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Brother of CDO (Protein BOC)

 BOC_HUMAN               Reviewed;        1114 AA.
Q9BWV1; A6NJ30; B2RMS8; D3DN70; Q6UXJ5; Q8N2P7; Q8NF26;
02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
27-SEP-2017, entry version 138.
RecName: Full=Brother of CDO;
Short=Protein BOC;
Flags: Precursor;
Name=BOC; ORFNames=UNQ604/PRO1190;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CDON,
GLYCOSYLATION, AND TISSUE SPECIFICITY.
TISSUE=Fetal brain;
PubMed=11782431; DOI=10.1093/emboj/21.1.114;
Kang J.-S., Mulieri P.J., Hu Y., Taliana L., Krauss R.S.;
"BOC, an Ig superfamily member, associates with CDO to positively
regulate myogenic differentiation.";
EMBO J. 21:114-124(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 317-1114 (ISOFORM 3).
TISSUE=Embryo, and Spleen;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16641997; DOI=10.1038/nature04728;
Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R.,
Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R.,
Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V.,
Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.,
Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S.,
Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q.,
Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C.,
Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G.,
Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B.,
Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R.,
Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J.,
Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A.,
Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J.,
Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H.,
Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G.,
Gibbs R.A.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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]
PROTEIN SEQUENCE OF 31-45.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[8]
IDENTIFICATION IN A COMPLEX WITH CDON; CDH2; CDH15 AND CTNNB1, AND
SUBCELLULAR LOCATION.
PubMed=12634428; DOI=10.1073/pnas.0736565100;
Kang J.-S., Feinleib J.L., Knox S., Ketteringham M.A., Krauss R.S.;
"Promyogenic members of the Ig and cadherin families associate to
positively regulate differentiation.";
Proc. Natl. Acad. Sci. U.S.A. 100:3989-3994(2003).
[9]
X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 710-817 IN COMPLEXES WITH
DHH AND IHH, AND INTERACTION WITH SHH; DHH AND IHH.
PubMed=20519495; DOI=10.1074/jbc.M110.131680;
Kavran J.M., Ward M.D., Oladosu O.O., Mulepati S., Leahy D.J.;
"All mammalian Hedgehog proteins interact with cell adhesion molecule,
down-regulated by oncogenes (CDO) and brother of CDO (BOC) in a
conserved manner.";
J. Biol. Chem. 285:24584-24590(2010).
[10]
VARIANT [LARGE SCALE ANALYSIS] MET-713.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Component of a cell-surface receptor complex that
mediates cell-cell interactions between muscle precursor cells.
Promotes differentiation of myogenic cells.
-!- SUBUNIT: Part of a complex that contains BOC, CDON, NEO1,
cadherins and CTNNB1. Interacts with NTN3 (By similarity).
Interacts with SHH, DHH and IHH. Interacts with CDH2 and CTNNB1.
Interacts with CDH15 only during the early stages of myoblast
differentiation. {ECO:0000250, ECO:0000269|PubMed:11782431,
ECO:0000269|PubMed:12634428, ECO:0000269|PubMed:20519495}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12634428};
Single-pass type I membrane protein {ECO:0000269|PubMed:12634428}.
Note=Enriched at sites of cell-cell contact.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9BWV1-1; Sequence=Displayed;
Name=2;
IsoId=Q9BWV1-2; Sequence=VSP_037603, VSP_037604;
Note=No experimental confirmation available. Incomplete
sequence.;
Name=3;
IsoId=Q9BWV1-3; Sequence=VSP_034684;
-!- TISSUE SPECIFICITY: Detected in skeletal muscle, heart, thymus,
kidney and small intestine. Detected at lower levels in brain,
placenta, lung and colon mucosa. {ECO:0000269|PubMed:11782431}.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:11782431}.
-!- MISCELLANEOUS: The C-terminal cytoplasmic domain is not required
for the stimuation of myogenesis.
-!- SEQUENCE CAUTION:
Sequence=BAC11057.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
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EMBL; AY027658; AAK14795.1; -; mRNA.
EMBL; AY358328; AAQ88694.1; -; mRNA.
EMBL; AK074556; BAC11057.1; ALT_INIT; mRNA.
EMBL; AK090455; BAC03436.1; -; mRNA.
EMBL; AC026329; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471052; EAW79643.1; -; Genomic_DNA.
EMBL; CH471052; EAW79644.1; -; Genomic_DNA.
EMBL; CH471052; EAW79646.1; -; Genomic_DNA.
EMBL; BC136390; AAI36391.1; -; mRNA.
CCDS; CCDS2971.1; -. [Q9BWV1-1]
CCDS; CCDS77788.1; -. [Q9BWV1-3]
RefSeq; NP_001288790.1; NM_001301861.1. [Q9BWV1-3]
RefSeq; NP_150279.1; NM_033254.3. [Q9BWV1-1]
RefSeq; XP_005247948.1; XM_005247891.2. [Q9BWV1-3]
RefSeq; XP_005247949.1; XM_005247892.2. [Q9BWV1-3]
RefSeq; XP_011511607.1; XM_011513305.2. [Q9BWV1-1]
RefSeq; XP_016862940.1; XM_017007451.1. [Q9BWV1-1]
UniGene; Hs.591318; -.
PDB; 3N1G; X-ray; 1.90 A; C/D=710-817.
PDB; 3N1M; X-ray; 1.69 A; C=710-817.
PDB; 3N1P; X-ray; 2.70 A; C=710-817.
PDBsum; 3N1G; -.
PDBsum; 3N1M; -.
PDBsum; 3N1P; -.
ProteinModelPortal; Q9BWV1; -.
SMR; Q9BWV1; -.
BioGrid; 124859; 12.
IntAct; Q9BWV1; 3.
STRING; 9606.ENSP00000347546; -.
iPTMnet; Q9BWV1; -.
PhosphoSitePlus; Q9BWV1; -.
BioMuta; BOC; -.
DMDM; 74761309; -.
PaxDb; Q9BWV1; -.
PeptideAtlas; Q9BWV1; -.
PRIDE; Q9BWV1; -.
Ensembl; ENST00000273395; ENSP00000273395; ENSG00000144857. [Q9BWV1-3]
Ensembl; ENST00000355385; ENSP00000347546; ENSG00000144857. [Q9BWV1-1]
Ensembl; ENST00000495514; ENSP00000418663; ENSG00000144857. [Q9BWV1-1]
GeneID; 91653; -.
KEGG; hsa:91653; -.
UCSC; uc003dzx.4; human. [Q9BWV1-1]
CTD; 91653; -.
DisGeNET; 91653; -.
EuPathDB; HostDB:ENSG00000144857.14; -.
GeneCards; BOC; -.
HGNC; HGNC:17173; BOC.
HPA; CAB025806; -.
HPA; HPA060778; -.
HPA; HPA061787; -.
MIM; 608708; gene.
neXtProt; NX_Q9BWV1; -.
OpenTargets; ENSG00000144857; -.
PharmGKB; PA143485316; -.
eggNOG; ENOG410IHIH; Eukaryota.
eggNOG; ENOG410XSVT; LUCA.
GeneTree; ENSGT00840000129688; -.
HOVERGEN; HBG061102; -.
InParanoid; Q9BWV1; -.
KO; K20020; -.
OMA; YTMVPLG; -.
OrthoDB; EOG091G00TB; -.
PhylomeDB; Q9BWV1; -.
TreeFam; TF332268; -.
Reactome; R-HSA-375170; CDO in myogenesis.
Reactome; R-HSA-5632681; Ligand-receptor interactions.
Reactome; R-HSA-5635838; Activation of SMO.
SignaLink; Q9BWV1; -.
SIGNOR; Q9BWV1; -.
ChiTaRS; BOC; human.
EvolutionaryTrace; Q9BWV1; -.
GeneWiki; BOC_(gene); -.
GenomeRNAi; 91653; -.
PRO; PR:Q9BWV1; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000144857; -.
CleanEx; HS_BOC; -.
ExpressionAtlas; Q9BWV1; baseline and differential.
Genevisible; Q9BWV1; HS.
GO; GO:0044295; C:axonal growth cone; IEA:Ensembl.
GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0007411; P:axon guidance; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0051149; P:positive regulation of muscle cell differentiation; TAS:Reactome.
GO; GO:0045663; P:positive regulation of myoblast differentiation; ISS:HGNC.
GO; GO:0007224; P:smoothened signaling pathway; IEA:InterPro.
CDD; cd00063; FN3; 3.
Gene3D; 2.60.40.10; -; 7.
InterPro; IPR032982; BOC.
InterPro; IPR003961; FN3_dom.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR013151; Immunoglobulin.
PANTHER; PTHR10489:SF799; PTHR10489:SF799; 1.
Pfam; PF00041; fn3; 3.
Pfam; PF07679; I-set; 1.
Pfam; PF00047; ig; 1.
SMART; SM00060; FN3; 3.
SMART; SM00409; IG; 4.
SMART; SM00408; IGc2; 4.
SUPFAM; SSF48726; SSF48726; 4.
SUPFAM; SSF49265; SSF49265; 2.
PROSITE; PS50853; FN3; 3.
PROSITE; PS50835; IG_LIKE; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell membrane;
Complete proteome; Direct protein sequencing; Disulfide bond;
Glycoprotein; Immunoglobulin domain; Membrane; Polymorphism;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 30 {ECO:0000269|PubMed:15340161}.
CHAIN 31 1114 Brother of CDO.
/FTId=PRO_0000234052.
TOPO_DOM 31 855 Extracellular. {ECO:0000255}.
TRANSMEM 856 876 Helical. {ECO:0000255}.
TOPO_DOM 877 1114 Cytoplasmic. {ECO:0000255}.
DOMAIN 36 123 Ig-like C2-type 1.
DOMAIN 129 213 Ig-like C2-type 2.
DOMAIN 235 315 Ig-like C2-type 3.
DOMAIN 323 409 Ig-like C2-type 4.
DOMAIN 474 571 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 608 703 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 712 812 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
CARBOHYD 65 65 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 76 76 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 189 189 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 275 275 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 517 517 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 725 725 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 759 759 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 106 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 150 200 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 252 299 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 344 391 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 183 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_037603.
VAR_SEQ 184 223 NLQIVNASQEDEGMYKCAAYNPVTQEVKTSGSSDRLRVRR
-> KTRNGCLIPSPCSLGLPPGHALQDILVHTPSVLALLAP
PG (in isoform 2). {ECO:0000305}.
/FTId=VSP_037604.
VAR_SEQ 514 514 K -> KQ (in isoform 3).
{ECO:0000303|PubMed:12975309,
ECO:0000303|PubMed:14702039}.
/FTId=VSP_034684.
VARIANT 713 713 V -> M (in a breast cancer sample;
somatic mutation; dbSNP:rs367589886).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035503.
VARIANT 883 883 K -> N (in dbSNP:rs35536878).
/FTId=VAR_033600.
VARIANT 915 915 Q -> H (in dbSNP:rs3814405).
/FTId=VAR_033601.
CONFLICT 461 461 Q -> K (in Ref. 2; AAQ88694).
{ECO:0000305}.
STRAND 717 725 {ECO:0000244|PDB:3N1M}.
STRAND 728 734 {ECO:0000244|PDB:3N1M}.
HELIX 737 740 {ECO:0000244|PDB:3N1M}.
STRAND 746 754 {ECO:0000244|PDB:3N1M}.
HELIX 760 762 {ECO:0000244|PDB:3N1M}.
STRAND 764 769 {ECO:0000244|PDB:3N1M}.
STRAND 774 777 {ECO:0000244|PDB:3N1M}.
STRAND 785 794 {ECO:0000244|PDB:3N1M}.
STRAND 805 808 {ECO:0000244|PDB:3N1M}.
SEQUENCE 1114 AA; 121059 MW; BDA9021D39CFE3BC CRC64;
MLRGTMTAWR GMRPEVTLAC LLLATAGCFA DLNEVPQVTV QPASTVQKPG GTVILGCVVE
PPRMNVTWRL NGKELNGSDD ALGVLITHGT LVITALNNHT VGRYQCVARM PAGAVASVPA
TVTLANLQDF KLDVQHVIEV DEGNTAVIAC HLPESHPKAQ VRYSVKQEWL EASRGNYLIM
PSGNLQIVNA SQEDEGMYKC AAYNPVTQEV KTSGSSDRLR VRRSTAEAAR IIYPPEAQTI
IVTKGQSLIL ECVASGIPPP RVTWAKDGSS VTGYNKTRFL LSNLLIDTTS EEDSGTYRCM
ADNGVGQPGA AVILYNVQVF EPPEVTMELS QLVIPWGQSA KLTCEVRGNP PPSVLWLRNA
VPLISSQRLR LSRRALRVLS MGPEDEGVYQ CMAENEVGSA HAVVQLRTSR PSITPRLWQD
AELATGTPPV SPSKLGNPEQ MLRGQPALPR PPTSVGPASP QCPGEKGQGA PAEAPIILSS
PRTSKTDSYE LVWRPRHEGS GRAPILYYVV KHRKVTNSSD DWTISGIPAN QHRLTLTRLD
PGSLYEVEMA AYNCAGEGQT AMVTFRTGRR PKPEIMASKE QQIQRDDPGA SPQSSSQPDH
GRLSPPEAPD RPTISTASET SVYVTWIPRG NGGFPIQSFR VEYKKLKKVG DWILATSAIP
PSRLSVEITG LEKGTSYKFR VRALNMLGES EPSAPSRPYV VSGYSGRVYE RPVAGPYITF
TDAVNETTIM LKWMYIPASN NNTPIHGFYI YYRPTDSDND SDYKKDMVEG DKYWHSISHL
QPETSYDIKM QCFNEGGESE FSNVMICETK ARKSSGQPGR LPPPTLAPPQ PPLPETIERP
VGTGAMVARS SDLPYLIVGV VLGSIVLIIV TFIPFCLWRA WSKQKHTTDL GFPRSALPPS
CPYTMVPLGG LPGHQASGQP YLSGISGRAC ANGIHMNRGC PSAAVGYPGM KPQQHCPGEL
QQQSDTSSLL RQTHLGNGYD PQSHQITRGP KSSPDEGSFL YTLPDDSTHQ LLQPHHDCCQ
RQEQPAAVGQ SGVRRAPDSP VLEAVWDPPF HSGPPCCLGL VPVEEVDSPD SCQVSGGDWC
PQHPVGAYVG QEPGMQLSPG PLVRVSFETP PLTI


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CSB-EL002770HU Human Brother of CDO(BOC) ELISA kit SpeciesHuman 96T
CSB-EL002770MO Mouse Brother of CDO(BOC) ELISA kit SpeciesMouse 96T
29-069 GRHL3 is a member of the grainyhead family of transcription factors. GRHL3 interacts with leader-binding protein 32 (LBP-32) and brother of mammalian grainyhead (BOM), and may function as a transcript 0.05 mg
29-070 GRHL3 is a member of the grainyhead family of transcription factors. GRHL3 interacts with leader-binding protein 32 (LBP-32) and brother of mammalian grainyhead (BOM), and may function as a transcript 0.1 mg
27-806 GRHL3 is a member of the grainyhead family of transcription factors. GRHL3 interacts with leader-binding protein 32 (LBP-32) and brother of mammalian grainyhead (BOM), and may function as a transcript 0.05 mg
BOC_HUMAN ELISA Kit FOR Brother of CDO; organism: Human; gene name: BOC 96T
EIAAB09775 Boris,Brother of the regulator of imprinted sites,CCCTC-binding factor,CTCF paralog,Ctcfl,CTCF-like protein,Mouse,Mus musculus,Transcriptional repressor CTCFL
490102 Brother HL-5240L Printer QBC AutoRead Plus Haematology System Accessories
EIAAB09774 BORIS,Brother of the regulator of imprinted sites,Cancer_testis antigen 27,CCCTC-binding factor,CT27,CTCF paralog,CTCFL,CTCF-like protein,Homo sapiens,Human,Transcriptional repressor CTCFL,Zinc finger
PAH-G1-2 Protein Arrays containing 234 Human Protein for simultaneous detection of Protein function, including Protein-protein interaction, Protein modification, antibody specificity, auto-antibody and small m 1 glass slide with 2 sub-arrays
29-850 The protein contains a RING finger, a motif present in a variety of functionally distinct proteins and known to be involved in protein-protein and protein-DNA interactions.The protein encoded by this 0.1 mg
29-844 RNF40 contains a RING finger, a motif known to be involved in protein-protein and protein-DNA interactions. This protein was reported to interact with the tumor suppressor protein RB1. Studies of the 0.1 mg
EIAAB10617 DCN1-like protein 1,DCUN1 domain-containing protein 1,Dcun1d1,Dcun1l1,Defective in cullin neddylation protein 1-like protein 1,Mouse,Mus musculus,Rp42,Tes3,Testis-specific protein 3
EIAAB44668 Dap12,DNAX-activation protein 12,Karap,KAR-associated protein,Killer-activating receptor-associated protein,Mouse,Mus musculus,TYRO protein tyrosine kinase-binding protein,Tyrobp
EIAAB44667 DAP12,DNAX-activation protein 12,Homo sapiens,Human,KARAP,KAR-associated protein,Killer-activating receptor-associated protein,TYRO protein tyrosine kinase-binding protein,TYROBP
18-003-43520 HSPB1-associated protein 1 - 27 KdA heat shock protein-associated protein 1; Protein associated with small stress protein 1 Polyclonal 0.05 mg Aff Pur
EIAAB25665 AML1T1,CBFA2T1,CDR,Cyclin-D-related protein,Eight twenty one protein,ETO,Homo sapiens,Human,MTG8,Protein CBFA2T1,Protein ETO,Protein MTG8,RUNX1T1,Zinc finger MYND domain-containing protein 2,ZMYND2


 

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