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Versican core protein (Chondroitin sulfate proteoglycan core protein 2) (Chondroitin sulfate proteoglycan 2) (Large fibroblast proteoglycan) (PG-M)

 CSPG2_MOUSE             Reviewed;        3357 AA.
Q62059; Q62058; Q9CUU0;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
13-JUN-2006, sequence version 2.
23-MAY-2018, entry version 157.
RecName: Full=Versican core protein;
AltName: Full=Chondroitin sulfate proteoglycan core protein 2;
Short=Chondroitin sulfate proteoglycan 2;
AltName: Full=Large fibroblast proteoglycan;
AltName: Full=PG-M;
Flags: Precursor;
Name=Vcan; Synonyms=Cspg2;
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] (ISOFORMS V0; V1 AND V2).
STRAIN=C57BL/6J, and Swiss Webster;
TISSUE=Brain, and Endothelial cell;
PubMed=7822336; DOI=10.1074/jbc.270.2.958;
Ito K., Shinomura T., Zako M., Ujita M., Kimata K.;
"Multiple forms of mouse PG-M, a large chondroitin sulfate
proteoglycan generated by alternative splicing.";
J. Biol. Chem. 270:958-965(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM V3).
STRAIN=C57BL/6J; TISSUE=Endothelial cell;
PubMed=7876137; DOI=10.1074/jbc.270.8.3914;
Zako M., Shinomura T., Ujita M., Ito K., Kimata K.;
"Expression of PG-M(V3), an alternatively spliced form of PG-M without
a chondroitin sulfate attachment in region in mouse and human
tissues.";
J. Biol. Chem. 270:3914-3918(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-1691 (ISOFORM V1).
STRAIN=C57BL/6J; TISSUE=Skin;
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).
[4]
PROTEIN SEQUENCE OF 277-288, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
INTERACTION WITH FBLN1.
PubMed=10400671; DOI=10.1074/jbc.274.29.20444;
Aspberg A., Adam S., Kostka G., Timpl R., Heinegaard D.;
"Fibulin-1 is a ligand for the C-type lectin domains of aggrecan and
versican.";
J. Biol. Chem. 274:20444-20449(1999).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2585 AND SER-2586, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
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).
-!- FUNCTION: May play a role in intercellular signaling and in
connecting cells with the extracellular matrix. May take part in
the regulation of cell motility, growth and differentiation. Binds
hyaluronic acid.
-!- SUBUNIT: Interacts with FBLN1. {ECO:0000269|PubMed:10400671}.
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Comment=Additional isoforms seem to exist.;
Name=V0;
IsoId=Q62059-1; Sequence=Displayed;
Name=V1;
IsoId=Q62059-2; Sequence=VSP_003087, VSP_003088;
Name=V2;
IsoId=Q62059-3; Sequence=VSP_003089;
Name=V3;
IsoId=Q62059-4; Sequence=VSP_003087, VSP_003090;
-!- TISSUE SPECIFICITY: Isoform V2 is found only in brain.
-!- DEVELOPMENTAL STAGE: Disappears after the cartilage development.
-!- PTM: Phosphorylated by FAM20C in the extracellular medium.
{ECO:0000250|UniProtKB:P13611}.
-!- SIMILARITY: Belongs to the aggrecan/versican proteoglycan family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Versican;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_157";
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EMBL; D16263; BAA03796.1; -; mRNA.
EMBL; D28599; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; D32040; BAA06802.1; -; mRNA.
EMBL; AK014525; BAB29411.3; -; mRNA.
PIR; A55535; A55535.
UniGene; Mm.158700; -.
UniGene; Mm.410783; -.
ProteinModelPortal; Q62059; -.
SMR; Q62059; -.
IntAct; Q62059; 2.
MINT; Q62059; -.
STRING; 10090.ENSMUSP00000105173; -.
iPTMnet; Q62059; -.
PhosphoSitePlus; Q62059; -.
PaxDb; Q62059; -.
PeptideAtlas; Q62059; -.
PRIDE; Q62059; -.
MGI; MGI:102889; Vcan.
eggNOG; ENOG410IFXS; Eukaryota.
eggNOG; ENOG410ZPDG; LUCA.
HOGENOM; HOG000168523; -.
HOVERGEN; HBG051140; -.
InParanoid; Q62059; -.
PhylomeDB; Q62059; -.
PRO; PR:Q62059; -.
Proteomes; UP000000589; Unplaced.
CleanEx; MM_VCAN; -.
GO; GO:0031012; C:extracellular matrix; ISO:MGI.
GO; GO:0005576; C:extracellular region; IDA:MGI.
GO; GO:0005615; C:extracellular space; HDA:BHF-UCL.
GO; GO:0005578; C:proteinaceous extracellular matrix; IDA:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0005201; F:extracellular matrix structural constituent; IBA:GO_Central.
GO; GO:0005540; F:hyaluronic acid binding; IBA:GO_Central.
GO; GO:0019903; F:protein phosphatase binding; IPI:MGI.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
GO; GO:0007417; P:central nervous system development; IBA:GO_Central.
GO; GO:0008347; P:glial cell migration; ISO:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IDA:MGI.
GO; GO:0001501; P:skeletal system development; IBA:GO_Central.
GO; GO:0001657; P:ureteric bud development; IEP:UniProtKB.
CDD; cd00033; CCP; 1.
CDD; cd03588; CLECT_CSPGs; 1.
Gene3D; 2.60.40.10; -; 1.
Gene3D; 3.10.100.10; -; 3.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR033987; CSPG_CTLD.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
InterPro; IPR018097; EGF_Ca-bd_CS.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
InterPro; IPR000538; Link_dom.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
Pfam; PF00008; EGF; 2.
Pfam; PF00059; Lectin_C; 1.
Pfam; PF00084; Sushi; 1.
Pfam; PF07686; V-set; 1.
Pfam; PF00193; Xlink; 2.
PRINTS; PR01265; LINKMODULE.
SMART; SM00032; CCP; 1.
SMART; SM00034; CLECT; 1.
SMART; SM00181; EGF; 2.
SMART; SM00179; EGF_CA; 2.
SMART; SM00409; IG; 1.
SMART; SM00406; IGv; 1.
SMART; SM00445; LINK; 2.
SUPFAM; SSF48726; SSF48726; 1.
SUPFAM; SSF56436; SSF56436; 3.
SUPFAM; SSF57535; SSF57535; 1.
PROSITE; PS00010; ASX_HYDROXYL; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 1.
PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PROSITE; PS00022; EGF_1; 2.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 2.
PROSITE; PS01187; EGF_CA; 1.
PROSITE; PS50835; IG_LIKE; 1.
PROSITE; PS01241; LINK_1; 2.
PROSITE; PS50963; LINK_2; 2.
PROSITE; PS50923; SUSHI; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Complete proteome;
Direct protein sequencing; Disulfide bond; EGF-like domain;
Extracellular matrix; Glycoprotein; Hyaluronic acid;
Immunoglobulin domain; Lectin; Phosphoprotein; Proteoglycan;
Reference proteome; Repeat; Secreted; Signal; Sushi.
SIGNAL 1 23 {ECO:0000255}.
CHAIN 24 3357 Versican core protein.
/FTId=PRO_0000017523.
DOMAIN 24 146 Ig-like V-type.
DOMAIN 150 245 Link 1. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
DOMAIN 251 347 Link 2. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
DOMAIN 3051 3087 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3089 3125 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
DOMAIN 3138 3252 C-type lectin. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 3256 3316 Sushi. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
REGION 348 1308 GAG-alpha (glucosaminoglycan attachment
domain).
REGION 1309 3051 GAG-beta.
MOD_RES 2585 2585 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 2586 2586 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
CARBOHYD 57 57 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 351 351 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 441 441 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 807 807 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 914 914 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 951 951 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1305 1305 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1371 1371 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1678 1678 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2053 2053 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2243 2243 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2361 2361 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2626 2626 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3029 3029 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3331 3331 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3341 3341 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 44 130 {ECO:0000250}.
DISULFID 172 243 {ECO:0000250}.
DISULFID 196 217 {ECO:0000250}.
DISULFID 270 333 {ECO:0000250}.
DISULFID 294 315 {ECO:0000250}.
DISULFID 3055 3066 {ECO:0000250}.
DISULFID 3060 3075 {ECO:0000250}.
DISULFID 3077 3086 {ECO:0000250}.
DISULFID 3093 3104 {ECO:0000250}.
DISULFID 3098 3113 {ECO:0000250}.
DISULFID 3115 3124 {ECO:0000250}.
DISULFID 3131 3142 {ECO:0000250}.
DISULFID 3159 3251 {ECO:0000250}.
DISULFID 3227 3243 {ECO:0000250}.
DISULFID 3258 3301 {ECO:0000250}.
DISULFID 3287 3314 {ECO:0000250}.
VAR_SEQ 348 348 P -> R (in isoform V1 and isoform V3).
{ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:7822336,
ECO:0000303|PubMed:7876137}.
/FTId=VSP_003087.
VAR_SEQ 349 3051 Missing (in isoform V3).
{ECO:0000303|PubMed:7876137}.
/FTId=VSP_003090.
VAR_SEQ 349 1308 Missing (in isoform V1).
{ECO:0000303|PubMed:16141072,
ECO:0000303|PubMed:7822336}.
/FTId=VSP_003088.
VAR_SEQ 1309 3051 Missing (in isoform V2).
{ECO:0000303|PubMed:7822336}.
/FTId=VSP_003089.
CONFLICT 126 126 A -> G (in Ref. 3). {ECO:0000305}.
CONFLICT 1657 1657 I -> T (in Ref. 3). {ECO:0000305}.
CONFLICT 1673 1679 TVWNSNS -> QFGIQTA (in Ref. 3).
{ECO:0000305}.
SEQUENCE 3357 AA; 366787 MW; AE82A0D942B8323A CRC64;
MLINMKGILW MCSTLLLTHA LHQAKMETSP PVKGSLSGKV VLPCHFSTLP TLPPNYNTSE
FLRIKWSKME VDKNGKDIKE TTVLVAQNGN IKIGQDYKGR VSVPTHPDDV GDASLTMVKL
RASDAAVYRC DVMYGIEDTQ DTMSLAVDGV VFHYRAATSR YTLNFAAAQQ ACLDIGAVIA
SPEQLFAAYE DGFEQCDAGW LSDQTVRYPI RAPREGCYGD MMGKEGVRTY GFRSPQETYD
VYCYVDHLDG DVFHITAPSK FTFEEAEAEC TSRDARLATV GELQAAWRNG FDQCDYGWLS
DASVRHPVTV ARAQCGGGLL GVRTLYRFEN QTCFPLPDSR FDAYCFKPKQ NISEATTIEM
NILAETSSPS LSKEPHMVPD RATPVIPLAT ELPIFTTHFP PAGNIVNSEQ KSVVYSQAIT
GRLATESPTT TRNTINSWDL NDSLASGSGP LGMPDISEIK EEELRSTTVI SQHATGSQAV
ITEDTQTHES VSQIEQIEVG PLVTSMEITN HISLKELPEK NKTPYESTEV TLEHTTEMPT
VSASPELATT SHYGFTLRED DREDRTLTVR SDQSTRVFSQ IPEVITVSKT SEDTTYSQLG
DLESISTSTI TMLGTDRSLI DKEKEPKTNG KVTEDEFGQS QPTTTFPSQH LTEVELLPYS
GDTTSVEGIS TVIYPSLQTD VTQGRERTET PRPELKKDPY TVDEIPEKVT KDPFIGKTEE
VFSGMPLSTS SSESSVERTE SVSPALTIEK LTGKPTEARD VEEMTTLTRL ETDVTKSDKD
VTRVHLTHST LNVEVVTVSK WPGDEDNSTS KPLPSTEHAG FTKLPPVPLS TIGINGKDKE
IPSFTDGGGE YTLFPDGTPK PLEKVSEEDL ASGELTVTFH TSTSIGSAEK SASGEPTTGD
RFLPTTSTED QVINATAEGS ALGEDTEASK PLFTGPPFVH TSDVEELAFV NYSSTQEPTT
YVDISHTSPL SIIPKTEWSV LETSVPLEDE ILGKSDQDIL EQTHLEATMS PGALRTTGVS
QGETQEEPQT PGSPFPTFSS TAVMAKETTA FEEGEGSTYT PSEGRLMTGS ERVPGLETTP
VGTSYPPGAI TDQEVEMDTM VTLMSTIRPT VVSSTESEVI YEAEGSSPTE FASTLRPFQT
HVTQLMEETT EEGKKASLDY TDLGSGLFEP RATELPKFPS TPSDISVFTA IDSLHRTPPL
SPSSSFTEEQ RVFEEESSEK TTGDILPGES VTQHPVTTLI DIVAMKTESD IDHMTSKPPV
TQPTRPSVVE RKTTSKTQEL STSTPAAGTK FHPDINVYII EVRENKTGRL SDMIVSGHPI
DSESKEEEPC SEETDPLHDL FAEILPELPD SFEIDIYHSE EDEDGEEDCV NATDVTTTPS
VQYINGKQLV TTVPKDPEAA EARRGQYESV APSQNFPDSS ATDTHQFILA ETESSTTMQF
KKSKEGTELL EITWKPETYP ETPDHVSSGE PDVFPTLSSH DGKTTRWSES ITESSPNLEN
PVHKQPKPVP LFPEESSGEG AIEQASQETI LSRATEVALG KETDQSPTLS TSSILSSSVS
VNVLEEEPLT LTGISQTDES MSTIESWVEI TPSQTVKFSE SSSAPIIEGS GEVEENKNKI
FNMVTDLPQR DPTDTLSPLD MSKIMITNHH IYIPATIAPL DSKLPSPDAR PTTVWNSNST
SEWVSDKSFE GRKKKENEDE EGAVNAAHQG EVRAATERSD HLLLTPELES SNVDASSDLA
TWEGFILETT PTESEKEMAN STPVFRETIG VANVEAQPFE HSSSSHPRVQ EELTTLSGNP
PSLFTDLGSG DASTGMELIT ASLFTLDLES ETKVKKELPS TPSPSVEISS SFEPTGLTPS
TVLDIEIAGV MSQTSQKTLI SEISGKPTSQ SGVRDLYTGF PMGEDFSGDF SEYPTVSYPT
MKEETVGMGG SDDERVRDTQ TSSSIPTTSD NIYPVPDSKG PDSTVASTTA FPWEEVMSSA
EGSGEQLASV RSSVGPVLPL AVDIFSGTES PYFDEEFEEV AAVTEANERP TVLPTAASGN
TVDLTENGYI EVNSTMSLDF PQTMEPSKLW SKPEVNLDKQ EIGRETVTKE KAQGQKTFES
LHSSFAPEQT ILETQSLIET EFQTSDYSML TTLKTYITNK EVEEEGMSIA HMSTPGPGIK
DLESYTTHPE APGKSHSFSA TALVTESGAA RSVLMDSSTQ EEESIKLFQK GVKLTNKESN
ADLSFSGLGS GGALPPLPTT SVNLTDMKQI ISTLYAETSH MESLGTSILG DKMEDHERME
DVSSNEVRML ISKIGSISQD STEALDTTLS HTGTEEPTTS TLPFVKLMDL ERSPKQDPSG
GKRKPKTHRP QTMSGLISNE NSSASEAEEG ATSPTAFLPQ TYSVEMTKHF APSESQPSDL
FNVNSGEGSG EVDTLDLVYT SGTTQASSQG DSMLASHGFL EKHPEVSKTE AGATDVSPTA
SAMFLHHSEY KSSLYPTSTL PSTEPYKSPS EGIEDGLQDN IQFEGSTLKP SRRKTTESII
IDLDKEDSKD LGLTITESAI VKSLPELTSD KNIIIDIDHT KPVYEYIPGI QTDLDPEIKL
ESHGSSEESL QVQEKYEGAV TLSPTEESFE GSGDALLAGY TQAIYNESVT PNDGKQAEDI
SFSFATGIPV SSTETELHTF FPTASTLHIP SKLTTASPEI DKPNIEAISL DDIFESSTLS
DGQAIADQSE VISTLGHLEK TQEEYEEKKY GGPSFQPEFF SGVGEVLTDP PAYVSIGSTY
LIAQTLTELP NVVRPSDSTH YTEATPEVSS LAELSPQIPS SPFPVYVDNG VSKFPEVPHT
SAQPVSTVTS SQKSIESPFK EVHANIEETI KPLGGNVHRT EPPSMSRDPA LDVSEDESKH
KLLEELETSP TKPETSQDFP NKAKDHIPGE TVGMLAGIRT TESEPVITAD DMELGGATQQ
PHSASAAFRV ETGMVPQPIQ QEPERPTFPS LEINHETHTS LFGESILATS EKQVSQKILD
NSNQATVSST LDLHTAHALS PFSILDNSNE TAFLIGISEE SVEGTAVYLP GPDLCKTNPC
LNGGTCYPTE TSYVCTCAPG YSGDQCELDF DECHSNPCRN GATCVDGFNT FRCLCLPSYV
GALCEQDTET CDYGWHKFQG QCYKYFAHRR TWDAAERECR LQGAHLTSIL SHEEQMFVNR
VGHDYQWIGL NDKMFEHDFR WTDGSALQYE NWRPNQPDSF FSAGEDCVVI IWHENGQWND
VPCNYHLTYT CKKGTVACGQ PPVVENAKTF GKMKPRYEIN SLIRYHCKDG FIQRHLPTIR
CLGNGRWAMP KITCMNPSAY QRTYSKKYLK NSSSAKDNSI NTSKHEHRWS RRQETRR


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U1817m CLIA kit Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,Cspg2,Large fibroblast proteoglycan,Mouse,Mus musculus,PG-M,Vcan,Versican core protein 96T
E1817m ELISA Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,Cspg2,Large fibroblast proteoglycan,Mouse,Mus musculus,PG-M,Vcan,Versican core protein 96T
U1817m CLIA Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,Cspg2,Large fibroblast proteoglycan,Mouse,Mus musculus,PG-M,Vcan,Versican core protein 96T
E1817m ELISA kit Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,Cspg2,Large fibroblast proteoglycan,Mouse,Mus musculus,PG-M,Vcan,Versican core protein 96T
U1817b CLIA Bos taurus,Bovine,Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,VCAN,Versican 96T
E1817b ELISA Bos taurus,Bovine,Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,VCAN,Versican 96T
U1817h CLIA Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Homo sapiens,Human,Large fibroblast proteoglycan,PG-M,VCAN,Versican 96T
U1817c CLIA kit Chicken,Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,Gallus gallus,Large fibroblast proteoglycan,PG-M,VCAN,Versican core protein 96T
U1817c CLIA Chicken,Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,Gallus gallus,Large fibroblast proteoglycan,PG-M,VCAN,Versican core protein 96T
E1817c ELISA Chicken,Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,Gallus gallus,Large fibroblast proteoglycan,PG-M,VCAN,Versican core protein 96T
E1817c ELISA kit Chicken,Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,Gallus gallus,Large fibroblast proteoglycan,PG-M,VCAN,Versican core protein 96T
U1817r CLIA kit Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,Cspg2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,Rat,Rattus norvegicus,Vcan, 96T
E1817r ELISA kit Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,Cspg2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,Rat,Rattus norvegicus,Vcan 96T
E1817b ELISA kit Bos taurus,Bovine,Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,VCAN,Ver 96T
U1817h CLIA kit Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Homo sapiens,Human,Large fibroblast proteoglycan,PG-M,VCAN,Ver 96T
U1817r CLIA Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,Cspg2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,Rat,Rattus norvegicus,Vcan,Versi 96T
E1817r ELISA Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,Cspg2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,Rat,Rattus norvegicus,Vcan,Vers 96T
U1817b CLIA kit Bos taurus,Bovine,Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Large fibroblast proteoglycan,PG-M,VCAN,Vers 96T
E1817h ELISA kit Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Homo sapiens,Human,Large fibroblast proteoglycan,PG-M,VCAN,Ve 96T
E1817h ELISA Chondroitin sulfate proteoglycan 2,Chondroitin sulfate proteoglycan core protein 2,CSPG2,GHAP,Glial hyaluronate-binding protein,Homo sapiens,Human,Large fibroblast proteoglycan,PG-M,VCAN,Versica 96T
U1908h CLIA ACAN,AGC1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,Chondroitin sulfate proteoglycan 1,Chondroitin sulfate proteoglycan core protein 1,CSPCP,CSPG1,Homo sapiens,Human,MSK1 96T
E1908h ELISA ACAN,AGC1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,Chondroitin sulfate proteoglycan 1,Chondroitin sulfate proteoglycan core protein 1,CSPCP,CSPG1,Homo sapiens,Human,MSK 96T
E1908h ELISA kit ACAN,AGC1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,Chondroitin sulfate proteoglycan 1,Chondroitin sulfate proteoglycan core protein 1,CSPCP,CSPG1,Homo sapiens,Huma 96T
U1908h CLIA kit ACAN,AGC1,Aggrecan core protein,Cartilage-specific proteoglycan core protein,Chondroitin sulfate proteoglycan 1,Chondroitin sulfate proteoglycan core protein 1,CSPCP,CSPG1,Homo sapiens,Human 96T
EIAAB39885 Chondroitin sulfate proteoglycan core protein,Cytolytic granule proteoglycan core protein,PG19 core protein,Pgsg,Prg,Prg1,Proteoglycan 10K core protein,Rat,Rattus norvegicus,Secretory granule proteogl


 

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