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C-type mannose receptor 2 (Lectin lambda) (Macrophage mannose receptor 2) (CD antigen CD280)

 MRC2_MOUSE              Reviewed;        1479 AA.
Q64449; A2AAB0; Q6ZQ64; Q8C6P0;
07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
28-FEB-2018, entry version 140.
RecName: Full=C-type mannose receptor 2;
AltName: Full=Lectin lambda;
AltName: Full=Macrophage mannose receptor 2;
AltName: CD_antigen=CD280;
Flags: Precursor;
Name=Mrc2; Synonyms=Kiaa0709;
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] (ISOFORM 1), TISSUE SPECIFICITY, AND
DEVELOPMENTAL STAGE.
PubMed=8702911; DOI=10.1074/jbc.271.35.21323;
Wu K., Yuan J., Lasky L.A.;
"Characterization of a novel member of the macrophage mannose receptor
type C lectin family.";
J. Biol. Chem. 271:21323-21330(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Oviduct;
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 MRNA] OF 479-1479 (ISOFORM 1).
TISSUE=Embryonic tail;
PubMed=14621295; DOI=10.1093/dnares/10.4.167;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
Saga Y., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
III. The complete nucleotide sequences of 500 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:167-180(2003).
[5]
DISRUPTION PHENOTYPE.
PubMed=12835757; DOI=10.1038/sj.embor.embor882;
East L., McCarthy A., Wienke D., Sturge J., Ashworth A., Isacke C.M.;
"A targeted deletion in the endocytic receptor gene Endo180 results in
a defect in collagen uptake.";
EMBO Rep. 4:710-716(2003).
[6]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=12668656; DOI=10.1083/jcb.200211091;
Engelholm L.H., List K., Netzel-Arnett S., Cukierman E., Mitola D.J.,
Aaronson H., Kjoller L., Larsen J.K., Yamada K.M., Strickland D.K.,
Holmbeck K., Danoe K., Birkedal-Hansen H., Behrendt N., Bugge T.H.;
"uPARAP/Endo180 is essential for cellular uptake of collagen and
promotes fibroblast collagen adhesion.";
J. Cell Biol. 160:1009-1015(2003).
[7]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=14729061; DOI=10.1016/j.yexcr.2003.10.008;
Kjoller L., Engelholm L.H., Hoyer-Hansen M., Danoe K., Bugge T.H.,
Behrendt N.;
"uPARAP/endo180 directs lysosomal delivery and degradation of collagen
IV.";
Exp. Cell Res. 293:106-116(2004).
[8]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=15967816; DOI=10.1083/jcb.200411153;
Curino A.C., Engelholm L.H., Yamada S.S., Holmbeck K., Lund L.R.,
Molinolo A.A., Behrendt N., Nielsen B.S., Bugge T.H.;
"Intracellular collagen degradation mediated by uPARAP/Endo180 is a
major pathway of extracellular matrix turnover during malignancy.";
J. Cell Biol. 169:977-985(2005).
[9]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-139 AND ASN-363.
TISSUE=Myoblast;
PubMed=19656770; DOI=10.1074/mcp.M900195-MCP200;
Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I.,
Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E.,
Wollscheid B.;
"The mouse C2C12 myoblast cell surface N-linked glycoproteome:
identification, glycosite occupancy, and membrane orientation.";
Mol. Cell. Proteomics 8:2555-2569(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, Spleen,
and Testis;
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).
[11]
STRUCTURE BY ELECTRON MICROSCOPY (18 ANGSTROMS).
PubMed=12856000; DOI=10.1038/sj.embor.embor898;
Rivera-Calzada A., Robertson D., MacFadyen J.R., Boskovic J.,
Isacke C.M., Llorca O.;
"Three-dimensional interplay among the ligand-binding domains of the
urokinase-plasminogen-activator-receptor-associated protein,
Endo180.";
EMBO Rep. 4:807-812(2003).
-!- FUNCTION: May play a role as endocytotic lectin receptor
displaying calcium-dependent lectin activity. Internalizes
glycosylated ligands from the extracellular space for release in
an endosomal compartment via clathrin-mediated endocytosis. May be
involved in plasminogen activation system controlling the
extracellular level of PLAUR/PLAU, and thus may regulate protease
activity at the cell surface. May contribute to cellular uptake,
remodeling and degradation of extracellular collagen matrices. May
participate in remodeling of extracellular matrix cooperating with
the matrix metalloproteinases (MMPs).
{ECO:0000269|PubMed:12668656, ECO:0000269|PubMed:14729061,
ECO:0000269|PubMed:15967816}.
-!- SUBUNIT: Interacts directly with PLAUR/UPAR and PLAU/pro-UPA to
form a tri-molecular complex. Interacts with collagen V and with
C-terminal region of type I collagen/COL1A1 (By similarity).
{ECO:0000250}.
-!- SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane
protein.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q64449-1; Sequence=Displayed;
Name=2;
IsoId=Q64449-2; Sequence=VSP_017223, VSP_017224;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Highly expressed in heart, lung and kidney,
but little or no expression in brain, thymus or adult liver.
Expressed at highly endothelialized sites such as those in choroid
plexus and kidney glomerulai as well as in chondrocytes in
cartilaginous regions of the embryo. {ECO:0000269|PubMed:8702911}.
-!- DEVELOPMENTAL STAGE: Highly expressed at day 7 of embryonic
development and detected throughout the later stages of embryonic
development. {ECO:0000269|PubMed:8702911}.
-!- DOMAIN: C-type lectin domains 3 to 8 are not required for calcium-
dependent binding of mannose, fucose and N-acetylglucosamine. C-
type lectin domain 2 is responsible for sugar-binding in a
calcium-dependent manner (By similarity). {ECO:0000250}.
-!- DOMAIN: Fibronectin type-II domain mediates collagen-binding.
{ECO:0000250}.
-!- DOMAIN: Ricin B-type lectin domain contacts with the second C-type
lectin domain.
-!- PTM: Phosphorylated. {ECO:0000250}.
-!- DISRUPTION PHENOTYPE: Mice show impaired mammary tumor growth.
Tumors from mice lacking Mrc2 display an abrogation of cellular
collagen uptake, a fibrotic state characterized by the
accumulation of both basement membrane and interstitial collagens,
and an overall tumor size reduction, despite the collagen
accumulation. Fibroblasts from mice lacking Mrc2 display a severe
impairment of internalization of collagen IV and V and thus,
exhibit a general deficiency in uptake and delivery of collagens
to vesicular compartments. Fibroblasts also have diminished
initial adhesion to collagen as well as impaired migration on
fibrillar collagen. Mice with a targeted deletion of Mrc2 exon 2-6
are phenotypically normal, healthy and fertile. This deletion
resulted in expression of a protein that lacks the ricin B-type
lectin domain, the fibronectin type-II domain and the first C-type
lectin domain. Fibroblasts from these mice display C-type lectin
activity, but have a defect in collagen-binding and
internalization, and an impaired migratory phenotype.
{ECO:0000269|PubMed:12668656, ECO:0000269|PubMed:12835757,
ECO:0000269|PubMed:14729061, ECO:0000269|PubMed:15967816}.
-!- SEQUENCE CAUTION:
Sequence=AAC52729.1; Type=Frameshift; Positions=120, 145; Evidence={ECO:0000305};
Sequence=BAC35672.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
Note=Endo180;
URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Ctlect_252";
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EMBL; U56734; AAC52729.1; ALT_FRAME; mRNA.
EMBL; AK054150; BAC35672.1; ALT_INIT; mRNA.
EMBL; AL645684; CAM22193.1; -; Genomic_DNA.
EMBL; AL645471; CAM22193.1; JOINED; Genomic_DNA.
EMBL; AL645572; CAM22193.1; JOINED; Genomic_DNA.
EMBL; AL645572; CAM22804.1; -; Genomic_DNA.
EMBL; AL645471; CAM22804.1; JOINED; Genomic_DNA.
EMBL; AL645684; CAM22804.1; JOINED; Genomic_DNA.
EMBL; AL645471; CAM24832.1; -; Genomic_DNA.
EMBL; AL645572; CAM24832.1; JOINED; Genomic_DNA.
EMBL; AL645684; CAM24832.1; JOINED; Genomic_DNA.
EMBL; AK129195; BAC98005.1; -; mRNA.
CCDS; CCDS25539.1; -. [Q64449-1]
PIR; T42710; T42710.
RefSeq; NP_032652.3; NM_008626.3. [Q64449-1]
UniGene; Mm.235616; -.
ProteinModelPortal; Q64449; -.
SMR; Q64449; -.
STRING; 10090.ENSMUSP00000097909; -.
iPTMnet; Q64449; -.
PhosphoSitePlus; Q64449; -.
PaxDb; Q64449; -.
PeptideAtlas; Q64449; -.
PRIDE; Q64449; -.
Ensembl; ENSMUST00000100335; ENSMUSP00000097909; ENSMUSG00000020695. [Q64449-1]
GeneID; 17534; -.
KEGG; mmu:17534; -.
UCSC; uc007lxi.1; mouse. [Q64449-1]
CTD; 9902; -.
MGI; MGI:107818; Mrc2.
eggNOG; ENOG410KDF3; Eukaryota.
eggNOG; ENOG410XQ89; LUCA.
GeneTree; ENSGT00720000108514; -.
HOGENOM; HOG000231191; -.
HOVERGEN; HBG053606; -.
InParanoid; Q64449; -.
KO; K06560; -.
OMA; HEQTYIN; -.
OrthoDB; EOG091G0EGC; -.
TreeFam; TF316663; -.
Reactome; R-MMU-1236978; Cross-presentation of soluble exogenous antigens (endosomes).
PRO; PR:Q64449; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020695; -.
CleanEx; MM_MRC2; -.
ExpressionAtlas; Q64449; baseline and differential.
Genevisible; Q64449; MM.
GO; GO:0009986; C:cell surface; ISO:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030246; F:carbohydrate binding; ISO:MGI.
GO; GO:0005518; F:collagen binding; ISO:MGI.
GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
GO; GO:0030574; P:collagen catabolic process; ISO:MGI.
GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
CDD; cd03590; CLECT_DC-SIGN_like; 1.
CDD; cd00062; FN2; 1.
CDD; cd00161; RICIN; 1.
Gene3D; 2.10.10.10; -; 1.
Gene3D; 3.10.100.10; -; 8.
InterPro; IPR001304; C-type_lectin-like.
InterPro; IPR016186; C-type_lectin-like/link_sf.
InterPro; IPR018378; C-type_lectin_CS.
InterPro; IPR033989; CD209-like_CTLD.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR000562; FN_type2_dom.
InterPro; IPR036943; FN_type2_sf.
InterPro; IPR013806; Kringle-like.
InterPro; IPR035992; Ricin_B-like_lectins.
InterPro; IPR000772; Ricin_B_lectin.
Pfam; PF00040; fn2; 1.
Pfam; PF00059; Lectin_C; 8.
SMART; SM00034; CLECT; 8.
SMART; SM00059; FN2; 1.
SMART; SM00458; RICIN; 1.
SUPFAM; SSF50370; SSF50370; 1.
SUPFAM; SSF56436; SSF56436; 8.
SUPFAM; SSF57440; SSF57440; 1.
PROSITE; PS00615; C_TYPE_LECTIN_1; 3.
PROSITE; PS50041; C_TYPE_LECTIN_2; 8.
PROSITE; PS00023; FN2_1; 1.
PROSITE; PS51092; FN2_2; 1.
PROSITE; PS50231; RICIN_B_LECTIN; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Complete proteome; Disulfide bond;
Endocytosis; Glycoprotein; Isopeptide bond; Lectin; Membrane;
Phosphoprotein; Receptor; Reference proteome; Repeat; Signal;
Transmembrane; Transmembrane helix; Ubl conjugation.
SIGNAL 1 30 {ECO:0000255}.
CHAIN 31 1479 C-type mannose receptor 2.
/FTId=PRO_0000046079.
TOPO_DOM 31 1413 Extracellular. {ECO:0000255}.
TRANSMEM 1414 1434 Helical. {ECO:0000255}.
TOPO_DOM 1435 1479 Cytoplasmic. {ECO:0000255}.
DOMAIN 37 190 Ricin B-type lectin.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
DOMAIN 181 229 Fibronectin type-II.
{ECO:0000255|PROSITE-ProRule:PRU00479}.
DOMAIN 243 359 C-type lectin 1. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 388 504 C-type lectin 2. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 527 643 C-type lectin 3. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 677 808 C-type lectin 4. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 831 950 C-type lectin 5. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 978 1106 C-type lectin 6. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 1131 1242 C-type lectin 7. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
DOMAIN 1271 1391 C-type lectin 8. {ECO:0000255|PROSITE-
ProRule:PRU00040}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 139 139 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 363 363 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19656770}.
CARBOHYD 1028 1028 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1348 1348 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 92 111 {ECO:0000250}.
DISULFID 186 212 {ECO:0000250}.
DISULFID 200 227 {ECO:0000250}.
DISULFID 265 358 {ECO:0000250}.
DISULFID 334 350 {ECO:0000250}.
DISULFID 409 503 {ECO:0000250}.
DISULFID 480 495 {ECO:0000250}.
DISULFID 617 634 {ECO:0000250}.
DISULFID 703 807 {ECO:0000250}.
DISULFID 784 799 {ECO:0000250}.
DISULFID 852 949 {ECO:0000250}.
DISULFID 926 941 {ECO:0000250}.
DISULFID 1077 1097 {ECO:0000250}.
DISULFID 1219 1233 {ECO:0000250}.
DISULFID 1367 1382 {ECO:0000250}.
CROSSLNK 1141 1141 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000250|UniProtKB:Q9UBG0}.
VAR_SEQ 173 180 EVYTIQGN -> GEGSIAKS (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_017223.
VAR_SEQ 181 1479 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_017224.
CONFLICT 66 66 V -> F (in Ref. 1; AAC52729).
{ECO:0000305}.
CONFLICT 519 519 G -> D (in Ref. 1; AAC52729).
{ECO:0000305}.
CONFLICT 869 869 D -> G (in Ref. 1; AAC52729).
{ECO:0000305}.
CONFLICT 984 984 R -> Q (in Ref. 4; BAC98005).
{ECO:0000305}.
SEQUENCE 1479 AA; 167074 MW; AFC78624FE331E32 CRC64;
MVPIRPALAP WPRHLLRCVL LLGGLRLGHP ADSAAALLEP DVFLIFSQGM QGCLEAQGVQ
VRVTPVCNAS LPAQRWKWVS RNRLFNLGAT QCLGTGWPVT NTTVSLGMYE CDREALSLRW
QCRTLGDQLS LLLGARASNA SKPGTLERGD QTRSGHWNIY GSEEDLCARP YYEVYTIQGN
SHGKPCTIPF KYDNQWFHGC TSTGREDGHL WCATTQDYGK DERWGFCPIK SNDCETFWDK
DQLTDSCYQF NFQSTLSWRE AWASCEQQGA DLLSITEIHE QTYINGLLTG YSSTLWIGLN
DLDTSGGWQW SDNSPLKYLN WESDQPDNPG EENCGVIRTE SSGGWQNHDC SIALPYVCKK
KPNATVEPIQ PDRWTNVKVE CDPSWQPFQG HCYRLQAEKR SWQESKRACL RGGGDLLSIH
SMAELEFITK QIKQEVEELW IGLNDLKLQM NFEWSDGSLV SFTHWHPFEP NNFRDSLEDC
VTIWGPEGRW NDSPCNQSLP SICKKAGRLS QGAAEEDHGC RKGWTWHSPS CYWLGEDQVI
YSDARRLCTD HGSQLVTITN RFEQAFVSSL IYNWEGEYFW TALQDLNSTG SFRWLSGDEV
IYTHWNRDQP GYRRGGCVAL ATGSAMGLWE VKNCTSFRAR YICRQSLGTP VTPELPGPDP
TPSLTGSCPQ GWVSDPKLRH CYKVFSSERL QEKKSWIQAL GVCRELGAQL LSLASYEEEH
FVAHMLNKIF GESEPESHEQ HWFWIGLNRR DPREGHSWRW SDGLGFSYHN FARSRHDDDD
IRGCAVLDLA SLQWVPMQCQ TQLDWICKIP RGVDVREPDI GRQGRLEWVR FQEAEYKFFE
HHSSWAQAQR ICTWFQADLT SVHSQAELDF LGQNLQKLSS DQEQHWWIGL HTLESDGRFR
WTDGSIINFI SWAPGKPRPI GKDKKCVYMT ARQEDWGDQR CHTALPYICK RSNSSGETQP
QDLPPSALGG CPSGWNQFLN KCFRIQGQDP QDRVKWSEAQ FSCEQQEAQL VTIANPLEQA
FITASLPNVT FDLWIGLHAS QRDFQWIEQE PLLYTNWAPG EPSGPSPAPS GTKPTSCAVI
LHSPSAHFTG RWDDRSCTEE THGFICQKGT DPSLSPSPAA TPPAPGAELS YLNHTFRLLQ
KPLRWKDALL LCESRNASLA HVPDPYTQAF LTQAARGLQT PLWIGLASEE GSRRYSWLSE
EPLNYVSWQD EEPQHSGGCA YVDVDGTWRT TSCDTKLQGA VCGVSRGPPP RRINYRGSCP
QGLADSSWIP FREHCYSFHM EVLLGHKEAL QRCQKAGGTV LSILDEMENV FVWEHLQTAE
AQSRGAWLGM NFNPKGGTLV WQDNTAVNYS NWGPPGLGPS MLSHNSCYWI QSSSGLWRPG
ACTNITMGVV CKLPRVEENS FLPSAALPES PVALVVVLTA VLLLLALMTA ALILYRRRQS
AERGSFEGAR YSRSSHSGPA EATEKNILVS DMEMNEQQE


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U1542h CLIA CLEC13D,CLEC13DL,C-type lectin domain family 13 member D,C-type lectin domain family 13 member D-like,Homo sapiens,Human,Macrophage mannose receptor 1,Macrophage mannose receptor 1-like protein 1 96T
E1542h ELISA CLEC13D,CLEC13DL,C-type lectin domain family 13 member D,C-type lectin domain family 13 member D-like,Homo sapiens,Human,Macrophage mannose receptor 1,Macrophage mannose receptor 1-like protein 96T
E1542h ELISA kit CLEC13D,CLEC13DL,C-type lectin domain family 13 member D,C-type lectin domain family 13 member D-like,Homo sapiens,Human,Macrophage mannose receptor 1,Macrophage mannose receptor 1-like pro 96T
EIAAB25356 C-type mannose receptor 2,Endo180,Endocytic receptor 180,Macrophage mannose receptor 2,Mrc2,Rat,Rattus norvegicus
U1629h CLIA 300 kDa mannose 6-phosphate receptor,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,Homo sapiens,Human,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Insu 96T
E1629b ELISA 300 kDa mannose 6-phosphate receptor,Bos taurus,Bovine,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Insu 96T
E1629h ELISA 300 kDa mannose 6-phosphate receptor,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,Homo sapiens,Human,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Ins 96T
U1629b CLIA 300 kDa mannose 6-phosphate receptor,Bos taurus,Bovine,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor,Insul 96T
E1629b ELISA kit 300 kDa mannose 6-phosphate receptor,Bos taurus,Bovine,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,IGF2R,IGF-II receptor,Insulin-like growth factor 2 receptor 96T
E1629h ELISA kit 300 kDa mannose 6-phosphate receptor,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,Homo sapiens,Human,IGF2R,IGF-II receptor,Insulin-like growth factor 2 recepto 96T
E1629m ELISA kit 300 kDa mannose 6-phosphate receptor,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,Igf2r,IGF-II receptor,Insulin-like growth factor 2 receptor,Insulin-like grow 96T
EIAAB25324 46 kDa mannose 6-phosphate receptor,Cation-dependent mannose-6-phosphate receptor,CD Man-6-P receptor,CD-MPR,Homo sapiens,Human,M6PR,MPR 46,MPR46,MPRD
EIAAB25325 46 kDa mannose 6-phosphate receptor,46mpr,Cation-dependent mannose-6-phosphate receptor,CD Man-6-P receptor,CD-MPR,M6pr,Mouse,MPR 46,Mus musculus
EIAAB25323 46 kDa mannose 6-phosphate receptor,Bos taurus,Bovine,Cation-dependent mannose-6-phosphate receptor,CD Man-6-P receptor,CD-MPR,M6PR,MPR 46
U1629m CLIA 300 kDa mannose 6-phosphate receptor,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,Igf2r,IGF-II receptor,Insulin-like growth factor 2 receptor,Insulin-like growth fac 96T
E1629m ELISA 300 kDa mannose 6-phosphate receptor,Cation-independent mannose-6-phosphate receptor,CI Man-6-P receptor,CI-MPR,Igf2r,IGF-II receptor,Insulin-like growth factor 2 receptor,Insulin-like growth fa 96T
15-288-21589A ERGIC-53 protein - ER-Golgi intermediate compartment 53 kDa protein; Lectin. mannose-binding 1; Gp58; Intracellular mannose-specific lectin MR60 Polyclonal 0.1 mg
15-288-21589A ERGIC-53 protein - ER-Golgi intermediate compartment 53 kDa protein; Lectin. mannose-binding 1; Gp58; Intracellular mannose-specific lectin MR60 Polyclonal 0.05 mg
15-288-21444 Cation-dependent mannose-6-phosphate receptor - CD Man-6-P receptor; CD-MPR; 46 kDa mannose 6-phosphate receptor; MPR 46 Polyclonal 0.1 mg
15-288-21444 Cation-dependent mannose-6-phosphate receptor - CD Man-6-P receptor; CD-MPR; 46 kDa mannose 6-phosphate receptor; MPR 46 Polyclonal 0.05 mg
EIAAB07673 Clec18a,C-type lectin domain family 18 member A,Mannose receptor-like protein,Mouse,Mrcl,Mrlp,Mus musculus
EIAAB07674 CLEC18A,C-type lectin domain family 18 member A,Homo sapiens,Human,Mannose receptor-like protein 2,MRLP2
EIAAB07676 CLEC18C,C-type lectin domain family 18 member C,Homo sapiens,Human,Mannose receptor-like protein 3,MRLP3


 

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