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Bone morphogenetic protein 2 (BMP-2) (Bone morphogenetic protein 2A) (BMP-2A)

 BMP2_MOUSE              Reviewed;         394 AA.
P21274; Q497W8;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
28-MAR-2018, entry version 165.
RecName: Full=Bone morphogenetic protein 2;
Short=BMP-2;
AltName: Full=Bone morphogenetic protein 2A;
Short=BMP-2A;
Flags: Precursor;
Name=Bmp2; Synonyms=Bmp-2;
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 [GENOMIC DNA].
PubMed=8018727; DOI=10.1016/0167-4781(94)90017-5;
Feng J.Q., Harris M.A., Ghosh-Choudhury N., Feng M., Mundy G.R.,
Harris S.E.;
"Structure and sequence of mouse bone morphogenetic protein-2 gene
(BMP-2): comparison of the structures and promoter regions of BMP-2
and BMP-4 genes.";
Biochim. Biophys. Acta 1218:221-224(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Embryo, and Medulla oblongata;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
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.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thyroid;
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-351.
PubMed=1970330; DOI=10.1016/0888-7543(90)90480-I;
Dickinson M.E., Kobrin M.S., Silan C.M., Kingsley D.M., Justice M.J.,
Miller D.A., Ceci J.D., Lock L.F., Lee A., Buchberg A.M.,
Siracusa L.D., Lyons K.M., Derynck R., Hogan B.L.M., Copeland N.G.,
Jenkins N.A.;
"Chromosomal localization of seven members of the murine TGF-beta
superfamily suggests close linkage to several morphogenetic mutant
loci.";
Genomics 6:505-520(1990).
[7]
INTERACTION WITH SOSTDC1.
PubMed=14623234; DOI=10.1016/j.ydbio.2003.08.011;
Laurikkala J., Kassai Y., Pakkasjaervi L., Thesleff I., Itoh N.;
"Identification of a secreted BMP antagonist, ectodin, integrating
BMP, FGF, and SHH signals from the tooth enamel knot.";
Dev. Biol. 264:91-105(2003).
[8]
INTERACTION WITH GREM2.
PubMed=15039429; DOI=10.1074/jbc.M402376200;
Sudo S., Avsian-Kretchmer O., Wang L.S., Hsueh A.J.;
"Protein related to DAN and cerberus is a bone morphogenetic protein
antagonist that participates in ovarian paracrine regulation.";
J. Biol. Chem. 279:23134-23141(2004).
[9]
INTERACTION WITH RGMB.
PubMed=15671031; DOI=10.1074/jbc.M410034200;
Samad T.A., Rebbapragada A., Bell E., Zhang Y., Sidis Y., Jeong S.-J.,
Campagna J.A., Perusini S., Fabrizio D.A., Schneyer A.L., Lin H.Y.,
Brivanlou A.H., Attisano L., Woolf C.J.;
"DRAGON, a bone morphogenetic protein co-receptor.";
J. Biol. Chem. 280:14122-14129(2005).
[10]
INTERACTION WITH RGMA.
PubMed=15975920; DOI=10.1074/jbc.M503511200;
Babitt J.L., Zhang Y., Samad T.A., Xia Y., Tang J., Campagna J.A.,
Schneyer A.L., Woolf C.J., Lin H.Y.;
"Repulsive guidance molecule (RGMa), a DRAGON homologue, is a bone
morphogenetic protein co-receptor.";
J. Biol. Chem. 280:29820-29827(2005).
[11]
INTERACTION WITH RGMC.
PubMed=16604073; DOI=10.1038/ng1777;
Babitt J.L., Huang F.W., Wrighting D.M., Xia Y., Sidis Y., Samad T.A.,
Campagna J.A., Chung R.T., Schneyer A.L., Woolf C.J., Andrews N.C.,
Lin H.Y.;
"Bone morphogenetic protein signaling by hemojuvelin regulates
hepcidin expression.";
Nat. Genet. 38:531-539(2006).
[12]
INTERACTION WITH RGMA.
PubMed=17472960; DOI=10.1074/jbc.M701679200;
Xia Y., Yu P.B., Sidis Y., Beppu H., Bloch K.D., Schneyer A.L.,
Lin H.Y.;
"Repulsive guidance molecule RGMa alters utilization of bone
morphogenetic protein (BMP) type II receptors by BMP2 and BMP4.";
J. Biol. Chem. 282:18129-18140(2007).
[13]
INTERACTION WITH ASPN.
PubMed=17522060; DOI=10.1074/jbc.M611181200;
Yamada S., Tomoeda M., Ozawa Y., Yoneda S., Terashima Y., Ikezawa K.,
Ikegawa S., Saito M., Toyosawa S., Murakami S.;
"PLAP-1/asporin, a novel negative regulator of periodontal ligament
mineralization.";
J. Biol. Chem. 282:23070-23080(2007).
[14]
INTERACTION WITH MFAP5.
PubMed=23963447; DOI=10.1074/jbc.M113.497727;
Combs M.D., Knutsen R.H., Broekelmann T.J., Toennies H.M., Brett T.J.,
Miller C.A., Kober D.L., Craft C.S., Atkinson J.J., Shipley J.M.,
Trask B.C., Mecham R.P.;
"Microfibril-associated glycoprotein 2 (MAGP2) loss of function has
pleiotropic effects in vivo.";
J. Biol. Chem. 288:28869-28880(2013).
-!- FUNCTION: Induces cartilage and bone formation. Stimulates the
differentiation of myoblasts into osteoblasts via the EIF2AK3-
EIF2A- ATF4 pathway. BMP2 activation of EIF2AK3 stimulates
phosphorylation of EIF2A which leads to increased expression of
ATF4 which plays a central role in osteoblast differentiation. In
addition stimulates TMEM119, which upregulates the expression of
ATF4. {ECO:0000250|UniProtKB:P12643}.
-!- SUBUNIT: Homodimer; disulfide-linked (By similarity). Interacts
with SOSTDC1, GREM2, RGMA, RGMB and RGMC. Interacts with ASPN.
Interacts with MFAP5. Interacts with FBN1 (via N-terminal domain)
and FBN2 (By similarity). {ECO:0000250|UniProtKB:P12643,
ECO:0000269|PubMed:14623234, ECO:0000269|PubMed:15039429,
ECO:0000269|PubMed:15671031, ECO:0000269|PubMed:15975920,
ECO:0000269|PubMed:16604073, ECO:0000269|PubMed:17472960,
ECO:0000269|PubMed:17522060, ECO:0000269|PubMed:23963447}.
-!- SUBCELLULAR LOCATION: Secreted.
-!- SIMILARITY: Belongs to the TGF-beta family. {ECO:0000305}.
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EMBL; L25602; AAB05665.1; -; Genomic_DNA.
EMBL; AK133923; BAE21928.1; -; mRNA.
EMBL; AK161862; BAE36612.1; -; mRNA.
EMBL; AL831753; CAM22737.1; -; Genomic_DNA.
EMBL; CH466519; EDL28371.1; -; Genomic_DNA.
EMBL; BC100344; AAI00345.1; -; mRNA.
CCDS; CCDS16782.1; -.
PIR; A34201; A34201.
PIR; S45355; S45355.
RefSeq; NP_031579.2; NM_007553.3.
UniGene; Mm.103205; -.
ProteinModelPortal; P21274; -.
SMR; P21274; -.
BioGrid; 198363; 1.
STRING; 10090.ENSMUSP00000028836; -.
PhosphoSitePlus; P21274; -.
MaxQB; P21274; -.
PaxDb; P21274; -.
PRIDE; P21274; -.
Ensembl; ENSMUST00000028836; ENSMUSP00000028836; ENSMUSG00000027358.
GeneID; 12156; -.
KEGG; mmu:12156; -.
UCSC; uc008mnr.2; mouse.
CTD; 650; -.
MGI; MGI:88177; Bmp2.
eggNOG; KOG3900; Eukaryota.
eggNOG; ENOG410XT8Z; LUCA.
GeneTree; ENSGT00760000118883; -.
HOGENOM; HOG000249478; -.
HOVERGEN; HBG004860; -.
InParanoid; P21274; -.
KO; K21283; -.
OMA; QGVSKRH; -.
OrthoDB; EOG091G0K7Z; -.
TreeFam; TF351789; -.
Reactome; R-MMU-201451; Signaling by BMP.
Reactome; R-MMU-2129379; Molecules associated with elastic fibres.
PRO; PR:P21274; -.
Proteomes; UP000000589; Chromosome 2.
Bgee; ENSMUSG00000027358; -.
CleanEx; MM_BMP2; -.
Genevisible; P21274; MM.
GO; GO:0070724; C:BMP receptor complex; ISO:MGI.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:MGI.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0070700; F:BMP receptor binding; ISO:MGI.
GO; GO:0039706; F:co-receptor binding; ISO:MGI.
GO; GO:0005125; F:cytokine activity; TAS:MGI.
GO; GO:0008083; F:growth factor activity; IEA:UniProtKB-KW.
GO; GO:0019211; F:phosphatase activator activity; ISO:MGI.
GO; GO:0046982; F:protein heterodimerization activity; ISO:MGI.
GO; GO:0004745; F:retinol dehydrogenase activity; IDA:MGI.
GO; GO:0046332; F:SMAD binding; ISO:MGI.
GO; GO:0005160; F:transforming growth factor beta receptor binding; IBA:GO_Central.
GO; GO:0000187; P:activation of MAPK activity; ISO:MGI.
GO; GO:0009887; P:animal organ morphogenesis; IMP:MGI.
GO; GO:0003181; P:atrioventricular valve morphogenesis; IMP:MGI.
GO; GO:0030509; P:BMP signaling pathway; IDA:MGI.
GO; GO:0003130; P:BMP signaling pathway involved in heart induction; ISO:MGI.
GO; GO:0030282; P:bone mineralization; IDA:MGI.
GO; GO:0035630; P:bone mineralization involved in bone maturation; ISO:MGI.
GO; GO:0001658; P:branching involved in ureteric bud morphogenesis; IGI:MGI.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; ISO:MGI.
GO; GO:0055007; P:cardiac muscle cell differentiation; IGI:BHF-UCL.
GO; GO:0055008; P:cardiac muscle tissue morphogenesis; IMP:MGI.
GO; GO:0035051; P:cardiocyte differentiation; ISO:MGI.
GO; GO:0045165; P:cell fate commitment; IMP:MGI.
GO; GO:0071773; P:cellular response to BMP stimulus; ISO:MGI.
GO; GO:0071363; P:cellular response to growth factor stimulus; IDA:MGI.
GO; GO:0071407; P:cellular response to organic cyclic compound; IDA:MGI.
GO; GO:0002062; P:chondrocyte differentiation; ISO:MGI.
GO; GO:0060128; P:corticotropin hormone secreting cell differentiation; IDA:MGI.
GO; GO:0035054; P:embryonic heart tube anterior/posterior pattern specification; IMP:MGI.
GO; GO:0003203; P:endocardial cushion morphogenesis; IMP:BHF-UCL.
GO; GO:0001837; P:epithelial to mesenchymal transition; ISO:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0006954; P:inflammatory response; IEP:UniProtKB.
GO; GO:0048839; P:inner ear development; IDA:MGI.
GO; GO:0048762; P:mesenchymal cell differentiation; ISS:UniProtKB.
GO; GO:0072138; P:mesenchymal cell proliferation involved in ureteric bud development; IMP:UniProtKB.
GO; GO:0060485; P:mesenchyme development; ISS:BHF-UCL.
GO; GO:0032348; P:negative regulation of aldosterone biosynthetic process; ISO:MGI.
GO; GO:0051042; P:negative regulation of calcium-independent cell-cell adhesion; ISO:MGI.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:2000726; P:negative regulation of cardiac muscle cell differentiation; ISO:MGI.
GO; GO:0045786; P:negative regulation of cell cycle; ISO:MGI.
GO; GO:0008285; P:negative regulation of cell proliferation; IGI:MGI.
GO; GO:2000065; P:negative regulation of cortisol biosynthetic process; ISO:MGI.
GO; GO:0010629; P:negative regulation of gene expression; IDA:MGI.
GO; GO:0043569; P:negative regulation of insulin-like growth factor receptor signaling pathway; ISO:MGI.
GO; GO:0010894; P:negative regulation of steroid biosynthetic process; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0003308; P:negative regulation of Wnt signaling pathway involved in heart development; ISO:MGI.
GO; GO:0007219; P:Notch signaling pathway; IMP:MGI.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IDA:MGI.
GO; GO:0001649; P:osteoblast differentiation; IDA:MGI.
GO; GO:0060389; P:pathway-restricted SMAD protein phosphorylation; ISO:MGI.
GO; GO:0060039; P:pericardium development; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:0048711; P:positive regulation of astrocyte differentiation; IDA:MGI.
GO; GO:0030501; P:positive regulation of bone mineralization; ISO:MGI.
GO; GO:0061036; P:positive regulation of cartilage development; IDA:MGI.
GO; GO:0045597; P:positive regulation of cell differentiation; IDA:MGI.
GO; GO:0030335; P:positive regulation of cell migration; IMP:BHF-UCL.
GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:MGI.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:BHF-UCL.
GO; GO:0045600; P:positive regulation of fat cell differentiation; IDA:MGI.
GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISO:MGI.
GO; GO:0050769; P:positive regulation of neurogenesis; ISO:MGI.
GO; GO:0045666; P:positive regulation of neuron differentiation; IDA:MGI.
GO; GO:0042482; P:positive regulation of odontogenesis; IDA:MGI.
GO; GO:0045778; P:positive regulation of ossification; IDA:MGI.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:MGI.
GO; GO:0033690; P:positive regulation of osteoblast proliferation; IMP:BHF-UCL.
GO; GO:1900745; P:positive regulation of p38MAPK cascade; ISO:MGI.
GO; GO:0010862; P:positive regulation of pathway-restricted SMAD protein phosphorylation; ISS:UniProtKB.
GO; GO:0010922; P:positive regulation of phosphatase activity; ISO:MGI.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; IGI:BHF-UCL.
GO; GO:0032092; P:positive regulation of protein binding; ISO:MGI.
GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:1901522; P:positive regulation of transcription from RNA polymerase II promoter involved in cellular response to chemical stimulus; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IDA:MGI.
GO; GO:0060804; P:positive regulation of Wnt signaling pathway by BMP signaling pathway; IDA:MGI.
GO; GO:0031648; P:protein destabilization; IDA:MGI.
GO; GO:0006468; P:protein phosphorylation; ISO:MGI.
GO; GO:0006029; P:proteoglycan metabolic process; IGI:MGI.
GO; GO:0042981; P:regulation of apoptotic process; IBA:GO_Central.
GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central.
GO; GO:0042487; P:regulation of odontogenesis of dentin-containing tooth; IGI:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0001666; P:response to hypoxia; IMP:MGI.
GO; GO:0060395; P:SMAD protein signal transduction; ISS:UniProtKB.
GO; GO:0021537; P:telencephalon development; ISO:MGI.
GO; GO:0021978; P:telencephalon regionalization; IGI:MGI.
GO; GO:0060129; P:thyroid-stimulating hormone-secreting cell differentiation; IDA:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; TAS:MGI.
Gene3D; 2.10.90.10; -; 1.
InterPro; IPR029034; Cystine-knot_cytokine.
InterPro; IPR001839; TGF-b_C.
InterPro; IPR001111; TGF-b_propeptide.
InterPro; IPR015615; TGF-beta-rel.
InterPro; IPR017948; TGFb_CS.
PANTHER; PTHR11848; PTHR11848; 1.
Pfam; PF00019; TGF_beta; 1.
Pfam; PF00688; TGFb_propeptide; 1.
SMART; SM00204; TGFB; 1.
SUPFAM; SSF57501; SSF57501; 1.
PROSITE; PS00250; TGF_BETA_1; 1.
PROSITE; PS51362; TGF_BETA_2; 1.
1: Evidence at protein level;
Chondrogenesis; Cleavage on pair of basic residues; Complete proteome;
Cytokine; Developmental protein; Differentiation; Disulfide bond;
Glycoprotein; Growth factor; Osteogenesis; Phosphoprotein;
Reference proteome; Secreted; Signal.
SIGNAL 1 19 {ECO:0000255}.
PROPEP 20 280 Cleaved by PCSK5. {ECO:0000305}.
/FTId=PRO_0000033826.
CHAIN 281 394 Bone morphogenetic protein 2.
/FTId=PRO_0000033827.
MOD_RES 86 86 Phosphoserine.
{ECO:0000250|UniProtKB:P12644}.
CARBOHYD 134 134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 162 162 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 198 198 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 336 336 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 294 359 {ECO:0000250}.
DISULFID 323 391 {ECO:0000250}.
DISULFID 327 393 {ECO:0000250}.
DISULFID 358 358 Interchain. {ECO:0000250}.
CONFLICT 110 110 S -> T (in Ref. 1; AAB05665).
{ECO:0000305}.
CONFLICT 113 114 HE -> QL (in Ref. 1; AAB05665).
{ECO:0000305}.
CONFLICT 271 271 G -> R (in Ref. 6; no nucleotide entry).
{ECO:0000305}.
SEQUENCE 394 AA; 44525 MW; D0C03B63B1D5C4E2 CRC64;
MVAGTRCLLV LLLPQVLLGG AAGLIPELGR KKFAAASSRP LSRPSEDVLS EFELRLLSMF
GLKQRPTPSK DVVVPPYMLD LYRRHSGQPG APAPDHRLER AASRANTVRS FHHEEAVEEL
PEMSGKTARR FFFNLSSVPS DEFLTSAELQ IFREQIQEAL GNSSFQHRIN IYEIIKPAAA
NLKFPVTRLL DTRLVNQNTS QWESFDVTPA VMRWTTQGHT NHGFVVEVAH LEENPGVSKR
HVRISRSLHQ DEHSWSQIRP LLVTFGHDGK GHPLHKREKR QAKHKQRKRL KSSCKRHPLY
VDFSDVGWND WIVAPPGYHA FYCHGECPFP LADHLNSTNH AIVQTLVNSV NSKIPKACCV
PTELSAISML YLDENEKVVL KNYQDMVVEG CGCR


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101-M233 BMP-2 Anti-Human Host: Mouse bone morphogenetic protein 2; BDA2; BMP2A; bone morphogenetic protein 4; ZYME; BMP2B; OFC11; BMP2B1; MCOPS6 100
102-P03A BMP-2 Anti-Human Host: Rabbit bone morphogenetic protein 2; BDA2; BMP2A; bone morphogenetic protein 4; ZYME; BMP2B; OFC11; BMP2B1; MCOPS6 100
U0014h CLIA BMP2B,BMP-2B,BMP4,BMP-4,Bone morphogenetic protein 2B,Bone morphogenetic protein 4,DVR4,Homo sapiens,Human 96T
E0014h ELISA kit BMP2B,BMP-2B,BMP4,BMP-4,Bone morphogenetic protein 2B,Bone morphogenetic protein 4,DVR4,Homo sapiens,Human 96T
E0014h ELISA BMP2B,BMP-2B,BMP4,BMP-4,Bone morphogenetic protein 2B,Bone morphogenetic protein 4,DVR4,Homo sapiens,Human 96T
E0013h ELISA BMP2,BMP-2,BMP2A,BMP-2A,Bone morphogenetic protein 2,Bone morphogenetic protein 2A,Homo sapiens,Human 96T
U0013h CLIA BMP2,BMP-2,BMP2A,BMP-2A,Bone morphogenetic protein 2,Bone morphogenetic protein 2A,Homo sapiens,Human 96T
E0013h ELISA kit BMP2,BMP-2,BMP2A,BMP-2A,Bone morphogenetic protein 2,Bone morphogenetic protein 2A,Homo sapiens,Human 96T
E0013m ELISA Bmp2,BMP-2,Bmp-2,BMP-2A,Bone morphogenetic protein 2,Bone morphogenetic protein 2A,Mouse,Mus musculus 96T
E0014m ELISA kit BMP-2B,Bmp4,BMP-4,Bmp-4,Bone morphogenetic protein 2B,Bone morphogenetic protein 4,Dvr-4,Mouse,Mus musculus 96T
U0013r CLIA Bmp2,BMP-2,Bmp-2,BMP-2A,Bone morphogenetic protein 2,Bone morphogenetic protein 2A,Rat,Rattus norvegicus 96T
U0014r CLIA BMP-2B,Bmp4,BMP-4,Bmp-4,Bone morphogenetic protein 2B,Bone morphogenetic protein 4,Dvr-4,Rat,Rattus norvegicus 96T
E0014m ELISA BMP-2B,Bmp4,BMP-4,Bmp-4,Bone morphogenetic protein 2B,Bone morphogenetic protein 4,Dvr-4,Mouse,Mus musculus 96T
U0014m CLIA BMP-2B,Bmp4,BMP-4,Bmp-4,Bone morphogenetic protein 2B,Bone morphogenetic protein 4,Dvr-4,Mouse,Mus musculus 96T
E0014r ELISA kit BMP-2B,Bmp4,BMP-4,Bmp-4,Bone morphogenetic protein 2B,Bone morphogenetic protein 4,Dvr-4,Rat,Rattus norvegicus 96T
E0013m ELISA kit Bmp2,BMP-2,Bmp-2,BMP-2A,Bone morphogenetic protein 2,Bone morphogenetic protein 2A,Mouse,Mus musculus 96T
E0014r ELISA BMP-2B,Bmp4,BMP-4,Bmp-4,Bone morphogenetic protein 2B,Bone morphogenetic protein 4,Dvr-4,Rat,Rattus norvegicus 96T
U0013m CLIA Bmp2,BMP-2,Bmp-2,BMP-2A,Bone morphogenetic protein 2,Bone morphogenetic protein 2A,Mouse,Mus musculus 96T
E0013r ELISA Bmp2,BMP-2,Bmp-2,BMP-2A,Bone morphogenetic protein 2,Bone morphogenetic protein 2A,Rat,Rattus norvegicus 96T
E0013r ELISA kit Bmp2,BMP-2,Bmp-2,BMP-2A,Bone morphogenetic protein 2,Bone morphogenetic protein 2A,Rat,Rattus norvegicus 96T
024-15071 Bone Morphogenetic Protein 13 (BMP 13), Human, recombinant Source Human bone morphogenetic protein 13 cDNA expressed in E.coli Appearance Lyophilized form with no additives (Sterile_filtered) Molecul 10ìg


 

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