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Myoblast determination protein 1

 MYOD1_MOUSE             Reviewed;         318 AA.
P10085; Q8C6B1;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
23-MAY-2018, entry version 183.
RecName: Full=Myoblast determination protein 1;
Name=Myod1; Synonyms=Myod;
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=3690668; DOI=10.1016/0092-8674(87)90585-X;
Davis R.L., Weintraub H., Lassar A.B.;
"Expression of a single transfected cDNA converts fibroblasts to
myoblasts.";
Cell 51:987-1000(1987).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=1754380; DOI=10.1093/nar/19.23.6433;
Zingg J.-M., Alva G.P., Jost J.-P.;
"Characterisation of a genomic clone covering the structural mouse
MyoD1 gene and its promoter region.";
Nucleic Acids Res. 19:6433-6439(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3286015; DOI=10.1016/0092-8674(88)90095-5;
Pinney D.F., Pearson-White S.H., Konieczny S.F., Latham K.E.,
Emerson C.P. Jr.;
"Myogenic lineage determination and differentiation: evidence for a
regulatory gene pathway.";
Cell 53:781-793(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Head;
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 MRNA].
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).
[6]
FUNCTION.
PubMed=3175662; DOI=10.1126/science.3175662;
Tapscott S.J., Davis R.L., Thayer M.J., Cheng P.-F., Weintraub H.,
Lassar A.B.;
"MyoD1: a nuclear phosphoprotein requiring a Myc homology region to
convert fibroblasts to myoblasts.";
Science 242:405-411(1988).
[7]
ACETYLATION.
PubMed=9029156; DOI=10.1093/emboj/16.2.369;
Puri P.L., Avantaggiati M.L., Balsano C., Sang N., Graessmann A.,
Giordano A., Levrero M.;
"p300 is required for MyoD-dependent cell cycle arrest and muscle-
specific gene transcription.";
EMBO J. 16:369-383(1997).
[8]
INHIBITION BY TWIST.
PubMed=9343420; DOI=10.1128/MCB.17.11.6563;
Hamamori Y., Wu H.Y., Sartorelli V., Kedes L.;
"The basic domain of myogenic basic helix-loop-helix (bHLH) proteins
is the novel target for direct inhibition by another bHLH protein,
Twist.";
Mol. Cell. Biol. 17:6563-6573(1997).
[9]
REVIEW ON ACETYLATION/DEACETYLATION.
PubMed=11532390; DOI=10.1016/S0959-437X(00)00224-0;
McKinsey T.A., Zhang C.L., Olson E.N.;
"Control of muscle development by dueling HATs and HDACs.";
Curr. Opin. Genet. Dev. 11:497-504(2001).
[10]
INTERACTION WITH P-TEFB COMPLEX.
PubMed=12037670; DOI=10.1038/sj.onc.1205493;
Simone C., Stiegler P., Bagella L., Pucci B., Bellan C., De Falco G.,
De Luca A., Guanti G., Puri P.L., Giordano A.;
"Activation of MyoD-dependent transcription by cdk9/cyclin T2.";
Oncogene 21:4137-4148(2002).
[11]
DEACETYLATION BY SIRT1.
PubMed=12887892; DOI=10.1016/S1097-2765(03)00226-0;
Fulco M., Schiltz R.L., Iezzi S., King M.T., Zhao P., Kashiwaya Y.,
Hoffman E., Veech R.L., Sartorelli V.;
"Sir2 regulates skeletal muscle differentiation as a potential sensor
of the redox state.";
Mol. Cell 12:51-62(2003).
[12]
INTERACTION WITH DDX5.
PubMed=17011493; DOI=10.1016/j.devcel.2006.08.003;
Caretti G., Schiltz R.L., Dilworth F.J., Di Padova M., Zhao P.,
Ogryzko V., Fuller-Pace F.V., Hoffman E.P., Tapscott S.J.,
Sartorelli V.;
"The RNA helicases p68/p72 and the noncoding RNA SRA are coregulators
of MyoD and skeletal muscle differentiation.";
Dev. Cell 11:547-560(2006).
[13]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=16901893; DOI=10.1074/jbc.M605445200;
Wilson E.M., Rotwein P.;
"Control of MyoD function during initiation of muscle differentiation
by an autocrine signaling pathway activated by insulin-like growth
factor-II.";
J. Biol. Chem. 281:29962-29971(2006).
[14]
INTERACTION WITH TSC22D3.
STRAIN=DBA/2J; TISSUE=Myoblast;
PubMed=20124407; DOI=10.1074/jbc.M109.070136;
Bruscoli S., Donato V., Velardi E., Di Sante M., Migliorati G.,
Donato R., Riccardi C.;
"Glucocorticoid-induced leucine zipper (GILZ) and long GILZ inhibit
myogenic differentiation and mediate anti-myogenic effects of
glucocorticoids.";
J. Biol. Chem. 285:10385-10396(2010).
[15]
INTERACTION WITH SETD3.
PubMed=21832073; DOI=10.1074/jbc.M110.203307;
Eom G.H., Kim K.B., Kim J.H., Kim J.Y., Kim J.R., Kee H.J., Kim D.W.,
Choe N., Park H.J., Son H.J., Choi S.Y., Kook H., Seo S.B.;
"Histone methyltransferase SETD3 regulates muscle differentiation.";
J. Biol. Chem. 286:34733-34742(2011).
[16]
FUNCTION, AND PROMOTER BINDING.
PubMed=21798092; DOI=10.1186/2044-5040-1-14;
Londhe P., Davie J.K.;
"Sequential association of myogenic regulatory factors and E proteins
at muscle-specific genes.";
Skelet. Muscle 1:14-14(2011).
[17]
INTERACTION WITH CHD2.
PubMed=22569126; DOI=10.1038/emboj.2012.136;
Harada A., Okada S., Konno D., Odawara J., Yoshimi T., Yoshimura S.,
Kumamaru H., Saiwai H., Tsubota T., Kurumizaka H., Akashi K.,
Tachibana T., Imbalzano A.N., Ohkawa Y.;
"Chd2 interacts with H3.3 to determine myogenic cell fate.";
EMBO J. 31:2994-3007(2012).
[18]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 102-166.
PubMed=8181063; DOI=10.1016/0092-8674(94)90159-7;
Ma P.C.M., Rould M.A., Weintraub H., Pabo C.O.;
"Crystal structure of MyoD bHLH domain-DNA complex: perspectives on
DNA recognition and implications for transcriptional activation.";
Cell 77:451-459(1994).
-!- FUNCTION: Acts as a transcriptional activator that promotes
transcription of muscle-specific target genes and plays a role in
muscle differentiation (PubMed:16901893). Together with MYF5 and
MYOG, co-occupies muscle-specific gene promoter core region during
myogenesis. Induces fibroblasts to differentiate into myoblasts.
Interacts with and is inhibited by the twist protein. This
interaction probably involves the basic domains of both proteins
(PubMed:21798092, PubMed:3175662). {ECO:0000269|PubMed:16901893,
ECO:0000269|PubMed:21798092, ECO:0000269|PubMed:3175662}.
-!- SUBUNIT: Interacts with SUV39H1 (By similarity). Efficient DNA
binding requires dimerization with another bHLH protein. Seems to
form active heterodimers with ITF-2. Interacts with DDX5.
Interacts with CHD2. Interacts with TSC22D3 isoform 1 and isoform
4. Interacts with SETD3 (PubMed:21832073). Interacts with P-TEFB
complex; promotes the transcriptional activity of MYOD1 through
its CDK9-mediated phosphorylation (PubMed:12037670). Interacts
with CSRP3 (By similarity). {ECO:0000250|UniProtKB:P15172,
ECO:0000269|PubMed:12037670, ECO:0000269|PubMed:17011493,
ECO:0000269|PubMed:20124407, ECO:0000269|PubMed:21832073,
ECO:0000269|PubMed:22569126}.
-!- INTERACTION:
P50463:Csrp3 (xeno); NbExp=3; IntAct=EBI-4405734, EBI-12502290;
P17844:DDX5 (xeno); NbExp=3; IntAct=EBI-4405734, EBI-351962;
Q92993:KAT5 (xeno); NbExp=5; IntAct=EBI-4405734, EBI-399080;
Q8VIM5-1:Myocd; NbExp=2; IntAct=EBI-4405734, EBI-15626132;
Q6P9Z1:Smarcd3; NbExp=6; IntAct=EBI-4405734, EBI-7525857;
O54864:Suv39h1; NbExp=3; IntAct=EBI-4405734, EBI-302230;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16901893}.
-!- PTM: Acetylated by a complex containing EP300 and PCAF. The
acetylation is essential to activate target genes. Conversely, its
deacetylation by SIRT1 inhibits its function.
{ECO:0000269|PubMed:9029156}.
-!- PTM: Ubiquitinated on the N-terminus; which is required for
proteasomal degradation. {ECO:0000250}.
-!- PTM: Phosphorylated by CDK9. This phosphorylation promotes its
function in muscle differentiation (By similarity). {ECO:0000250}.
-!- PTM: Methylation at Lys-104 by EHMT2/G9a inhibits myogenic
activity. {ECO:0000250}.
-----------------------------------------------------------------------
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EMBL; M18779; AAA39799.1; -; mRNA.
EMBL; X61655; CAA43836.1; -; Genomic_DNA.
EMBL; M84918; AAA39798.1; -; mRNA.
EMBL; AK076157; BAC36224.1; -; mRNA.
EMBL; AK142859; BAE25213.1; -; mRNA.
EMBL; BC103613; AAI03614.1; -; mRNA.
EMBL; BC103618; AAI03619.1; -; mRNA.
EMBL; BC103619; AAI03620.1; -; mRNA.
CCDS; CCDS21277.1; -.
PIR; A29636; A29636.
RefSeq; NP_034996.2; NM_010866.2.
UniGene; Mm.1526; -.
PDB; 1MDY; X-ray; 2.80 A; A=102-166, B/C/D=105-166.
PDBsum; 1MDY; -.
ProteinModelPortal; P10085; -.
SMR; P10085; -.
BioGrid; 201673; 30.
CORUM; P10085; -.
DIP; DIP-37N; -.
ELM; P10085; -.
IntAct; P10085; 18.
MINT; P10085; -.
STRING; 10090.ENSMUSP00000072330; -.
iPTMnet; P10085; -.
PhosphoSitePlus; P10085; -.
PaxDb; P10085; -.
PRIDE; P10085; -.
Ensembl; ENSMUST00000072514; ENSMUSP00000072330; ENSMUSG00000009471.
GeneID; 17927; -.
KEGG; mmu:17927; -.
UCSC; uc012fkv.1; mouse.
CTD; 4654; -.
MGI; MGI:97275; Myod1.
eggNOG; KOG3960; Eukaryota.
eggNOG; ENOG4111SED; LUCA.
GeneTree; ENSGT00530000063004; -.
HOGENOM; HOG000234800; -.
HOVERGEN; HBG006429; -.
InParanoid; P10085; -.
KO; K09064; -.
OMA; PNPIYQV; -.
OrthoDB; EOG091G0GKD; -.
TreeFam; TF316344; -.
Reactome; R-MMU-375170; CDO in myogenesis.
EvolutionaryTrace; P10085; -.
PRO; PR:P10085; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000009471; -.
CleanEx; MM_MYOD1; -.
Genevisible; P10085; MM.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0030016; C:myofibril; IDA:MGI.
GO; GO:0016604; C:nuclear body; ISO:MGI.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005667; C:transcription factor complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0001047; F:core promoter binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:MGI.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0035257; F:nuclear hormone receptor binding; ISO:MGI.
GO; GO:1990841; F:promoter-specific chromatin binding; IDA:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; ISO:MGI.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; TAS:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0001077; F:transcriptional activator activity, RNA polymerase II proximal promoter sequence-specific DNA binding; IC:NTNU_SB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:MGI.
GO; GO:0055007; P:cardiac muscle cell differentiation; NAS:UniProtKB.
GO; GO:0071392; P:cellular response to estradiol stimulus; IDA:UniProtKB.
GO; GO:0071385; P:cellular response to glucocorticoid stimulus; IDA:MGI.
GO; GO:0071453; P:cellular response to oxygen levels; IDA:MGI.
GO; GO:0009267; P:cellular response to starvation; IDA:MGI.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:MGI.
GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
GO; GO:0007517; P:muscle organ development; IDA:MGI.
GO; GO:0045445; P:myoblast differentiation; IDA:MGI.
GO; GO:0007518; P:myoblast fate determination; IDA:MGI.
GO; GO:0007520; P:myoblast fusion; IMP:MGI.
GO; GO:0014904; P:myotube cell development; ISO:MGI.
GO; GO:0014902; P:myotube differentiation; IDA:MGI.
GO; GO:0014908; P:myotube differentiation involved in skeletal muscle regeneration; IMP:MGI.
GO; GO:2000818; P:negative regulation of myoblast proliferation; IMP:MGI.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; IDA:UniProtKB.
GO; GO:0045663; P:positive regulation of myoblast differentiation; IBA:GO_Central.
GO; GO:1901741; P:positive regulation of myoblast fusion; ISO:MGI.
GO; GO:0048743; P:positive regulation of skeletal muscle fiber development; IBA:GO_Central.
GO; GO:0043415; P:positive regulation of skeletal muscle tissue regeneration; IMP:MGI.
GO; GO:1905382; P:positive regulation of snRNA transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IDA:MGI.
GO; GO:0010468; P:regulation of gene expression; IDA:CACAO.
GO; GO:0043484; P:regulation of RNA splicing; ISO:MGI.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0035914; P:skeletal muscle cell differentiation; IMP:MGI.
GO; GO:0043503; P:skeletal muscle fiber adaptation; IMP:MGI.
GO; GO:0048741; P:skeletal muscle fiber development; IMP:MGI.
GO; GO:0007519; P:skeletal muscle tissue development; IDA:MGI.
GO; GO:0051146; P:striated muscle cell differentiation; IMP:MGI.
CDD; cd00083; HLH; 1.
Gene3D; 4.10.280.10; -; 1.
InterPro; IPR002546; Basic.
InterPro; IPR011598; bHLH_dom.
InterPro; IPR036638; HLH_DNA-bd_sf.
InterPro; IPR022032; Myf5.
Pfam; PF01586; Basic; 1.
Pfam; PF00010; HLH; 1.
Pfam; PF12232; Myf5; 1.
SMART; SM00520; BASIC; 1.
SMART; SM00353; HLH; 1.
SUPFAM; SSF47459; SSF47459; 1.
PROSITE; PS50888; BHLH; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Complete proteome;
Developmental protein; Differentiation; DNA-binding; Methylation;
Myogenesis; Nucleus; Phosphoprotein; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 318 Myoblast determination protein 1.
/FTId=PRO_0000127361.
DOMAIN 109 160 bHLH. {ECO:0000255|PROSITE-
ProRule:PRU00981}.
MOD_RES 104 104 N6-methyllysine; by EHMT2.
{ECO:0000250|UniProtKB:P15172}.
CROSSLNK 1 1 Peptide (Met-Gly) (interchain with G-Cter
in ubiquitin). {ECO:0000250}.
CONFLICT 53 53 M -> V (in Ref. 1; AAA39799, 2; CAA43836
and 3; AAA39798). {ECO:0000305}.
CONFLICT 66 66 P -> S (in Ref. 1; AAA39799, 2; CAA43836
and 3; AAA39798). {ECO:0000305}.
CONFLICT 234 234 A -> V (in Ref. 1; AAA39799, 2; CAA43836
and 3; AAA39798). {ECO:0000305}.
HELIX 106 133 {ECO:0000244|PDB:1MDY}.
HELIX 146 162 {ECO:0000244|PDB:1MDY}.
SEQUENCE 318 AA; 34233 MW; AEC6572277A78D54 CRC64;
MELLSPPLRD IDLTGPDGSL CSFETADDFY DDPCFDSPDL RFFEDLDPRL VHMGALLKPE
EHAHFPTAVH PGPGAREDEH VRAPSGHHQA GRCLLWACKA CKRKTTNADR RKAATMRERR
RLSKVNEAFE TLKRCTSSNP NQRLPKVEIL RNAIRYIEGL QALLRDQDAA PPGAAAFYAP
GPLPPGRGSE HYSGDSDASS PRSNCSDGMM DYSGPPSGPR RQNGYDTAYY SEAARESRPG
KSAAVSSLDC LSSIVERIST DSPAAPALLL ADAPPESPPG PPEGASLSDT EQGTQTPSPD
AAPQCPAGSN PNAIYQVL


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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




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