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

Macrophage colony-stimulating factor 1 (CSF-1) (MCSF) [Cleaved into: Processed macrophage colony-stimulating factor 1]

 CSF1_MOUSE              Reviewed;         552 AA.
P07141; Q3U395; Q8R3C8;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
12-SEP-2018, entry version 169.
RecName: Full=Macrophage colony-stimulating factor 1;
Short=CSF-1;
Short=MCSF;
Contains:
RecName: Full=Processed macrophage colony-stimulating factor 1;
Flags: Precursor;
Name=Csf1; Synonyms=Csfm;
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].
PubMed=3494232; DOI=10.1093/nar/15.5.2389;
Delamarter J.F., Hession C., Semon D., Gough N.M., Rothenbuhler R.,
Mermod J.-J.;
"Nucleotide sequence of a cDNA encoding murine CSF-1 (Macrophage-
CSF).";
Nucleic Acids Res. 15:2389-2390(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2457916; DOI=10.1073/pnas.85.18.6706;
Ladner M.B., Martin G.A., Noble J.A., Wittman V.P., Warren M.K.,
McGrogan M., Stanley E.R.;
"cDNA cloning and expression of murine macrophage colony-stimulating
factor from L929 cells.";
Proc. Natl. Acad. Sci. U.S.A. 85:6706-6710(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8357831; DOI=10.1016/0167-4781(93)90108-P;
Borycki A.G., Lenormund J., Guillier M., Leibovitch S.A.;
"Isolation and characterization of a cDNA clone encoding for rat CSF-1
gene. Post-transcriptional repression occurs in myogenic
differentiation.";
Biochim. Biophys. Acta 1174:143-152(1993).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD; TISSUE=Head, and Spinal cord;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Embryonic germ cell, and Neural stem cell;
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).
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-100.
PubMed=3493488; DOI=10.1073/pnas.84.5.1157;
Rajavashisth T.B., Eng R., Shadduck R.K., Waheed A., Ben-Avram C.M.,
Shively J.E., Lusis A.J.;
"Cloning and tissue-specific expression of mouse macrophage colony-
stimulating factor mRNA.";
Proc. Natl. Acad. Sci. U.S.A. 84:1157-1161(1987).
[8]
PROTEIN SEQUENCE OF 33-57.
PubMed=3925458; DOI=10.1073/pnas.82.13.4486;
Ben-Avram C.M., Shively J.E., Shadduck R.K., Waheed A.,
Rajavashisth T.B., Lusis A.J.;
"Amino-terminal amino acid sequence of murine colony-stimulating
factor 1.";
Proc. Natl. Acad. Sci. U.S.A. 82:4486-4489(1985).
[9]
NUCLEOTIDE SEQUENCE OF 1-13.
PubMed=1874443; DOI=10.1016/0378-1119(91)90074-L;
Harrington M.A., Edenberg H.J., Saxman S.M., Pedigo L.M., Daub R.,
Broxmeyer H.E.;
"Cloning and characterization of the murine promoter for the colony-
stimulating factor-1-encoding gene.";
Gene 102:165-170(1991).
[10]
SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:8357831 ORIGINATES FROM MOUSE.
PubMed=12074592; DOI=10.1016/S0006-291X(02)00598-3;
Dobbins D.E., Sood R., Hashiramoto A., Hansen C.T., Wilder R.L.,
Remmers E.F.;
"Mutation of macrophage colony stimulating factor (Csf1) causes
osteopetrosis in the tl rat.";
Biochem. Biophys. Res. Commun. 294:1114-1120(2002).
[11]
SHOWS THAT SEQUENCE DESCRIBED IN PUBMED:8357831 ORIGINATES FROM MOUSE.
PubMed=12379742; DOI=10.1073/pnas.202332999;
Van Wesenbeeck L., Odgren P.R., MacKay C.A., D'Angelo M., Safadi F.F.,
Popoff S.N., Van Hul W., Marks S.C. Jr.;
"The osteopetrotic mutation toothless (tl) is a loss-of-function
frameshift mutation in the rat Csf1 gene: evidence of a crucial role
for CSF-1 in osteoclastogenesis and endochondral ossification.";
Proc. Natl. Acad. Sci. U.S.A. 99:14303-14308(2002).
[12]
CHARACTERIZATION.
PubMed=1733926;
Price L.K.H., Choi H.U., Rosenberg L., Stanley E.R.;
"The predominant form of secreted colony stimulating factor-1 is a
proteoglycan.";
J. Biol. Chem. 267:2190-2199(1992).
[13]
DISEASE.
PubMed=2188141; DOI=10.1038/345442a0;
Yoshida H., Hayashi S., Kunisada T., Ogawa M., Nishikawa S.,
Okamura H., Sudo T., Shultz L.D., Nishikawa S.;
"The murine mutation osteopetrosis is in the coding region of the
macrophage colony stimulating factor gene.";
Nature 345:442-444(1990).
[14]
X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 36-180 IN COMPLEX WITH
CSF1R, SUBUNIT, AND DISULFIDE BONDS.
PubMed=19017797; DOI=10.1073/pnas.0807762105;
Chen X., Liu H., Focia P.J., Shim A.H., He X.;
"Structure of macrophage colony stimulating factor bound to FMS:
diverse signaling assemblies of class III receptor tyrosine kinases.";
Proc. Natl. Acad. Sci. U.S.A. 105:18267-18272(2008).
-!- FUNCTION: Cytokine that plays an essential role in the regulation
of survival, proliferation and differentiation of hematopoietic
precursor cells, especially mononuclear phagocytes, such as
macrophages and monocytes. Promotes the release of proinflammatory
chemokines, and thereby plays an important role in innate immunity
and in inflammatory processes. Plays an important role in the
regulation of osteoclast proliferation and differentiation, the
regulation of bone resorption, and is required for normal bone
development. Required for normal male and female fertility.
Promotes reorganization of the actin cytoskeleton, regulates
formation of membrane ruffles, cell adhesion and cell migration.
Plays a role in lipoprotein clearance.
-!- SUBUNIT: Homodimer or heterodimer; disulfide-linked. Interacts
with CSF1R. {ECO:0000269|PubMed:19017797}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-777188, EBI-777188;
Q8C161:Aar2; NbExp=2; IntAct=EBI-777188, EBI-777252;
P03228:BARF1 (xeno); NbExp=8; IntAct=EBI-777188, EBI-16007073;
Q60771:Cldn11; NbExp=2; IntAct=EBI-777188, EBI-309095;
P09581:Csf1r; NbExp=6; IntAct=EBI-777188, EBI-6305373;
Q9JHU4:Dync1h1; NbExp=2; IntAct=EBI-777188, EBI-645061;
P05480:Src; NbExp=2; IntAct=EBI-777188, EBI-298680;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Processed macrophage colony-stimulating
factor 1: Secreted, extracellular space {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P07141-1; Sequence=Displayed;
Name=2;
IsoId=P07141-2; Sequence=VSP_001189;
Note=No experimental confirmation available.;
-!- PTM: N-glycosylated. The predominant soluble form is a chondroitin
sulfate-containing proteoglycan.
-!- DISEASE: Note=A defect in Csf1 is the cause of osteopetrosis.
Osteopetrotic mice (op/op) are severely deficient in mature
macrophages and osteoclasts, display failed tooth eruption, and
have a restricted capacity for bone remodeling.
{ECO:0000269|PubMed:2188141}.
-!- CAUTION: The sequence reported in PubMed:8357831 was thought to
originate from rat, but was later shown (PubMed:12074592 and
PubMed:12379742) to be derived from mouse. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; X05010; CAA28660.1; -; mRNA.
EMBL; M21952; AAA37481.1; -; mRNA.
EMBL; M21149; AAA37482.1; -; mRNA.
EMBL; M84361; AAA03032.1; -; mRNA.
EMBL; AK138489; BAE23681.1; -; mRNA.
EMBL; AK154872; BAE32893.1; -; mRNA.
EMBL; AK160995; BAE36140.1; -; mRNA.
EMBL; CH466607; EDL01916.1; -; Genomic_DNA.
EMBL; CH466607; EDL01919.1; -; Genomic_DNA.
EMBL; BC025593; AAH25593.1; -; mRNA.
EMBL; BC066187; AAH66187.1; -; mRNA.
EMBL; BC066200; AAH66200.1; -; mRNA.
EMBL; BC066205; AAH66205.1; -; mRNA.
EMBL; M15692; AAA37480.1; -; mRNA.
EMBL; M81316; AAA19866.1; -; Unassigned_DNA.
CCDS; CCDS17740.1; -. [P07141-1]
CCDS; CCDS51044.1; -. [P07141-2]
PIR; A31401; A31401.
RefSeq; NP_001107001.1; NM_001113529.1. [P07141-2]
RefSeq; NP_001107002.1; NM_001113530.1. [P07141-1]
RefSeq; NP_031804.3; NM_007778.4. [P07141-1]
UniGene; Mm.795; -.
PDB; 3EJJ; X-ray; 2.40 A; A/B=36-180.
PDB; 3UF5; X-ray; 2.80 A; A/B=33-181.
PDB; 4ADQ; X-ray; 4.50 A; E/F/G/H=33-181.
PDBsum; 3EJJ; -.
PDBsum; 3UF5; -.
PDBsum; 4ADQ; -.
ProteinModelPortal; P07141; -.
SMR; P07141; -.
DIP; DIP-45278N; -.
IntAct; P07141; 43.
STRING; 10090.ENSMUSP00000014743; -.
BindingDB; P07141; -.
ChEMBL; CHEMBL3638330; -.
iPTMnet; P07141; -.
PhosphoSitePlus; P07141; -.
SwissPalm; P07141; -.
PaxDb; P07141; -.
PeptideAtlas; P07141; -.
PRIDE; P07141; -.
Ensembl; ENSMUST00000014743; ENSMUSP00000014743; ENSMUSG00000014599. [P07141-1]
Ensembl; ENSMUST00000118593; ENSMUSP00000113136; ENSMUSG00000014599. [P07141-2]
Ensembl; ENSMUST00000120243; ENSMUSP00000113617; ENSMUSG00000014599. [P07141-1]
GeneID; 12977; -.
KEGG; mmu:12977; -.
UCSC; uc008qxk.2; mouse. [P07141-1]
UCSC; uc008qxl.2; mouse. [P07141-2]
CTD; 1435; -.
MGI; MGI:1339753; Csf1.
eggNOG; ENOG410II8R; Eukaryota.
eggNOG; ENOG410Z5Q9; LUCA.
GeneTree; ENSGT00390000015805; -.
HOGENOM; HOG000112010; -.
HOVERGEN; HBG005410; -.
InParanoid; P07141; -.
KO; K05453; -.
OMA; DTGHERQ; -.
OrthoDB; EOG091G0TMC; -.
PhylomeDB; P07141; -.
TreeFam; TF337718; -.
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-449836; Other interleukin signaling.
Reactome; R-MMU-8957275; Post-translational protein phosphorylation.
EvolutionaryTrace; P07141; -.
PRO; PR:P07141; -.
Proteomes; UP000000589; Chromosome 3.
Bgee; ENSMUSG00000014599; Expressed in 268 organ(s), highest expression level in uterus.
CleanEx; MM_CSF1; -.
ExpressionAtlas; P07141; baseline and differential.
Genevisible; P07141; MM.
GO; GO:1990682; C:CSF1-CSF1R complex; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005125; F:cytokine activity; ISO:MGI.
GO; GO:0008083; F:growth factor activity; ISO:MGI.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005157; F:macrophage colony-stimulating factor receptor binding; IPI:BHF-UCL.
GO; GO:0042803; F:protein homodimerization activity; IPI:BHF-UCL.
GO; GO:0060444; P:branching involved in mammary gland duct morphogenesis; IMP:MGI.
GO; GO:0008283; P:cell proliferation; ISO:MGI.
GO; GO:0003006; P:developmental process involved in reproduction; IMP:BHF-UCL.
GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0038145; P:macrophage colony-stimulating factor signaling pathway; IDA:BHF-UCL.
GO; GO:0030225; P:macrophage differentiation; ISO:MGI.
GO; GO:0060763; P:mammary duct terminal end bud growth; IMP:MGI.
GO; GO:0060611; P:mammary gland fat development; IMP:MGI.
GO; GO:0042476; P:odontogenesis; ISO:MGI.
GO; GO:0001503; P:ossification; ISO:MGI.
GO; GO:0030316; P:osteoclast differentiation; IDA:MGI.
GO; GO:0002158; P:osteoclast proliferation; IDA:MGI.
GO; GO:0030335; P:positive regulation of cell migration; IGI:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; ISO:MGI.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IGI:MGI.
GO; GO:0032270; P:positive regulation of cellular protein metabolic process; ISO:MGI.
GO; GO:0010628; P:positive regulation of gene expression; ISO:MGI.
GO; GO:0010759; P:positive regulation of macrophage chemotaxis; ISO:MGI.
GO; GO:1902228; P:positive regulation of macrophage colony-stimulating factor signaling pathway; ISO:MGI.
GO; GO:0010744; P:positive regulation of macrophage derived foam cell differentiation; ISO:MGI.
GO; GO:0045651; P:positive regulation of macrophage differentiation; IMP:MGI.
GO; GO:1904141; P:positive regulation of microglial cell migration; ISO:MGI.
GO; GO:0045657; P:positive regulation of monocyte differentiation; IMP:MGI.
GO; GO:0032946; P:positive regulation of mononuclear cell proliferation; ISO:MGI.
GO; GO:0040018; P:positive regulation of multicellular organism growth; IMP:MGI.
GO; GO:0042488; P:positive regulation of odontogenesis of dentin-containing tooth; IMP:MGI.
GO; GO:0045672; P:positive regulation of osteoclast differentiation; IDA:MGI.
GO; GO:0045860; P:positive regulation of protein kinase activity; IGI:MGI.
GO; GO:0046579; P:positive regulation of Ras protein signal transduction; IDA:MGI.
GO; GO:0030278; P:regulation of ossification; IMP:MGI.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; ISO:MGI.
InterPro; IPR009079; 4_helix_cytokine-like_core.
InterPro; IPR008001; MCSF-1.
PANTHER; PTHR10058; PTHR10058; 1.
Pfam; PF05337; CSF-1; 1.
PIRSF; PIRSF001948; MCSF-1; 1.
SUPFAM; SSF47266; SSF47266; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Cytokine; Direct protein sequencing; Disulfide bond; Glycoprotein;
Growth factor; Immunity; Inflammatory response; Innate immunity;
Membrane; Proteoglycan; Reference proteome; Secreted; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 32 {ECO:0000269|PubMed:3925458}.
CHAIN 33 552 Macrophage colony-stimulating factor 1.
/FTId=PRO_0000005858.
CHAIN 33 447 Processed macrophage colony-stimulating
factor 1. {ECO:0000250|UniProtKB:Q8JZQ0}.
/FTId=PRO_0000296232.
TOPO_DOM 33 492 Extracellular. {ECO:0000255}.
TRANSMEM 493 515 Helical. {ECO:0000255}.
TOPO_DOM 516 552 Cytoplasmic. {ECO:0000255}.
CARBOHYD 107 107 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 154 154 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 39 122 {ECO:0000269|PubMed:19017797}.
DISULFID 63 63 Interchain.
{ECO:0000269|PubMed:19017797}.
DISULFID 80 171 {ECO:0000269|PubMed:19017797}.
DISULFID 134 178 {ECO:0000269|PubMed:19017797}.
DISULFID 189 189 Interchain. {ECO:0000250}.
DISULFID 191 191 Interchain. {ECO:0000250}.
VAR_SEQ 182 476 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_001189.
VARIANT 292 292 D -> G.
VARIANT 345 345 S -> P.
CONFLICT 3 3 Missing (in Ref. 7; AAA37480).
{ECO:0000305}.
CONFLICT 6 6 A -> R (in Ref. 7; AAA37480).
{ECO:0000305}.
CONFLICT 7 8 AG -> PR (in Ref. 7; AAA37480).
{ECO:0000305}.
CONFLICT 246 246 P -> A (in Ref. 1; CAA28660).
{ECO:0000305}.
HELIX 37 41 {ECO:0000244|PDB:3EJJ}.
HELIX 45 55 {ECO:0000244|PDB:3EJJ}.
STRAND 65 70 {ECO:0000244|PDB:3EJJ}.
TURN 72 74 {ECO:0000244|PDB:3EJJ}.
HELIX 78 95 {ECO:0000244|PDB:3EJJ}.
HELIX 104 118 {ECO:0000244|PDB:3EJJ}.
HELIX 119 122 {ECO:0000244|PDB:3EJJ}.
TURN 131 134 {ECO:0000244|PDB:3EJJ}.
STRAND 135 140 {ECO:0000244|PDB:3EJJ}.
HELIX 142 162 {ECO:0000244|PDB:3EJJ}.
TURN 164 167 {ECO:0000244|PDB:3EJJ}.
HELIX 172 177 {ECO:0000244|PDB:3EJJ}.
SEQUENCE 552 AA; 60649 MW; 3886D72D70E770AF CRC64;
MTARGAAGRC PSSTWLGSRL LLVCLLMSRS IAKEVSEHCS HMIGNGHLKV LQQLIDSQME
TSCQIAFEFV DQEQLDDPVC YLKKAFFLVQ DIIDETMRFK DNTPNANATE RLQELSNNLN
SCFTKDYEEQ NKACVRTFHE TPLQLLEKIK NFFNETKNLL EKDWNIFTKN CNNSFAKCSS
RDVVTKPDCN CLYPKATPSS DPASASPHQP PAPSMAPLAG LAWDDSQRTE GSSLLPSELP
LRIEDPGSAK QRPPRSTCQT LESTEQPNHG DRLTEDSQPH PSAGGPVPGV EDILESSLGT
NWVLEEASGE ASEGFLTQEA KFSPSTPVGG SIQAETDRPR ALSASPFPKS TEDQKPVDIT
DRPLTEVNPM RPIGQTQNNT PEKTDGTSTL REDHQEPGSP HIATPNPQRV SNSATPVAQL
LLPKSHSWGI VLPLGELEGK RSTRDRRSPA ELEGGSASEG AARPVARFNS IPLTDTGHVE
QHEGSSDPQI PESVFHLLVP GIILVLLTVG GLLFYKWKWR SHRDPQTLDS SVGRPEDSSL
TQDEDRQVEL PV


Related products :

Catalog number Product name Quantity
orb82742 Human MCSF protein Macrophage Colony Stimulating Factor (MCSF) is a four alpha helical bundle cytokine that is the primary regulator of macrophage survival, proliferation and differentiation. MCSF is 1 mg
20-663-48028 Granulocyte Macrophage Colony Stimulating Factor (mAHuGM-CSF) - Mouse Anti-Human Granulocyte Macrophage Colony Stimulating Factor (mAHuGM-CSF); GM-CSF; Colony-stimulating factor; CSF; Sargramostim; Mo 1 mg
20-663-48028 Granulocyte Macrophage Colony Stimulating Factor (mAHuGM-CSF) - Mouse Anti-Human Granulocyte Macrophage Colony Stimulating Factor (mAHuGM-CSF); GM-CSF; Colony-stimulating factor; CSF; Sargramostim; Mo 0.5 mg
RF0036- Granulocyte-macrophage colony-stimulating factor (GM-CSF), Colony-stimulating factor (CSF), Molgramostin, Sargramostim, rHuman GM-CSF (Granulocyte-macrophage colony-stimulating factor ) 50ug
RF0036- Granulocyte-macrophage colony-stimulating factor (GM-CSF), Colony-stimulating factor (CSF), Molgramostin, Sargramostim, rHuman GM-CSF (Granulocyte-macrophage colony-stimulating factor ) 100ug
RF0036- Granulocyte-macrophage colony-stimulating factor (GM-CSF), Colony-stimulating factor (CSF), Molgramostin, Sargramostim, rHuman GM-CSF (Granulocyte-macrophage colony-stimulating factor ) 10ug
RF0036-10 rHuman GM-CSF (Granulocyte-macrophage colony-stimulating factor ); Granulocyte-macrophage colony-stimulating factor (GM-CSF), Colony-stimulating factor (CSF), Molgramostin, Sargramostim 10ug
RF0036-20 rHuman GM-CSF (Granulocyte-macrophage colony-stimulating factor ); Granulocyte-macrophage colony-stimulating factor (GM-CSF), Colony-stimulating factor (CSF), Molgramostin, Sargramostim 20ug
RF0036-50 rHuman GM-CSF (Granulocyte-macrophage colony-stimulating factor ); Granulocyte-macrophage colony-stimulating factor (GM-CSF), Colony-stimulating factor (CSF), Molgramostin, Sargramostim 50ug
RF0036-100 rHuman GM-CSF (Granulocyte-macrophage colony-stimulating factor ); Granulocyte-macrophage colony-stimulating factor (GM-CSF), Colony-stimulating factor (CSF), Molgramostin, Sargramostim 100ug
RF0036- Granulocyte-macrophage colony-stimulating factor (GM-CSF), Colony-stimulating factor (CSF), Molgramostin, Sargramostim, rHuman GM-CSF (Granulocyte-macrophage colony-stimulating factor ) 20ug
139-13613 Macrophage Colony Stimulating Factor (M_CSF), Human, recombinant Source Human macrophage colony stimulating factor cDNA expressed in E.coli Appearance Lyophilized powder Molecularweight 36,800 (dim 50 ug
PNb-032 GM-CSF Human Host: Nicotiana benthamiana CSF2; GMCSF Granulocyte-macrophage colony-stimulating factor (GM-CSF), Colony-stimulating factor (CSF), Molgramostin, Sargramostim 10
PNb-033 GM-CSF Human Host: Nicotiana benthamiana CSF2; GMCSF Granulocyte-macrophage colony-stimulating factor (GM-CSF), Colony-stimulating factor (CSF), Molgramostin, Sargramostim 20
PNb-034 GM-CSF Human Host: Nicotiana benthamiana CSF2; GMCSF Granulocyte-macrophage colony-stimulating factor (GM-CSF), Colony-stimulating factor (CSF), Molgramostin, Sargramostim 50
E0045h ELISA Colony-stimulating factor,CSF,CSF2,GMCSF,GM-CSF,Granulocyte-macrophage colony-stimulating factor,Homo sapiens,Human,Molgramostin,Sargramostim 96T
U0045h CLIA Colony-stimulating factor,CSF,CSF2,GMCSF,GM-CSF,Granulocyte-macrophage colony-stimulating factor,Homo sapiens,Human,Molgramostin,Sargramostim 96T
E0045h ELISA kit Colony-stimulating factor,CSF,CSF2,GMCSF,GM-CSF,Granulocyte-macrophage colony-stimulating factor,Homo sapiens,Human,Molgramostin,Sargramostim 96T
20-321-175015 GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR (GM-CSF) - MONOCLONAL ANTIBODY TO MOUSE GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR (GM-CSF); GM-CSF; Colony-stimulating factor; CSF Monoclonal 0.5 mg
20-321-175014 GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR (GM-CSF) - MONOCLONAL ANTIBODY TO MOUSE GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR (GM-CSF); GM-CSF; Colony-stimulating factor; CSF Monoclonal 0.1 mg
20-321-175012 GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR (GM-CSF) - MONOCLONAL ANTIBODY TO MOUSE GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR (GM-CSF); GM-CSF; Colony-stimulating factor; CSF Monoclonal 0.1 mg
DL-MCSF-Mu Mouse Colony Stimulating Factor 1, Macrophage (MCSF) ELISA Kit 96T
DL-MCSF-Hu Human Colony Stimulating Factor 1, Macrophage (MCSF) ELISA Kit 96T
U0045m CLIA Colony-stimulating factor,CSF,Csf2,Csfgm,GM-CSF,Granulocyte-macrophage colony-stimulating factor,Mouse,Mus musculus 96T
E0045r ELISA kit Colony-stimulating factor,CSF,Csf2,Csfgm,GM-CSF,Granulocyte-macrophage colony-stimulating factor,Rat,Rattus norvegicus 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