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

Mothers against decapentaplegic homolog 5 (MAD homolog 5) (Mothers against DPP homolog 5) (Dwarfin-C) (Dwf-C) (SMAD family member 5) (SMAD 5) (Smad5) (mSmad5)

 SMAD5_MOUSE             Reviewed;         465 AA.
P97454; P70341; Q810K0;
04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
04-MAY-2001, sequence version 2.
27-SEP-2017, entry version 166.
RecName: Full=Mothers against decapentaplegic homolog 5;
Short=MAD homolog 5;
Short=Mothers against DPP homolog 5;
AltName: Full=Dwarfin-C;
Short=Dwf-C;
AltName: Full=SMAD family member 5;
Short=SMAD 5;
Short=Smad5;
Short=mSmad5;
Name=Smad5; Synonyms=Madh5, Msmad5;
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=8799132; DOI=10.1073/pnas.93.17.8940;
Yingling J.M., Das P., Savage C., Zhang M., Padgett R.W., Wang X.-F.;
"Mammalian dwarfins are phosphorylated in response to transforming
growth factor beta and are implicated in control of cell growth.";
Proc. Natl. Acad. Sci. U.S.A. 93:8940-8944(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9076683; DOI=10.1016/S0925-4773(96)00629-6;
Meersseman G., Verschueren K., Nelles L., Blumenstock C., Kraft H.,
Wuytens G., Remacle J., Kozak C.A., Tylzanowski P., Niehrs C.,
Huylebroeck D.;
"The C-terminal domain of Mad-like signal transducers is sufficient
for biological activity in the Xenopus embryo and transcriptional
activation.";
Mech. Dev. 61:127-140(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=129/Sv;
Chang H., Kraft H., Verschueren K., Wang P., Huylebroeck D.,
Matzuk M.M.;
"Genomic organization and expression of mouse Smad5.";
Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=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 MRNA].
TISSUE=Eye;
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]
REVIEW.
PubMed=10708952; DOI=10.1016/S1359-6101(99)00028-3;
Weinstein M., Yang X., Deng C.-X.;
"Functions of mammalian Smad genes as revealed by targeted gene
disruption in mice.";
Cytokine Growth Factor Rev. 11:49-58(2000).
[7]
INTERACTION WITH ZNF8.
PubMed=12370310; DOI=10.1128/MCB.22.21.7633-7644.2002;
Jiao K., Zhou Y., Hogan B.L.M.;
"Identification of mZnf8, a mouse Kruppel-like transcriptional
repressor, as a novel nuclear interaction partner of Smad1.";
Mol. Cell. Biol. 22:7633-7644(2002).
[8]
INTERACTION WITH WWP1.
PubMed=15221015; DOI=10.1038/sj.onc.1207885;
Komuro A., Imamura T., Saitoh M., Yoshida Y., Yamori T., Miyazono K.,
Miyazawa K.;
"Negative regulation of transforming growth factor-beta (TGF-beta)
signaling by WW domain-containing protein 1 (WWP1).";
Oncogene 23:6914-6923(2004).
[9]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[10]
INTERACTION WITH TMEM119.
PubMed=21239498; DOI=10.1074/jbc.M110.179127;
Hisa I., Inoue Y., Hendy G.N., Canaff L., Kitazawa R., Kitazawa S.,
Komori T., Sugimoto T., Seino S., Kaji H.;
"Parathyroid hormone-responsive Smad3-related factor, Tmem119,
promotes osteoblast differentiation and interacts with the bone
morphogenetic protein-Runx2 pathway.";
J. Biol. Chem. 286:9787-9796(2011).
-!- FUNCTION: Transcriptional modulator activated by BMP (bone
morphogenetic proteins) type 1 receptor kinase. SMAD5 is a
receptor-regulated SMAD (R-SMAD) (By similarity). Required for
angiogenesis. {ECO:0000250}.
-!- SUBUNIT: May form trimers with the co-SMAD SMAD4. Interacts with
PEBP2-alpha subunit and SMURF1. Interacts with SUV39H1 and
SUV39H2. Interacts (via MH2 domain) with LEMD3 (By similarity).
Interacts with WWP1. Interacts with TMEM119 (PubMed:21239498).
Interacts with ZNF8 (PubMed:12370310). Interacts with RANBP3L (By
similarity). {ECO:0000250|UniProtKB:Q99717,
ECO:0000269|PubMed:12370310, ECO:0000269|PubMed:15221015,
ECO:0000269|PubMed:21239498}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus
{ECO:0000250}. Note=In the cytoplasm in the absence of ligand.
Migration to the nucleus when complexed with SMAD4 (By
similarity). {ECO:0000250}.
-!- PTM: Phosphorylated on serine by BMP (bone morphogenetic proteins)
type 1 receptor kinase.
-!- PTM: Ubiquitin-mediated proteolysis by SMAD-specific E3 ubiquitin
ligase SMURF1. {ECO:0000250}.
-!- SIMILARITY: Belongs to the dwarfin/SMAD family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; U58993; AAB07871.1; -; mRNA.
EMBL; U77638; AAB39737.1; -; mRNA.
EMBL; AF063006; AAC83580.1; -; mRNA.
EMBL; AK082997; BAC38724.1; -; mRNA.
EMBL; BC050001; AAH50001.2; -; mRNA.
CCDS; CCDS26565.1; -.
RefSeq; NP_001157513.1; NM_001164041.1.
RefSeq; NP_001157514.1; NM_001164042.1.
RefSeq; NP_032567.1; NM_008541.3.
RefSeq; XP_006517180.1; XM_006517117.1.
RefSeq; XP_006517181.1; XM_006517118.3.
UniGene; Mm.272920; -.
PDB; 5X6G; X-ray; 3.05 A; A/B=1-143.
PDB; 5X6H; X-ray; 3.10 A; B=1-143.
PDB; 5X6M; X-ray; 3.20 A; A/B/E/F=1-143.
PDBsum; 5X6G; -.
PDBsum; 5X6H; -.
PDBsum; 5X6M; -.
ProteinModelPortal; P97454; -.
SMR; P97454; -.
BioGrid; 201278; 13.
IntAct; P97454; 2.
MINT; MINT-99279; -.
STRING; 10090.ENSMUSP00000065798; -.
iPTMnet; P97454; -.
PhosphoSitePlus; P97454; -.
MaxQB; P97454; -.
PaxDb; P97454; -.
PeptideAtlas; P97454; -.
PRIDE; P97454; -.
Ensembl; ENSMUST00000069557; ENSMUSP00000065798; ENSMUSG00000021540.
Ensembl; ENSMUST00000109874; ENSMUSP00000105500; ENSMUSG00000021540.
Ensembl; ENSMUST00000109876; ENSMUSP00000105502; ENSMUSG00000021540.
GeneID; 17129; -.
KEGG; mmu:17129; -.
UCSC; uc007qsw.2; mouse.
CTD; 4090; -.
MGI; MGI:1328787; Smad5.
eggNOG; KOG3701; Eukaryota.
eggNOG; ENOG410XQKU; LUCA.
GeneTree; ENSGT00760000119091; -.
HOGENOM; HOG000286018; -.
HOVERGEN; HBG053353; -.
InParanoid; P97454; -.
KO; K16790; -.
OMA; DVQPVEY; -.
OrthoDB; EOG091G082C; -.
PhylomeDB; P97454; -.
TreeFam; TF314923; -.
Reactome; R-MMU-201451; Signaling by BMP.
PRO; PR:P97454; -.
Proteomes; UP000000589; Chromosome 13.
Bgee; ENSMUSG00000021540; -.
CleanEx; MM_SMAD5; -.
Genevisible; P97454; MM.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0043234; C:protein complex; ISO:MGI.
GO; GO:0005667; C:transcription factor complex; IEA:InterPro.
GO; GO:0017151; F:DEAD/H-box RNA helicase binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0000979; F:RNA polymerase II core promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000983; F:transcription factor activity, RNA polymerase II core promoter sequence-specific; IC:NTNU_SB.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IC:NTNU_SB.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
GO; GO:0060348; P:bone development; IGI:MGI.
GO; GO:0060048; P:cardiac muscle contraction; IMP:MGI.
GO; GO:0051216; P:cartilage development; IGI:MGI.
GO; GO:0071773; P:cellular response to BMP stimulus; IGI:BHF-UCL.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
GO; GO:0009880; P:embryonic pattern specification; ISS:UniProtKB.
GO; GO:0030218; P:erythrocyte differentiation; IMP:MGI.
GO; GO:0007281; P:germ cell development; IMP:MGI.
GO; GO:0001880; P:Mullerian duct regression; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:NTNU_SB.
GO; GO:0002051; P:osteoblast fate commitment; IGI:MGI.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IGI:MGI.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:MGI.
GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; IGI:BHF-UCL.
GO; GO:0006468; P:protein phosphorylation; IDA:MGI.
GO; GO:0060395; P:SMAD protein signal transduction; IGI:BHF-UCL.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IDA:MGI.
GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
Gene3D; 2.60.200.10; -; 1.
Gene3D; 3.90.520.10; -; 1.
InterPro; IPR013790; Dwarfin.
InterPro; IPR003619; MAD_homology1_Dwarfin-type.
InterPro; IPR013019; MAD_homology_MH1.
InterPro; IPR017855; SMAD_dom-like.
InterPro; IPR001132; SMAD_dom_Dwarfin-type.
InterPro; IPR008984; SMAD_FHA_domain.
PANTHER; PTHR13703; PTHR13703; 1.
Pfam; PF03165; MH1; 1.
Pfam; PF03166; MH2; 1.
SMART; SM00523; DWA; 1.
SMART; SM00524; DWB; 1.
SUPFAM; SSF49879; SSF49879; 1.
SUPFAM; SSF56366; SSF56366; 1.
PROSITE; PS51075; MH1; 1.
PROSITE; PS51076; MH2; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Angiogenesis; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; DNA-binding; Metal-binding;
Nucleus; Phosphoprotein; Reference proteome; Transcription;
Transcription regulation; Zinc.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q99717}.
CHAIN 2 465 Mothers against decapentaplegic homolog
5.
/FTId=PRO_0000090866.
DOMAIN 13 137 MH1. {ECO:0000255|PROSITE-
ProRule:PRU00438}.
DOMAIN 271 465 MH2. {ECO:0000255|PROSITE-
ProRule:PRU00439}.
COMPBIAS 40 46 Poly-Lys.
METAL 65 65 Zinc. {ECO:0000250}.
METAL 110 110 Zinc. {ECO:0000250}.
METAL 122 122 Zinc. {ECO:0000250}.
METAL 127 127 Zinc. {ECO:0000250}.
MOD_RES 2 2 N-acetylthreonine.
{ECO:0000250|UniProtKB:Q99717}.
MOD_RES 463 463 Phosphoserine.
{ECO:0000250|UniProtKB:Q99717,
ECO:0000255|PROSITE-ProRule:PRU00439}.
MOD_RES 465 465 Phosphoserine.
{ECO:0000250|UniProtKB:Q99717,
ECO:0000255|PROSITE-ProRule:PRU00439}.
CONFLICT 196 196 S -> P (in Ref. 2; AAB39737).
{ECO:0000305}.
HELIX 13 20 {ECO:0000244|PDB:5X6G}.
HELIX 26 42 {ECO:0000244|PDB:5X6G}.
HELIX 48 57 {ECO:0000244|PDB:5X6G}.
STRAND 59 61 {ECO:0000244|PDB:5X6G}.
STRAND 67 69 {ECO:0000244|PDB:5X6G}.
STRAND 72 74 {ECO:0000244|PDB:5X6G}.
STRAND 76 78 {ECO:0000244|PDB:5X6G}.
STRAND 81 83 {ECO:0000244|PDB:5X6G}.
HELIX 85 93 {ECO:0000244|PDB:5X6G}.
HELIX 101 103 {ECO:0000244|PDB:5X6G}.
STRAND 104 106 {ECO:0000244|PDB:5X6G}.
STRAND 110 112 {ECO:0000244|PDB:5X6H}.
HELIX 114 116 {ECO:0000244|PDB:5X6G}.
STRAND 119 122 {ECO:0000244|PDB:5X6G}.
HELIX 125 127 {ECO:0000244|PDB:5X6G}.
STRAND 128 130 {ECO:0000244|PDB:5X6G}.
SEQUENCE 465 AA; 52172 MW; D66B638DA76BC20B CRC64;
MTSMASLFSF TSPAVKRLLG WKQGDEEEKW AEKAVDALVK KLKKKKGAME ELEKALSSPG
QPSKCVTIPR SLDGRLQVSH RKGLPHVIYC RVWRWPDLQS HHELKPLDIC EFPFGSKQKE
VCINPYHYKR VESPVLPPVL VPRHNEFNPQ HSLLVQFRNL SHNEPHMPQN ATFPDSFHQP
NNAPFPLSPN SPYPPSPASS TYPNSPASSG PGSPFQLPAD TPPPAYMPPD DQMAPDNSQP
MDTSSNMIPQ TMPSISSRDV QPVAYEEPKH WCSIVYYELN NRVGEAFHAS STSVLVDGFT
DPSNNKSRFC LGLLSNVNRN STIENTRRHI GKGVHLYYVG GEVYAECLSD SSIFVQSRNC
NFHHGFHPTT VCKIPSSCSL KIFNNQEFAQ LLAQSVNHGF EAVYELTKMC TIRMSFVKGW
GAEYHRQDVT STPCWIEIHL HGPLQWLDKV LTQMGSPLNP ISSVS


Related products :

Catalog number Product name Quantity
E2186m ELISA Dwarfin-C,Dwf-C,MAD homolog 5,Madh5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,Mouse,mSmad5,Msmad5,Mus musculus,SMAD 5,SMAD family member 5,Smad5,Smad5 96T
U2186m CLIA Dwarfin-C,Dwf-C,MAD homolog 5,Madh5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,Mouse,mSmad5,Msmad5,Mus musculus,SMAD 5,SMAD family member 5,Smad5,Smad5 96T
U2186m CLIA kit Dwarfin-C,Dwf-C,MAD homolog 5,Madh5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,Mouse,mSmad5,Msmad5,Mus musculus,SMAD 5,SMAD family member 5,Smad5,Smad5 96T
E2186m ELISA kit Dwarfin-C,Dwf-C,MAD homolog 5,Madh5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,Mouse,mSmad5,Msmad5,Mus musculus,SMAD 5,SMAD family member 5,Smad5,Smad5 96T
E2186m Dwarfin-C,Dwf-C,MAD homolog 5,Madh5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,Mouse,mSmad5,Msmad5,Mus musculus,SMAD 5,SMAD family member 5,Smad5,Smad5
U2186h CLIA kit Homo sapiens,hSmad5,Human,JV5-1,MAD homolog 5,MADH5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,SMAD 5,SMAD family member 5,Smad5,SMAD5 96T
E2186h ELISA Homo sapiens,hSmad5,Human,JV5-1,MAD homolog 5,MADH5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,SMAD 5,SMAD family member 5,Smad5,SMAD5 96T
U2186h CLIA Homo sapiens,hSmad5,Human,JV5-1,MAD homolog 5,MADH5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,SMAD 5,SMAD family member 5,Smad5,SMAD5 96T
E2186h ELISA kit Homo sapiens,hSmad5,Human,JV5-1,MAD homolog 5,MADH5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,SMAD 5,SMAD family member 5,Smad5,SMAD5 96T
E2186h Homo sapiens,hSmad5,Human,JV5-1,MAD homolog 5,MADH5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,SMAD 5,SMAD family member 5,Smad5,SMAD5
E2186r ELISA kit MAD homolog 5,Madh5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,Rat,Rattus norvegicus,SMAD 5,SMAD family member 5,Smad5,Smad5 96T
U2186r CLIA MAD homolog 5,Madh5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,Rat,Rattus norvegicus,SMAD 5,SMAD family member 5,Smad5,Smad5 96T
U2186r CLIA kit MAD homolog 5,Madh5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,Rat,Rattus norvegicus,SMAD 5,SMAD family member 5,Smad5,Smad5 96T
E2186r ELISA MAD homolog 5,Madh5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,Rat,Rattus norvegicus,SMAD 5,SMAD family member 5,Smad5,Smad5 96T
E2186r MAD homolog 5,Madh5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,Rat,Rattus norvegicus,SMAD 5,SMAD family member 5,Smad5,Smad5
U0647h CLIA BSP1,BSP-1,Homo sapiens,hSMAD1,Human,JV4-1,MAD homolog 1,MADH1,MADR1,Mad-related protein 1,Mothers against decapentaplegic homolog 1,Mothers against DPP homolog 1,SMAD 1,SMAD family member 1,Smad 96T
E2186c ELISA Chicken,Gallus gallus,MAD homolog 5,MADH5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,SMAD 5,SMAD family member 5,Smad5,SMAD5 96T
U2186c CLIA Chicken,Gallus gallus,MAD homolog 5,MADH5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,SMAD 5,SMAD family member 5,Smad5,SMAD5 96T
U2186c CLIA kit Chicken,Gallus gallus,MAD homolog 5,MADH5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,SMAD 5,SMAD family member 5,Smad5,SMAD5 96T
E2186c ELISA kit Chicken,Gallus gallus,MAD homolog 5,MADH5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,SMAD 5,SMAD family member 5,Smad5,SMAD5 96T
E2186c Chicken,Gallus gallus,MAD homolog 5,MADH5,Mothers against decapentaplegic homolog 5,Mothers against DPP homolog 5,SMAD 5,SMAD family member 5,Smad5,SMAD5
EIAAB38719 Deletion target in pancreatic carcinoma 4 homolog,Dpc4,MAD homolog 4,Madh4,Mothers against decapentaplegic homolog 4,Mothers against DPP homolog 4,Mouse,Mus musculus,SMAD 4,SMAD family member 4,Smad4,
E0647h ELISA kit BSP1,BSP-1,Homo sapiens,hSMAD1,Human,JV4-1,MAD homolog 1,MADH1,MADR1,Mad-related protein 1,Mothers against decapentaplegic homolog 1,Mothers against DPP homolog 1,SMAD 1,SMAD family member 96T
E0647h ELISA BSP1,BSP-1,Homo sapiens,hSMAD1,Human,JV4-1,MAD homolog 1,MADH1,MADR1,Mad-related protein 1,Mothers against decapentaplegic homolog 1,Mothers against DPP homolog 1,SMAD 1,SMAD family member 1,Sma 96T
U2184h CLIA kit hMAD-2,Homo sapiens,hSMAD2,Human,JV18-1,MAD homolog 2,MADH2,MADR2,Mad-related protein 2,Mothers against decapentaplegic homolog 2,Mothers against DPP homolog 2,SMAD 2,SMAD family member 2,Sm 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