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Putative vitellogenin receptor (Protein yolkless) (YL)

 YL_DROME                Reviewed;        1984 AA.
P98163; Q86P52; Q9VY56;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
10-MAY-2004, sequence version 2.
18-JUL-2018, entry version 159.
RecName: Full=Putative vitellogenin receptor;
AltName: Full=Protein yolkless;
Short=YL;
Flags: Precursor;
Name=yl; ORFNames=CG1372;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
TISSUE=Ovary;
PubMed=7878005; DOI=10.1073/pnas.92.5.1485;
Schonbaum C.P., Lee S., Mahowald A.P.;
"The Drosophila yolkless gene encodes a vitellogenin receptor
belonging to the low density lipoprotein receptor superfamily.";
Proc. Natl. Acad. Sci. U.S.A. 92:1485-1489(1995).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[3]
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
STRAIN=Berkeley; TISSUE=Embryo;
Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W.,
Champe M., Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E.,
George R.A., Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G.,
Miranda A., Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S.,
Patel S., Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M.,
Celniker S.E.;
Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1926, AND IDENTIFICATION
BY MASS SPECTROMETRY.
TISSUE=Embryo;
PubMed=18327897; DOI=10.1021/pr700696a;
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
J. Proteome Res. 7:1675-1682(2008).
-!- FUNCTION: Involved in uptake of vitellogenin by endocytosis.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=B;
IsoId=P98163-1; Sequence=Displayed;
Note=No experimental confirmation available.;
Name=A;
IsoId=P98163-2; Sequence=VSP_010300;
-!- TISSUE SPECIFICITY: Ovary.
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EMBL; U13637; AAB60217.1; -; mRNA.
EMBL; AE014298; AAF48349.2; -; Genomic_DNA.
EMBL; AE014298; AAS65339.1; -; Genomic_DNA.
EMBL; BT003478; AAO39481.1; -; mRNA.
PIR; T13171; T13171.
RefSeq; NP_511151.2; NM_078596.3. [P98163-2]
RefSeq; NP_996433.1; NM_206710.2. [P98163-1]
ProteinModelPortal; P98163; -.
BioGrid; 58737; 8.
IntAct; P98163; 8.
MINT; P98163; -.
STRING; 7227.FBpp0073715; -.
iPTMnet; P98163; -.
PaxDb; P98163; -.
PRIDE; P98163; -.
EnsemblMetazoa; FBtr0073897; FBpp0073714; FBgn0004649. [P98163-2]
EnsemblMetazoa; FBtr0073898; FBpp0073715; FBgn0004649. [P98163-1]
GeneID; 32367; -.
KEGG; dme:Dmel_CG1372; -.
CTD; 32367; -.
FlyBase; FBgn0004649; yl.
eggNOG; ENOG410IPSU; Eukaryota.
eggNOG; ENOG410YUAB; LUCA.
GeneTree; ENSGT00760000118968; -.
InParanoid; P98163; -.
OMA; DEHDKCG; -.
OrthoDB; EOG091G00V3; -.
PhylomeDB; P98163; -.
GenomeRNAi; 32367; -.
PRO; PR:P98163; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0004649; -.
Genevisible; P98163; DM.
GO; GO:0030135; C:coated vesicle; IDA:FlyBase.
GO; GO:0031410; C:cytoplasmic vesicle; IDA:FlyBase.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0008196; F:vitellogenin receptor activity; ISS:FlyBase.
GO; GO:0048477; P:oogenesis; TAS:FlyBase.
CDD; cd00112; LDLa; 13.
Gene3D; 2.120.10.30; -; 3.
InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
InterPro; IPR026823; cEGF.
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; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
Pfam; PF12662; cEGF; 1.
Pfam; PF07645; EGF_CA; 1.
Pfam; PF00057; Ldl_recept_a; 12.
Pfam; PF00058; Ldl_recept_b; 3.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 7.
SMART; SM00179; EGF_CA; 4.
SMART; SM00192; LDLa; 13.
SMART; SM00135; LY; 10.
SUPFAM; SSF57424; SSF57424; 13.
PROSITE; PS00010; ASX_HYDROXYL; 2.
PROSITE; PS01186; EGF_2; 3.
PROSITE; PS50026; EGF_3; 3.
PROSITE; PS01187; EGF_CA; 2.
PROSITE; PS01209; LDLRA_1; 12.
PROSITE; PS50068; LDLRA_2; 13.
PROSITE; PS51120; LDLRB; 10.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein; Membrane;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix.
SIGNAL 1 ? {ECO:0000255}.
CHAIN ? 1984 Putative vitellogenin receptor.
/FTId=PRO_0000007781.
TOPO_DOM ? 1800 Extracellular. {ECO:0000255}.
TRANSMEM 1801 1821 Helical. {ECO:0000255}.
TOPO_DOM 1822 1984 Cytoplasmic. {ECO:0000255}.
DOMAIN 89 125 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 128 167 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 183 221 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 226 263 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 265 305 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 306 347 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 348 388 EGF-like 2; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 441 485 LDL-receptor class B 1.
REPEAT 486 528 LDL-receptor class B 2.
REPEAT 529 572 LDL-receptor class B 3.
REPEAT 573 614 LDL-receptor class B 4.
REPEAT 615 649 LDL-receptor class B 5.
DOMAIN 660 701 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 750 792 LDL-receptor class B 6.
REPEAT 793 836 LDL-receptor class B 7.
REPEAT 884 925 LDL-receptor class B 8.
REPEAT 934 976 LDL-receptor class B 9.
DOMAIN 984 1026 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1024 1063 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1073 1110 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1117 1153 LDL-receptor class A 8.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1157 1194 LDL-receptor class A 9.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1197 1233 LDL-receptor class A 10.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1242 1280 LDL-receptor class A 11.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1282 1319 LDL-receptor class A 12.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1339 1376 LDL-receptor class A 13.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1375 1417 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1418 1457 EGF-like 6; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 1588 1637 LDL-receptor class B 10.
REPEAT 1638 1687 LDL-receptor class B 11.
DOMAIN 1734 1770 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
SITE 1837 1837 Critical for endocytosis. {ECO:0000255}.
SITE 1878 1878 Critical for endocytosis. {ECO:0000255}.
SITE 1892 1892 Critical for endocytosis. {ECO:0000255}.
MOD_RES 1926 1926 Phosphoserine.
{ECO:0000269|PubMed:18327897}.
CARBOHYD 30 30 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 384 384 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 429 429 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 666 666 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 749 749 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 782 782 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1022 1022 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1240 1240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1265 1265 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1326 1326 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1475 1475 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1490 1490 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 90 102 {ECO:0000250}.
DISULFID 97 115 {ECO:0000250}.
DISULFID 109 124 {ECO:0000250}.
DISULFID 129 144 {ECO:0000250}.
DISULFID 137 157 {ECO:0000250}.
DISULFID 151 166 {ECO:0000250}.
DISULFID 184 197 {ECO:0000250}.
DISULFID 191 210 {ECO:0000250}.
DISULFID 204 220 {ECO:0000250}.
DISULFID 227 239 {ECO:0000250}.
DISULFID 234 253 {ECO:0000250}.
DISULFID 247 262 {ECO:0000250}.
DISULFID 266 281 {ECO:0000250}.
DISULFID 275 294 {ECO:0000250}.
DISULFID 288 304 {ECO:0000250}.
DISULFID 310 321 {ECO:0000250}.
DISULFID 315 331 {ECO:0000250}.
DISULFID 333 346 {ECO:0000250}.
DISULFID 352 363 {ECO:0000250}.
DISULFID 359 372 {ECO:0000250}.
DISULFID 374 387 {ECO:0000250}.
DISULFID 664 673 {ECO:0000250}.
DISULFID 669 685 {ECO:0000250}.
DISULFID 687 700 {ECO:0000250}.
DISULFID 988 999 {ECO:0000250}.
DISULFID 995 1009 {ECO:0000250}.
DISULFID 1011 1025 {ECO:0000250}.
DISULFID 1031 1040 {ECO:0000250}.
DISULFID 1035 1053 {ECO:0000250}.
DISULFID 1047 1062 {ECO:0000250}.
DISULFID 1074 1087 {ECO:0000250}.
DISULFID 1081 1100 {ECO:0000250}.
DISULFID 1094 1109 {ECO:0000250}.
DISULFID 1118 1130 {ECO:0000250}.
DISULFID 1125 1143 {ECO:0000250}.
DISULFID 1137 1152 {ECO:0000250}.
DISULFID 1158 1170 {ECO:0000250}.
DISULFID 1165 1183 {ECO:0000250}.
DISULFID 1177 1193 {ECO:0000250}.
DISULFID 1198 1210 {ECO:0000250}.
DISULFID 1205 1223 {ECO:0000250}.
DISULFID 1217 1232 {ECO:0000250}.
DISULFID 1243 1257 {ECO:0000250}.
DISULFID 1250 1270 {ECO:0000250}.
DISULFID 1264 1279 {ECO:0000250}.
DISULFID 1283 1296 {ECO:0000250}.
DISULFID 1290 1309 {ECO:0000250}.
DISULFID 1303 1318 {ECO:0000250}.
DISULFID 1340 1352 {ECO:0000250}.
DISULFID 1347 1365 {ECO:0000250}.
DISULFID 1359 1375 {ECO:0000250}.
DISULFID 1379 1392 {ECO:0000250}.
DISULFID 1388 1401 {ECO:0000250}.
DISULFID 1403 1416 {ECO:0000250}.
DISULFID 1422 1432 {ECO:0000250}.
DISULFID 1428 1441 {ECO:0000250}.
DISULFID 1443 1456 {ECO:0000250}.
DISULFID 1738 1747 {ECO:0000250}.
DISULFID 1743 1756 {ECO:0000250}.
DISULFID 1758 1769 {ECO:0000250}.
VAR_SEQ 1925 1984 ESKLHALDGGGAGGDGDGGRGVGRQVPDILVADMDDDAAKS
AGQFGGNYAGNDANARFVS -> VSSDGGQMAVEDM (in
isoform A). {ECO:0000303|Ref.4}.
/FTId=VSP_010300.
CONFLICT 457 457 K -> E (in Ref. 4; AAO39481).
{ECO:0000305}.
CONFLICT 470 470 T -> S (in Ref. 4; AAO39481).
{ECO:0000305}.
CONFLICT 727 727 R -> A (in Ref. 1; AAB60217).
{ECO:0000305}.
CONFLICT 1068 1068 R -> H (in Ref. 1; AAB60217).
{ECO:0000305}.
CONFLICT 1077 1077 N -> S (in Ref. 1; AAB60217).
{ECO:0000305}.
CONFLICT 1156 1156 S -> L (in Ref. 1; AAB60217).
{ECO:0000305}.
CONFLICT 1203 1203 Q -> H (in Ref. 1; AAB60217).
{ECO:0000305}.
CONFLICT 1207 1207 L -> S (in Ref. 1; AAB60217).
{ECO:0000305}.
CONFLICT 1261 1261 T -> A (in Ref. 1; AAB60217).
{ECO:0000305}.
CONFLICT 1519 1519 I -> V (in Ref. 1; AAB60217).
{ECO:0000305}.
CONFLICT 1696 1696 V -> M (in Ref. 1; AAB60217).
{ECO:0000305}.
CONFLICT 1884 1884 T -> S (in Ref. 1; AAB60217).
{ECO:0000305}.
CONFLICT 1944 1944 R -> C (in Ref. 1; AAB60217).
{ECO:0000305}.
SEQUENCE 1984 AA; 219521 MW; 0B6F9CF4EFC4914C CRC64;
MCQAEHQVHP SEQRIRVESP KMTASRRGFN LTSQTRAHPS SGGSTSSRYG NCQRTHLIIN
GRHVAISLLL LVGLCGGTAA GTPGSADTRC DAGQFQCRDG GCILQAKMCD GRGDCKDSSD
ELDCDYRLCR PPHWFPCAQP HGACLAAELM CNGIDNCPGG EDELNCPVRP GFRFGDTAHR
MRSCSKYEFM CQQDRTCIPI DFMCDGRPDC TDKSDEVAGC KQAEITCPGE GHLCANGRCL
RRKQWVCDGV DDCGDGSDER GCLNLCEPQK GKFLCRNRET CLTLSEVCDG HSDCSDGSDE
TDLCHSKPDC DAKKCALGAK CHMMPASGAE CFCPKGFRLA KFEDKCEDVD ECKEQDDLCS
QGCENTSGGY RCVCDAGYLL DKDNRTCRAV VYGSKEQQPL LLYTTQMTIM GMHLREDNVR
NHVYQVAGNL SKVIGVAYDG SHIYWTNIQN EAESIVKANG DGSNAEILLT SGLDAPEDLA
VDWLTQNIYF SDNIMRHIAV CSNDGLNCAV LVTQDVHQPR SLAVWPQKGL MFWTDWGEKP
MIGRASMDGS RSRPIVSDNI EWPNGIALDM HQQRIYWVDA KLGSVQTVRP DGTGRRTVLD
GMLKHPYGLA IFEDQLYWSD WATKSVHACH KFSGKDHRIL AKDRTIYAVH IYHPAKQPNS
PHGCENATCS HLCLLAEPEI GGHSCACPDG MRLAPDHRRC MLMEKRQRLF IGLGQVLLEI
EHTAFGRHQV SKSYTLPCLI NEMVYNRING SLIIADNDQR LILEFQPESH ESNVLVRSNL
GNVSALAFDH LSRNLYWADT ERAVIEVLSL QTRHRALIRF FPGQEVPIGL TVMPAEGYLY
VVLKAKRHSH IDKIPLSGKG EQVHVFEDDL GDDDIKLVTD YETQTIFWSD SDLGRISYSN
YRVPHSQIFR GKLRRPYSLA MVHHDLFWNE LGTPRIYWTH KSNMGPRKVI DIMEKDDPAA
IMPYVPVATP NGIPLAASSP VGQESHPCQQ QNGGCSHICV GEGPYHSICL CPAGFVYRDA
GNRTCVEALD CEFRCHSGEC LTMNHRCNGR RDCVDNSDEM NCDEEHRRKP KVLCSPNQFA
CHSGEQCVDK ERRCDNRKDC HDHSDEQHCE KFDKSKKCHV HQHGCDNGKC VDSSLVCDGT
NDCGDNSDEL LCEATSRCEP GMFQCGSGSC IAGSWECDGR IDCSDGSDEH DKCVHRSCPP
DMQRCLLGQC LDRSLVCDGH NDCGDKSDEL NCGTDSSTMN ISCAEDQYQC TSNLKICLPS
TVRCNGTTEC PRGEDEADCG DVCSIYEFKC RSGRECIRRE FRCDGQKDCG DGSDELSCEL
EKGHHNQSQI QPWSTSSRSC RPHLFDCQDG ECVDLSRVCN NFPDCTNGHD EGPKCATACR
SASGRQVCQH KCRATPAGAV CSCFDGYRLD ADQKSCLDID ECQEQQPCAQ LCENTLGGYQ
CQCHADFMLR QDRVSCKSLQ SGATLLFSSF NEVRNLSEQP VMLNVAWSAN DSRITGFDLA
MHRQMGYFSA EDEGIVYQID LQTKVIVRAL GLPAPTKLSV DWVTGNVYVL SGAQEIQACS
FVGRMCGRIV HVKSPRHVKH LAVDGYHARI FYIVIRTEGY GQTSSEIHMA RLDGSRRDML
LQRSESFMTA LTTDPHQQLL YFVDQHMRTL ERISYRLKTG PMRRPEIMLQ KSNALMHPSG
LSVYENNAFI VNLGSVEAVQ CALYGSRICH KISINVLNAQ DIVVAGRSRQ PQKASHPCAH
AHCHGLCLQA DYGYECMCGN RLVAEGERCP HGSGNEVAVL GAVNSLELEH EHEQNGHFHW
LMALFVLAAG SLIAGLGYMY YQYRQRGHTD LNINMHFQNP LATLGGTKAF LEHERAEAGV
GFTTETGTVS SRGSNDTFTT TSATSSFAAQ QFSVPNALQR LLRPRQSASG DPMAQELLLE
SPSRESKLHA LDGGGAGGDG DGGRGVGRQV PDILVADMDD DAAKSAGQFG GNYAGNDANA
RFVS


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EIAAB45812 Chicken,Gallus gallus,Major vitellogenin,Vitellogenin II,Vitellogenin-2,VTG2,VTGII
EIAAB27756 Homo sapiens,Human,NPY Y1-like receptor,NPY1RL,NPY6R,NPY6-R,PP2,Putative neuropeptide Y receptor type 6,Putative pancreatic polypeptide receptor 2,Y2B
EIAAB13188 ER lumen protein retaining receptor 1,ERD2.1,Homo sapiens,Human,KDEL endoplasmic reticulum protein retention receptor 1,KDEL receptor 1,KDELR1,Putative MAPK-activating protein PM23
V01403101-500 Antibodies Vitellogenin monoclonal mouse anti-carp vitellogenin Purified ND-2D3 500 μl
V01411201-500 Antibodies Vitellogenin polyclonal rabbit anti-turbot vitellogenin Purified CK-4B3 CS-2 500 μl
V01040101-500 Antibodies Vitellogenin monoclonal mouse anti-bird vitellogenin Purified ND-3C3 500 μl
V01412201-100 Antibodies Vitellogenin polyclonal rabbit anti-wolffish vitellogenin Purified CK-4B3 CS-3 100 μl
V01402102-100 Antibodies Vitellogenin monoclonal mouse anti-salmon vitellogenin Purified KB-1 100 μl
V01408102-100 Antibodies Vitellogenin monoclonal mouse anti-zebrafish vitellogenin Purified ND-3C3 JE-2A6 100 μl
V01403101-100 Antibodies Vitellogenin monoclonal mouse anti-carp vitellogenin Purified ND-2D3 100 μl
V01408102-500 Antibodies Vitellogenin monoclonal mouse anti-zebrafish vitellogenin Purified ND-3G6 JE-2A6 500 μl
V01402102-500 Antibodies Vitellogenin monoclonal mouse anti-salmon vitellogenin Purified KB-1 500 μl
V01406201-500 Antibodies Vitellogenin polyclonal rabbit anti-cod vitellogenin Purified JE-10D4 CS-1 500 μl
V01411201-100 Antibodies Vitellogenin polyclonal rabbit anti-turbot vitellogenin Purified JE-8D6 CS-2 100 μl
V01402101-500 Antibodies Vitellogenin monoclonal mouse anti-salmon vitellogenin Purified BN-5 500 μl
V01413101-500 Antibodies Vitellogenin monoclonal mouse anti-medaka vitellogenin Purified BN-5 CK-4B3 500 μl
V01407101-500 Antibodies Vitellogenin monoclonal mouse anti-killifish vitellogenin Purified ND-5F8 500 μl
V01402101-100 Antibodies Vitellogenin monoclonal mouse anti-salmon vitellogenin Purified BN-5 100 μl
V01041101-500 Antibodies Vitellogenin monoclonal mouse anti-alligator vitellogenin Purified ND-1E8 500 μl
V01413101-100 Antibodies Vitellogenin monoclonal mouse anti-medaka vitellogenin Purified ND-1E8 CK-4B3 100 μl


 

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