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Interleukin-6 (IL-6) (B-cell hybridoma growth factor) (Interleukin HP-1)

 IL6_MOUSE               Reviewed;         211 AA.
P08505; Q3UCQ0; Q8BN26;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
25-OCT-2017, entry version 165.
RecName: Full=Interleukin-6;
Short=IL-6;
AltName: Full=B-cell hybridoma growth factor;
AltName: Full=Interleukin HP-1;
Flags: Precursor;
Name=Il6; Synonyms=Il-6;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2965020; DOI=10.1002/eji.1830180202;
van Snick J., Cayphas S., Szikora J.-P., Renauld J.-C., van Roost E.,
Boon T., Simpson R.J.;
"cDNA cloning of murine interleukin-HP1: homology with human
interleukin 6.";
Eur. J. Immunol. 18:193-197(1988).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=3263439;
Tanabe O., Akira S., Kamiya T., Wong G.G., Hirano T., Kishimoto T.;
"Genomic structure of the murine IL-6 gene. High degree conservation
of potential regulatory sequences between mouse and human.";
J. Immunol. 141:3875-3881(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3262872; DOI=10.1073/pnas.85.19.7099;
Chiu C.P., Moulds C., Coffman R.L., Rennick D., Lee F.;
"Multiple biological activities are expressed by a mouse interleukin 6
cDNA clone isolated from bone marrow stromal cells.";
Proc. Natl. Acad. Sci. U.S.A. 85:7099-7103(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ;
PubMed=2243807; DOI=10.1093/nar/18.21.6455;
Grenett H.E., Fuentes N.L., Fuller G.M.;
"Cloning and sequence analysis of the cDNA for murine interleukin-6.";
Nucleic Acids Res. 18:6455-6455(1990).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Macrophage;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-6.
STRAIN=BALB/cJ;
PubMed=2106569; DOI=10.1084/jem.171.3.965;
Blankenstein T., Qin Z., Li W., Diamantstein T.;
"DNA rearrangement and constitutive expression of the interleukin 6
gene in a mouse plasmacytoma.";
J. Exp. Med. 171:965-970(1990).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 5-211.
STRAIN=C57BL/6J;
PubMed=2563387;
Mock B.A., Nordan R.P., Justice M.J., Kozak C., Jenkins N.A.,
Copeland N.G., Clark S.C., Wong G.G., Rudikoff S.;
"The murine Il-6 gene maps to the proximal region of chromosome 5.";
J. Immunol. 142:1372-1376(1989).
[8]
PROTEIN SEQUENCE OF 25-45.
PubMed=2948184; DOI=10.1073/pnas.83.24.9679;
van Snick J., Cayphas S., Vink A., Uyttenhove C., Coulie P.G.,
Rubira M.R., Simpson R.J.;
"Purification and NH2-terminal amino acid sequence of a T-cell-derived
lymphokine with growth factor activity for B-cell hybridomas.";
Proc. Natl. Acad. Sci. U.S.A. 83:9679-9683(1986).
[9]
PROTEIN SEQUENCE OF 25-211.
PubMed=3262059; DOI=10.1111/j.1432-1033.1988.tb14267.x;
Simpson R.J., Moritz R.L., Rubira M.R., van Snick J.;
"Murine hybridoma/plasmacytoma growth factor. Complete amino-acid
sequence and relation to human interleukin-6.";
Eur. J. Biochem. 176:187-197(1988).
[10]
PROTEIN SEQUENCE OF 66-75; 78-84 AND 128-148.
PubMed=2302197; DOI=10.1016/0006-291X(90)91922-F;
Jahnen W., Ward L.D., Reid G.E., Moritz R.L., Simpson R.J.;
"Internal amino acid sequencing of proteins by in situ cyanogen
bromide cleavage in polyacrylamide gels.";
Biochem. Biophys. Res. Commun. 166:139-145(1990).
[11]
DISULFIDE BONDS.
PubMed=3264160; DOI=10.1016/S0006-291X(88)80056-1;
Simpson R.J., Moritz R.L., van Roost E., van Snick J.;
"Characterization of a recombinant murine interleukin-6: assignment of
disulphide bonds.";
Biochem. Biophys. Res. Commun. 157:364-372(1988).
[12]
FUNCTION IN TH17 DIFFERENTIATION, AND DISRUPTION PHENOTYPE.
PubMed=16990136; DOI=10.1016/j.cell.2006.07.035;
Ivanov I.I., McKenzie B.S., Zhou L., Tadokoro C.E., Lepelley A.,
Lafaille J.J., Cua D.J., Littman D.R.;
"The orphan nuclear receptor RORgammat directs the differentiation
program of proinflammatory IL-17+ T helper cells.";
Cell 126:1121-1133(2006).
-!- FUNCTION: Cytokine with a wide variety of biological functions. It
is a potent inducer of the acute phase response. Plays an
essential role in the final differentiation of B-cells into Ig-
secreting cells Involved in lymphocyte and monocyte
differentiation. Acts on B-cells, T-cells, hepatocytes,
hematopoietic progenitor cells and cells of the CNS. Required for
the generation of T(H)17 cells. Also acts as a myokine. It is
discharged into the bloodstream after muscle contraction and acts
to increase the breakdown of fats and to improve insulin
resistance. It induces myeloma and plasmacytoma growth and induces
nerve cells differentiation. {ECO:0000269|PubMed:16990136}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- DISRUPTION PHENOTYPE: Animals have normal T-cell numbers in the
lamina propria but the T(H)17 cells are reduced by about 10-fold.
{ECO:0000269|PubMed:16990136}.
-!- SIMILARITY: Belongs to the IL-6 superfamily. {ECO:0000305}.
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EMBL; X06203; CAA29560.1; -; mRNA.
EMBL; M20572; AAA39302.1; -; Genomic_DNA.
EMBL; J03783; AAA39301.1; -; mRNA.
EMBL; X54542; CAA38411.1; -; mRNA.
EMBL; AK150440; BAE29562.1; -; mRNA.
EMBL; X51457; CAA35824.1; -; Genomic_DNA.
EMBL; M24221; AAA68814.1; -; Genomic_DNA.
CCDS; CCDS19153.1; -.
PIR; A30531; ICMS6.
RefSeq; NP_001300983.1; NM_001314054.1.
RefSeq; NP_112445.1; NM_031168.2.
UniGene; Mm.1019; -.
PDB; 2L3Y; NMR; -; A=27-211.
PDBsum; 2L3Y; -.
ProteinModelPortal; P08505; -.
SMR; P08505; -.
BioGrid; 200641; 2.
IntAct; P08505; 1.
STRING; 10090.ENSMUSP00000026845; -.
PhosphoSitePlus; P08505; -.
MaxQB; P08505; -.
PaxDb; P08505; -.
PRIDE; P08505; -.
Ensembl; ENSMUST00000026845; ENSMUSP00000026845; ENSMUSG00000025746.
GeneID; 16193; -.
KEGG; mmu:16193; -.
UCSC; uc008wuu.1; mouse.
CTD; 3569; -.
MGI; MGI:96559; Il6.
eggNOG; ENOG410IW11; Eukaryota.
eggNOG; ENOG4112BXV; LUCA.
GeneTree; ENSGT00390000000878; -.
HOGENOM; HOG000236330; -.
HOVERGEN; HBG000471; -.
InParanoid; P08505; -.
KO; K05405; -.
OMA; LQAQNQW; -.
OrthoDB; EOG091G0NW5; -.
PhylomeDB; P08505; -.
TreeFam; TF335984; -.
Reactome; R-MMU-110056; MAPK3 (ERK1) activation.
Reactome; R-MMU-112411; MAPK1 (ERK2) activation.
Reactome; R-MMU-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
Reactome; R-MMU-6783589; Interleukin-6 family signaling.
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
EvolutionaryTrace; P08505; -.
PRO; PR:P08505; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000025746; -.
CleanEx; MM_IL6; -.
ExpressionAtlas; P08505; baseline and differential.
Genevisible; P08505; MM.
GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0005896; C:interleukin-6 receptor complex; ISO:MGI.
GO; GO:0005125; F:cytokine activity; IDA:BHF-UCL.
GO; GO:0008083; F:growth factor activity; ISO:MGI.
GO; GO:0005138; F:interleukin-6 receptor binding; IDA:MGI.
GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0046849; P:bone remodeling; IEA:Ensembl.
GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IDA:MGI.
GO; GO:0016049; P:cell growth; IEA:Ensembl.
GO; GO:0045454; P:cell redox homeostasis; IEA:Ensembl.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0071392; P:cellular response to estradiol stimulus; IEA:Ensembl.
GO; GO:0035729; P:cellular response to hepatocyte growth factor stimulus; IDA:MGI.
GO; GO:0070301; P:cellular response to hydrogen peroxide; ISO:MGI.
GO; GO:0071347; P:cellular response to interleukin-1; IDA:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:MGI.
GO; GO:0031669; P:cellular response to nutrient levels; IEA:Ensembl.
GO; GO:1990646; P:cellular response to prolactin; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:MGI.
GO; GO:0019221; P:cytokine-mediated signaling pathway; ISO:MGI.
GO; GO:0042832; P:defense response to protozoan; IMP:MGI.
GO; GO:0051607; P:defense response to virus; ISO:MGI.
GO; GO:0031018; P:endocrine pancreas development; IMP:BHF-UCL.
GO; GO:0060664; P:epithelial cell proliferation involved in salivary gland morphogenesis; IDA:MGI.
GO; GO:0070091; P:glucagon secretion; IMP:BHF-UCL.
GO; GO:0042593; P:glucose homeostasis; IGI:MGI.
GO; GO:0002384; P:hepatic immune response; ISO:MGI.
GO; GO:0006954; P:inflammatory response; ISO:MGI.
GO; GO:0070102; P:interleukin-6-mediated signaling pathway; IDA:BHF-UCL.
GO; GO:0031294; P:lymphocyte costimulation; IEA:Ensembl.
GO; GO:0046716; P:muscle cell cellular homeostasis; IGI:MGI.
GO; GO:0002262; P:myeloid cell homeostasis; IMP:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0045779; P:negative regulation of bone resorption; IMP:BHF-UCL.
GO; GO:0008285; P:negative regulation of cell proliferation; IEA:Ensembl.
GO; GO:0045079; P:negative regulation of chemokine biosynthetic process; IDA:MGI.
GO; GO:0032966; P:negative regulation of collagen biosynthetic process; ISO:MGI.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IEA:Ensembl.
GO; GO:0050710; P:negative regulation of cytokine secretion; IEA:Ensembl.
GO; GO:0045721; P:negative regulation of gluconeogenesis; IEA:Ensembl.
GO; GO:0046888; P:negative regulation of hormone secretion; IDA:MGI.
GO; GO:2000660; P:negative regulation of interleukin-1-mediated signaling pathway; IMP:BHF-UCL.
GO; GO:0045837; P:negative regulation of membrane potential; IEA:Ensembl.
GO; GO:0048635; P:negative regulation of muscle organ development; IEA:Ensembl.
GO; GO:1901215; P:negative regulation of neuron death; IEA:Ensembl.
GO; GO:0006469; P:negative regulation of protein kinase activity; IEA:Ensembl.
GO; GO:0031175; P:neuron projection development; ISO:MGI.
GO; GO:0001781; P:neutrophil apoptotic process; IDA:MGI.
GO; GO:0002675; P:positive regulation of acute inflammatory response; ISO:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0050871; P:positive regulation of B cell activation; ISO:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0071864; P:positive regulation of cell proliferation in bone marrow; IGI:MGI.
GO; GO:0032722; P:positive regulation of chemokine production; ISO:MGI.
GO; GO:0045740; P:positive regulation of DNA replication; IEA:Ensembl.
GO; GO:0050679; P:positive regulation of epithelial cell proliferation; IDA:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0010628; P:positive regulation of gene expression; IGI:MGI.
GO; GO:0051024; P:positive regulation of immunoglobulin secretion; ISO:MGI.
GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
GO; GO:0046427; P:positive regulation of JAK-STAT cascade; ISO:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; IEA:Ensembl.
GO; GO:0033138; P:positive regulation of peptidyl-serine phosphorylation; ISO:MGI.
GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; ISO:MGI.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IEA:Ensembl.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IEA:Ensembl.
GO; GO:0051091; P:positive regulation of sequence-specific DNA binding transcription factor activity; ISO:MGI.
GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; ISO:MGI.
GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:MGI.
GO; GO:2000553; P:positive regulation of T-helper 2 cell cytokine production; IMP:BHF-UCL.
GO; GO:0045630; P:positive regulation of T-helper 2 cell differentiation; IDA:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0045727; P:positive regulation of translation; ISO:MGI.
GO; GO:0051971; P:positive regulation of transmission of nerve impulse; IEA:Ensembl.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; ISO:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IMP:MGI.
GO; GO:0042127; P:regulation of cell proliferation; IGI:MGI.
GO; GO:0008360; P:regulation of cell shape; IEA:Ensembl.
GO; GO:0045188; P:regulation of circadian sleep/wake cycle, non-REM sleep; IEA:Ensembl.
GO; GO:0010574; P:regulation of vascular endothelial growth factor production; ISO:MGI.
GO; GO:0043200; P:response to amino acid; IEA:Ensembl.
GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
GO; GO:0010996; P:response to auditory stimulus; IEA:Ensembl.
GO; GO:0031000; P:response to caffeine; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; IEA:Ensembl.
GO; GO:0009409; P:response to cold; IEA:Ensembl.
GO; GO:0042493; P:response to drug; IEA:Ensembl.
GO; GO:0051602; P:response to electrical stimulus; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; ISO:MGI.
GO; GO:0009408; P:response to heat; IEA:Ensembl.
GO; GO:0032868; P:response to insulin; IEA:Ensembl.
GO; GO:0009611; P:response to wounding; IDA:MGI.
GO; GO:0001878; P:response to yeast; IEA:Ensembl.
GO; GO:0042110; P:T cell activation; IGI:MGI.
GO; GO:0072540; P:T-helper 17 cell lineage commitment; IMP:UniProtKB.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR003574; IL-6.
InterPro; IPR030474; IL-6/GCSF/MGF.
InterPro; IPR030473; IL6/GCSF/MGF_CS.
Pfam; PF00489; IL6; 1.
PIRSF; PIRSF001935; IL6_MGF_GCSF; 1.
PRINTS; PR00433; IL6GCSFMGF.
SMART; SM00126; IL6; 1.
SUPFAM; SSF47266; SSF47266; 1.
PROSITE; PS00254; INTERLEUKIN_6; 1.
1: Evidence at protein level;
3D-structure; Acute phase; Complete proteome; Cytokine;
Direct protein sequencing; Disulfide bond; Growth factor;
Reference proteome; Secreted; Signal.
SIGNAL 1 24 {ECO:0000269|PubMed:2948184,
ECO:0000269|PubMed:3262059}.
CHAIN 25 211 Interleukin-6.
/FTId=PRO_0000015588.
DISULFID 70 76 {ECO:0000269|PubMed:3264160}.
DISULFID 99 109 {ECO:0000269|PubMed:3264160}.
HELIX 48 68 {ECO:0000244|PDB:2L3Y}.
TURN 69 72 {ECO:0000244|PDB:2L3Y}.
HELIX 74 77 {ECO:0000244|PDB:2L3Y}.
TURN 81 83 {ECO:0000244|PDB:2L3Y}.
HELIX 84 86 {ECO:0000244|PDB:2L3Y}.
STRAND 101 103 {ECO:0000244|PDB:2L3Y}.
HELIX 114 129 {ECO:0000244|PDB:2L3Y}.
HELIX 133 160 {ECO:0000244|PDB:2L3Y}.
HELIX 170 176 {ECO:0000244|PDB:2L3Y}.
HELIX 186 209 {ECO:0000244|PDB:2L3Y}.
SEQUENCE 211 AA; 24384 MW; BBB47DDA9E86787A CRC64;
MKFLSARDFH PVAFLGLMLV TTTAFPTSQV RRGDFTEDTT PNRPVYTTSQ VGGLITHVLW
EIVEMRKELC NGNSDCMNND DALAENNLKL PEIQRNDGCY QTGYNQEICL LKISSGLLEY
HSYLEYMKNN LKDNKKDKAR VLQRDTETLI HIFNQEVKDL HKIVLPTPIS NALLTDKLES
QKEWLRTKTI QFILKSLEEF LKVTLRSTRQ T


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10-663-45216 Interleukin-6 Rat - IL-6; B-cell stimulatory factor 2; BSF-2; Interferon beta-2; Hybridoma growth factor; CTL differentiation factor; CDF N_A 0.01 mg
10-663-45216 Interleukin-6 Rat - IL-6; B-cell stimulatory factor 2; BSF-2; Interferon beta-2; Hybridoma growth factor; CTL differentiation factor; CDF N_A 0.002 mg
10-663-45216 Interleukin-6 Rat - IL-6; B-cell stimulatory factor 2; BSF-2; Interferon beta-2; Hybridoma growth factor; CTL differentiation factor; CDF N_A 1 mg
15-288-22495 Interleukin-6 - IL-6; B-cell stimulatory factor 2; BSF-2; Interferon beta-2; Hybridoma growth factor; CTL differentiation factor; CDF Polyclonal 0.05 mg
10-663-45083 Interleukin-6 (IL-6) Human - IL-6; B-cell stimulatory factor 2; BSF-2; Interferon beta-2; Hybridoma growth factor; CTL differentiation factor; CDF N_A 0.005 mg
10-663-45226 Interleukin-6 (IL-6) Porcine - IL-6; B-cell stimulatory factor 2; BSF-2; Interferon beta-2; Hybridoma growth factor; CTL differentiation factor; CDF N_A 0.002 mg
15-288-22495 Interleukin-6 - IL-6; B-cell stimulatory factor 2; BSF-2; Interferon beta-2; Hybridoma growth factor; CTL differentiation factor; CDF Polyclonal 0.1 mg
10-663-45226 Interleukin-6 (IL-6) Porcine - IL-6; B-cell stimulatory factor 2; BSF-2; Interferon beta-2; Hybridoma growth factor; CTL differentiation factor; CDF N_A 0.01 mg
10-663-45226 Interleukin-6 (IL-6) Porcine - IL-6; B-cell stimulatory factor 2; BSF-2; Interferon beta-2; Hybridoma growth factor; CTL differentiation factor; CDF N_A 0.1 mg
10-663-45083 Interleukin-6 (IL-6) Human - IL-6; B-cell stimulatory factor 2; BSF-2; Interferon beta-2; Hybridoma growth factor; CTL differentiation factor; CDF N_A 0.02 mg


 

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