin 1 mg
10-288-22461 Interleukin-2 (IL-2) Human Recombinant Protein. E. coli - IL-2; T-cell growth factor; TCGF; Aldesleukin 0.01 mg
20-663-48002 Interleukin-2 (mAHuIL-2) - Mouse Anti-Human Interleukin-2 (mAHuIL-2); IL-2; T-cell growth factor; TCGF; Aldesleukin Monoclonal 0.5 mg
20-663-48002 Interleukin-2 (mAHuIL-2) - Mouse Anti-Human Interleukin-2 (mAHuIL-2); IL-2; T-cell growth factor; TCGF; Aldesleukin Monoclonal 1 mg
10-663-45200 Interleukin-2 (IL-2) Murine - IL-2; T-cell growth factor; TCGF N_A 1 mg
10-663-45200 Interleukin-2 (IL-2) Murine - IL-2; T-cell growth factor; TCGF N_A 0.02 mg
10-663-45200 Interleukin-2 (IL-2) Murine - IL-2; T-cell growth factor; TCGF N_A 0.005 mg
E0073p ELISA IL2,IL-2,Interleukin-2,Pig,Sus scrofa,T-cell growth factor,TCGF 96T
U0073p CLIA IL2,IL-2,Interleukin-2,Pig,Sus scrofa,T-cell growth factor,TCGF 96T
E0073p ELISA kit IL2,IL-2,Interleukin-2,Pig,Sus scrofa,T-cell growth factor,TCGF 96T
0801017 Natural Human Interleukin-2 IL-2 per T-Cell Growth Factor TCGF 50 mL, 25,000 BRMP Units
E0073r ELISA Il2,IL-2,Il-2,Interleukin-2,Rat,Rattus norvegicus,T-cell growth factor,TCGF 96T


 

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