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Activin receptor type-2B (EC 2.7.11.30) (Activin receptor type IIB) (ACTR-IIB)

 AVR2B_HUMAN             Reviewed;         512 AA.
Q13705; Q4VAV0;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
16-MAY-2006, sequence version 3.
22-NOV-2017, entry version 184.
RecName: Full=Activin receptor type-2B;
EC=2.7.11.30;
AltName: Full=Activin receptor type IIB;
Short=ACTR-IIB;
Flags: Precursor;
Name=ACVR2B;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=8161782;
Hilden K., Tuuri T., Eramaa M., Ritvos O.;
"Expression of type II activin receptor genes during differentiation
of human K562 cells and cDNA cloning of the human type IIB activin
receptor.";
Blood 83:2163-2170(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT ASP-459.
PubMed=9621519; DOI=10.1007/s100380050054;
Ishikawa S., Kai M., Murata Y., Tamari M., Daigo Y., Murano T.,
Ogawa M., Nakamura Y.;
"Genomic organization and mapping of the human activin receptor type
IIB (hActR-IIB) gene.";
J. Hum. Genet. 43:132-134(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING, AND VARIANTS
HTX4 HIS-40 AND ILE-494.
PubMed=9916847;
DOI=10.1002/(SICI)1096-8628(19990101)82:1<70::AID-AJMG14>3.0.CO;2-Y;
Kosaki R., Gebbia M., Kosaki K., Lewin M., Bowers P., Towbin J.A.,
Casey B.;
"Left-right axis malformations associated with mutations in ACVR2B,
the gene for human activin receptor type IIB.";
Am. J. Med. Genet. 82:70-76(1999).
[4]
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).
[5]
PHOSPHORYLATION, INTERACTION WITH ACVR1B, AND FUNCTION IN
PHOSPHORYLATION OF ACVR1B.
PubMed=8622651; DOI=10.1128/MCB.16.3.1066;
Attisano L., Wrana J.L., Montalvo E., Massague J.;
"Activation of signalling by the activin receptor complex.";
Mol. Cell. Biol. 16:1066-1073(1996).
[6]
INTERACTION WITH VPS39.
PubMed=12941698; DOI=10.1093/emboj/cdg428;
Felici A., Wurthner J.U., Parks W.T., Giam L.R., Reiss M.,
Karpova T.S., McNally J.G., Roberts A.B.;
"TLP, a novel modulator of TGF-beta signaling, has opposite effects on
Smad2- and Smad3-dependent signaling.";
EMBO J. 22:4465-4477(2003).
[7]
X-RAY CRYSTALLOGRAPHY (3.36 ANGSTROMS) OF 19-134 IN COMPLEX WITH
ACVRL1 AND BMP9, DISULFIDE BONDS, AND GLYCOSYLATION AT ASN-42 AND
ASN-65.
PubMed=22718755; DOI=10.1074/jbc.M112.377960;
Townson S.A., Martinez-Hackert E., Greppi C., Lowden P., Sako D.,
Liu J., Ucran J.A., Liharska K., Underwood K.W., Seehra J., Kumar R.,
Grinberg A.V.;
"Specificity and structure of a high affinity activin receptor-like
kinase 1 (ALK1) signaling complex.";
J. Biol. Chem. 287:27313-27325(2012).
[8]
VARIANT [LARGE SCALE ANALYSIS] ARG-176.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
-!- FUNCTION: Transmembrane serine/threonine kinase activin type-2
receptor forming an activin receptor complex with activin type-1
serine/threonine kinase receptors (ACVR1, ACVR1B or ACVR1c).
Transduces the activin signal from the cell surface to the
cytoplasm and is thus regulating many physiological and
pathological processes including neuronal differentiation and
neuronal survival, hair follicle development and cycling, FSH
production by the pituitary gland, wound healing, extracellular
matrix production, immunosuppression and carcinogenesis. Activin
is also thought to have a paracrine or autocrine role in
follicular development in the ovary. Within the receptor complex,
the type-2 receptors act as a primary activin receptors (binds
activin-A/INHBA, activin-B/INHBB as well as inhibin-A/INHA-INHBA).
The type-1 receptors like ACVR1B act as downstream transducers of
activin signals. Activin binds to type-2 receptor at the plasma
membrane and activates its serine-threonine kinase. The activated
receptor type-2 then phosphorylates and activates the type-1
receptor. Once activated, the type-1 receptor binds and
phosphorylates the SMAD proteins SMAD2 and SMAD3, on serine
residues of the C-terminal tail. Soon after their association with
the activin receptor and subsequent phosphorylation, SMAD2 and
SMAD3 are released into the cytoplasm where they interact with the
common partner SMAD4. This SMAD complex translocates into the
nucleus where it mediates activin-induced transcription.
Inhibitory SMAD7, which is recruited to ACVR1B through FKBP1A, can
prevent the association of SMAD2 and SMAD3 with the activin
receptor complex, thereby blocking the activin signal. Activin
signal transduction is also antagonized by the binding to the
receptor of inhibin-B via the IGSF1 inhibin coreceptor.
{ECO:0000269|PubMed:8622651}.
-!- CATALYTIC ACTIVITY: ATP + [receptor-protein] = ADP + [receptor-
protein] phosphate.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
-!- SUBUNIT: Forms an activin receptor complex with activin type II
receptors such as ACVR1B. Interacts with VPS39. Interacts with
DYNLT1. {ECO:0000250|UniProtKB:P27040,
ECO:0000269|PubMed:12941698, ECO:0000269|PubMed:22718755,
ECO:0000269|PubMed:8622651}.
-!- INTERACTION:
O14793:MSTN; NbExp=4; IntAct=EBI-1383577, EBI-8542977;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass
type I membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=ActR-IIB2;
IsoId=Q13705-1; Sequence=Displayed;
Name=ActR-IIB1;
IsoId=Q13705-2; Sequence=Not described;
Note=Produced from the insertion in the transcript of 82 base
pairs, leading to frameshift and protein truncation. May be not
functional.;
-!- PTM: Phosphorylated. Constitutive phosphorylation is in part
catalyzed by its own kinase activity.
{ECO:0000269|PubMed:8622651}.
-!- DISEASE: Heterotaxy, visceral, 4, autosomal (HTX4) [MIM:613751]: A
form of visceral heterotaxy, a complex disorder due to disruption
of the normal left-right asymmetry of the thoracoabdominal organs.
Visceral heterotaxy or situs ambiguus results in randomization of
the placement of visceral organs, including the heart, lungs,
liver, spleen, and stomach. The organs are oriented randomly with
respect to the left-right axis and with respect to one another. It
can been associated with variety of congenital defects including
cardiac malformations. HTX4 clinical features include
dextrocardia, right aortic arch and a right-sided spleen,
anomalies of the inferior and the superior vena cava, atrial
ventricular canal defect with dextro-transposed great arteries,
pulmonary stenosis, polysplenia and midline liver.
{ECO:0000269|PubMed:9916847}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
protein kinase family. TGFB receptor subfamily. {ECO:0000305}.
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EMBL; X77533; CAA54671.1; -; mRNA.
EMBL; AB008681; BAA24180.2; -; Genomic_DNA.
EMBL; AF060202; AAC64515.1; -; Genomic_DNA.
EMBL; AF060199; AAC64515.1; JOINED; Genomic_DNA.
EMBL; AF060200; AAC64515.1; JOINED; Genomic_DNA.
EMBL; AF060201; AAC64515.1; JOINED; Genomic_DNA.
EMBL; BC096243; AAH96243.1; -; mRNA.
EMBL; BC096244; AAH96244.1; -; mRNA.
EMBL; BC099642; AAH99642.1; -; mRNA.
CCDS; CCDS2679.1; -. [Q13705-1]
PIR; I37134; I37134.
RefSeq; NP_001097.2; NM_001106.3. [Q13705-1]
UniGene; Hs.174273; -.
PDB; 2H62; X-ray; 1.85 A; D=19-116.
PDB; 2QLU; X-ray; 2.00 A; A=190-487.
PDB; 4FAO; X-ray; 3.36 A; E/F/K/L/Q/R/W/X/e/f/k/l=19-134.
PDBsum; 2H62; -.
PDBsum; 2QLU; -.
PDBsum; 4FAO; -.
ProteinModelPortal; Q13705; -.
SMR; Q13705; -.
BioGrid; 106608; 72.
IntAct; Q13705; 6.
MINT; MINT-3028545; -.
STRING; 9606.ENSP00000340361; -.
BindingDB; Q13705; -.
ChEMBL; CHEMBL5466; -.
GuidetoPHARMACOLOGY; 1792; -.
iPTMnet; Q13705; -.
PhosphoSitePlus; Q13705; -.
BioMuta; ACVR2B; -.
DMDM; 97535735; -.
EPD; Q13705; -.
PaxDb; Q13705; -.
PeptideAtlas; Q13705; -.
PRIDE; Q13705; -.
DNASU; 93; -.
Ensembl; ENST00000352511; ENSP00000340361; ENSG00000114739. [Q13705-1]
GeneID; 93; -.
KEGG; hsa:93; -.
UCSC; uc003cif.4; human. [Q13705-1]
CTD; 93; -.
DisGeNET; 93; -.
EuPathDB; HostDB:ENSG00000114739.13; -.
GeneCards; ACVR2B; -.
HGNC; HGNC:174; ACVR2B.
HPA; CAB025115; -.
HPA; HPA007398; -.
MalaCards; ACVR2B; -.
MIM; 602730; gene.
MIM; 613751; phenotype.
neXtProt; NX_Q13705; -.
OpenTargets; ENSG00000114739; -.
Orphanet; 157769; Situs ambiguus.
PharmGKB; PA24495; -.
eggNOG; KOG3653; Eukaryota.
eggNOG; ENOG410XS2Z; LUCA.
GeneTree; ENSGT00760000118876; -.
HOVERGEN; HBG054502; -.
InParanoid; Q13705; -.
KO; K13596; -.
OMA; PAIKDHW; -.
OrthoDB; EOG091G03YO; -.
PhylomeDB; Q13705; -.
TreeFam; TF352876; -.
Reactome; R-HSA-1181150; Signaling by NODAL.
Reactome; R-HSA-1433617; Regulation of signaling by NODAL.
Reactome; R-HSA-1502540; Signaling by Activin.
Reactome; R-HSA-201451; Signaling by BMP.
SignaLink; Q13705; -.
SIGNOR; Q13705; -.
ChiTaRS; ACVR2B; human.
EvolutionaryTrace; Q13705; -.
GeneWiki; ACVR2B; -.
GenomeRNAi; 93; -.
PRO; PR:Q13705; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114739; -.
CleanEx; HS_ACVR2B; -.
Genevisible; Q13705; HS.
GO; GO:0005737; C:cytoplasm; IDA:HGNC.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0043234; C:protein complex; IDA:MGI.
GO; GO:0043235; C:receptor complex; IPI:BHF-UCL.
GO; GO:0048185; F:activin binding; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0019838; F:growth factor binding; IPI:HGNC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004674; F:protein serine/threonine kinase activity; IMP:HGNC.
GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:Ensembl.
GO; GO:0004702; F:signal transducer, downstream of receptor, with serine/threonine kinase activity; IEA:InterPro.
GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:InterPro.
GO; GO:0032147; P:activation of protein kinase activity; IEA:Ensembl.
GO; GO:0032924; P:activin receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0009952; P:anterior/posterior pattern specification; IMP:HGNC.
GO; GO:0060840; P:artery development; ISS:BHF-UCL.
GO; GO:0001974; P:blood vessel remodeling; ISS:BHF-UCL.
GO; GO:0030509; P:BMP signaling pathway; IDA:BHF-UCL.
GO; GO:0007368; P:determination of left/right symmetry; IEA:Ensembl.
GO; GO:0048617; P:embryonic foregut morphogenesis; IEA:Ensembl.
GO; GO:0001702; P:gastrulation with mouth forming second; IEA:Ensembl.
GO; GO:0007507; P:heart development; IEA:Ensembl.
GO; GO:0030073; P:insulin secretion; IEA:Ensembl.
GO; GO:0001822; P:kidney development; IEA:Ensembl.
GO; GO:0030324; P:lung development; IEA:Ensembl.
GO; GO:0001946; P:lymphangiogenesis; ISS:BHF-UCL.
GO; GO:0060836; P:lymphatic endothelial cell differentiation; ISS:BHF-UCL.
GO; GO:0007498; P:mesoderm development; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IGI:BHF-UCL.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEA:Ensembl.
GO; GO:0035265; P:organ growth; IEA:Ensembl.
GO; GO:0060021; P:palate development; IEA:Ensembl.
GO; GO:0031016; P:pancreas development; IEA:Ensembl.
GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IDA:HGNC.
GO; GO:0030501; P:positive regulation of bone mineralization; IMP:BHF-UCL.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:BHF-UCL.
GO; GO:0009791; P:post-embryonic development; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:HGNC.
GO; GO:0009749; P:response to glucose; IEA:Ensembl.
GO; GO:0061298; P:retina vasculature development in camera-type eye; ISS:BHF-UCL.
GO; GO:0007165; P:signal transduction; IDA:HGNC.
GO; GO:0048705; P:skeletal system morphogenesis; IEA:Ensembl.
GO; GO:0007178; P:transmembrane receptor protein serine/threonine kinase signaling pathway; TAS:ProtInc.
GO; GO:0060841; P:venous blood vessel development; ISS:BHF-UCL.
InterPro; IPR000472; Activin_recp.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR008271; Ser/Thr_kinase_AS.
InterPro; IPR000333; TGFB_receptor.
PANTHER; PTHR23255; PTHR23255; 1.
Pfam; PF01064; Activin_recp; 1.
Pfam; PF00069; Pkinase; 1.
PRINTS; PR00653; ACTIVIN2R.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Complete proteome; Disease mutation; Disulfide bond; Glycoprotein;
Heterotaxy; Kinase; Magnesium; Manganese; Membrane; Metal-binding;
Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Serine/threonine-protein kinase; Signal;
Transferase; Transmembrane; Transmembrane helix.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 512 Activin receptor type-2B.
/FTId=PRO_0000024404.
TOPO_DOM 19 137 Extracellular. {ECO:0000255}.
TRANSMEM 138 158 Helical. {ECO:0000255}.
TOPO_DOM 159 512 Cytoplasmic. {ECO:0000255}.
DOMAIN 190 480 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 196 204 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
REGION 491 512 Interaction with DYNLT1.
{ECO:0000250|UniProtKB:P27040}.
ACT_SITE 321 321 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10027}.
BINDING 217 217 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
CARBOHYD 42 42 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22718755}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:22718755}.
DISULFID 29 59 {ECO:0000269|PubMed:22718755}.
DISULFID 49 77 {ECO:0000269|PubMed:22718755}.
DISULFID 84 103 {ECO:0000269|PubMed:22718755}.
DISULFID 90 102 {ECO:0000269|PubMed:22718755}.
DISULFID 104 109 {ECO:0000269|PubMed:22718755}.
VARIANT 40 40 R -> H (in HTX4; dbSNP:rs121434437).
{ECO:0000269|PubMed:9916847}.
/FTId=VAR_013281.
VARIANT 176 176 P -> R (in dbSNP:rs35882617).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_041396.
VARIANT 459 459 E -> D (in dbSNP:rs500611).
{ECO:0000269|PubMed:9621519}.
/FTId=VAR_050594.
VARIANT 494 494 V -> I (in HTX4; dbSNP:rs121434438).
{ECO:0000269|PubMed:9916847}.
/FTId=VAR_013282.
CONFLICT 16 17 CA -> WP (in Ref. 1; CAA54671).
{ECO:0000305}.
CONFLICT 64 64 R -> A (in Ref. 1 and 2). {ECO:0000305}.
CONFLICT 459 459 E -> A (in Ref. 3; AAC64515).
{ECO:0000305}.
STRAND 27 33 {ECO:0000244|PDB:2H62}.
HELIX 36 39 {ECO:0000244|PDB:2H62}.
STRAND 43 49 {ECO:0000244|PDB:2H62}.
STRAND 57 66 {ECO:0000244|PDB:2H62}.
STRAND 69 79 {ECO:0000244|PDB:2H62}.
HELIX 82 84 {ECO:0000244|PDB:2H62}.
STRAND 88 91 {ECO:0000244|PDB:2H62}.
STRAND 98 106 {ECO:0000244|PDB:2H62}.
TURN 107 110 {ECO:0000244|PDB:2H62}.
STRAND 111 114 {ECO:0000244|PDB:2H62}.
STRAND 191 197 {ECO:0000244|PDB:2QLU}.
STRAND 200 209 {ECO:0000244|PDB:2QLU}.
STRAND 212 219 {ECO:0000244|PDB:2QLU}.
HELIX 221 223 {ECO:0000244|PDB:2QLU}.
HELIX 224 235 {ECO:0000244|PDB:2QLU}.
STRAND 247 253 {ECO:0000244|PDB:2QLU}.
TURN 256 258 {ECO:0000244|PDB:2QLU}.
STRAND 260 266 {ECO:0000244|PDB:2QLU}.
HELIX 273 279 {ECO:0000244|PDB:2QLU}.
HELIX 284 302 {ECO:0000244|PDB:2QLU}.
STRAND 305 308 {ECO:0000244|PDB:2QLU}.
TURN 309 311 {ECO:0000244|PDB:2QLU}.
STRAND 312 314 {ECO:0000244|PDB:2QLU}.
STRAND 316 318 {ECO:0000244|PDB:2QLU}.
HELIX 324 326 {ECO:0000244|PDB:2QLU}.
STRAND 327 329 {ECO:0000244|PDB:2QLU}.
STRAND 335 337 {ECO:0000244|PDB:2QLU}.
STRAND 344 346 {ECO:0000244|PDB:2QLU}.
HELIX 362 364 {ECO:0000244|PDB:2QLU}.
HELIX 367 370 {ECO:0000244|PDB:2QLU}.
HELIX 378 398 {ECO:0000244|PDB:2QLU}.
TURN 413 417 {ECO:0000244|PDB:2QLU}.
HELIX 424 431 {ECO:0000244|PDB:2QLU}.
HELIX 442 446 {ECO:0000244|PDB:2QLU}.
HELIX 448 460 {ECO:0000244|PDB:2QLU}.
HELIX 465 467 {ECO:0000244|PDB:2QLU}.
HELIX 471 482 {ECO:0000244|PDB:2QLU}.
SEQUENCE 512 AA; 57724 MW; B377FEF92EF74937 CRC64;
MTAPWVALAL LWGSLCAGSG RGEAETRECI YYNANWELER TNQSGLERCE GEQDKRLHCY
ASWRNSSGTI ELVKKGCWLD DFNCYDRQEC VATEENPQVY FCCCEGNFCN ERFTHLPEAG
GPEVTYEPPP TAPTLLTVLA YSLLPIGGLS LIVLLAFWMY RHRKPPYGHV DIHEDPGPPP
PSPLVGLKPL QLLEIKARGR FGCVWKAQLM NDFVAVKIFP LQDKQSWQSE REIFSTPGMK
HENLLQFIAA EKRGSNLEVE LWLITAFHDK GSLTDYLKGN IITWNELCHV AETMSRGLSY
LHEDVPWCRG EGHKPSIAHR DFKSKNVLLK SDLTAVLADF GLAVRFEPGK PPGDTHGQVG
TRRYMAPEVL EGAINFQRDA FLRIDMYAMG LVLWELVSRC KAADGPVDEY MLPFEEEIGQ
HPSLEELQEV VVHKKMRPTI KDHWLKHPGL AQLCVTIEEC WDHDAEARLS AGCVEERVSL
IRRSVNGTTS DCLVSLVTSV TNVDLPPKES SI


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C302 Activin Receptor Type IIB Activin RIIB (C-His tag) lmg
C302 Activin Receptor Type IIB Activin RIIB (C-His tag) 500
CD58 Activin Receptor Type IIB Activin RIIB (C-Fc-His tag) lmg
C561 Activin Receptor Type-2A Activin RIIA (C-His tag) lmg
C860 Activin Receptor Type-2A Activin RIIA (C-Fc-His tag) lmg
C860 Activin Receptor Type-2A Activin RIIA (C-Fc-His tag) 500
E0015m ELISA kit Activin receptor-like kinase 3,Acvrlk3,ALK-3,BMP type-1A receptor,BMP-2_BMP-4 receptor,Bmpr,Bmpr1a,BMPR-1A,Bone morphogenetic protein receptor type-1A,Mouse,Mus musculus,Serine_threonine-pr 96T
EIAAB42160 Activin A receptor type II-like protein kinase of 53kD,Activin receptor-like kinase 5,ALK5,ALK5,ALK-5,Homo sapiens,Human,Serine_threonine-protein kinase receptor R4,SKR4,SKR4,TbetaR-I,TGF-beta recepto
U0015h CLIA Activin receptor-like kinase 3,ACVRLK3,ALK3,ALK-3,BMP type-1A receptor,BMPR1A,BMPR-1A,Bone morphogenetic protein receptor type-1A,Homo sapiens,Human,Serine_threonine-protein kinase receptor R5,SK 96T


 

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