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Stabilin-2 (Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 2) (FEEL-2) [Cleaved into: Short form stabilin-2]

 STAB2_MOUSE             Reviewed;        2559 AA.
Q8R4U0; Q8BM87;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2002, sequence version 1.
30-AUG-2017, entry version 132.
RecName: Full=Stabilin-2;
AltName: Full=Fasciclin, EGF-like, laminin-type EGF-like and link domain-containing scavenger receptor 2;
Short=FEEL-2;
Contains:
RecName: Full=Short form stabilin-2;
Flags: Precursor;
Name=Stab2 {ECO:0000312|MGI:MGI:2178743}; Synonyms=Feel2, Hare;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1] {ECO:0000312|EMBL:AAL91684.2}
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=BALB/cJ {ECO:0000312|EMBL:AAL91684.2};
TISSUE=Liver {ECO:0000312|EMBL:AAL91684.2};
PubMed=11829752; DOI=10.1042/0264-6021:3620155;
Politz O., Gratchev A., McCourt P.A.G., Schledzewski K., Guillot P.,
Johansson S., Svineng G., Franke P., Kannicht C., Kzhyshkowska J.,
Longati P., Velten F.W., Johansson S., Goerdt S.;
"Stabilin-1 and -2 constitute a novel family of fasciclin-like
hyaluronan receptor homologues.";
Biochem. J. 362:155-164(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1666-2559.
STRAIN=C57BL/6J; TISSUE=Diencephalon;
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]
TISSUE SPECIFICITY.
PubMed=12473645; DOI=10.1074/jbc.M210211200;
Tamura Y., Adachi H., Osuga J., Ohashi K., Yahagi N., Sekiya M.,
Okazaki H., Tomita S., Iizuka Y., Shimano H., Nagai R., Kimura S.,
Tsujimoto M., Ishibashi S.;
"FEEL-1 and FEEL-2 are endocytic receptors for advanced glycation end
products.";
J. Biol. Chem. 278:12613-12617(2003).
[4]
TISSUE SPECIFICITY.
PubMed=14598175; DOI=10.1007/s00418-003-0585-5;
Falkowski M., Schledzewski K., Hansen B., Goerdt S.;
"Expression of stabilin-2, a novel fasciclin-like hyaluronan receptor
protein, in murine sinusoidal endothelia, avascular tissues, and at
solid/liquid interfaces.";
Histochem. Cell Biol. 120:361-369(2003).
[5]
FUNCTION, INTERACTION WITH CLATHRIN AND AP2, AND SUBCELLULAR LOCATION.
PubMed=15572036; DOI=10.1016/j.yexcr.2004.09.017;
Hansen B., Longati P., Elvevold K., Nedredal G.-I., Schledzewski K.,
Olsen R., Falkowski M., Kzhyshkowska J., Carlsson F., Johansson S.,
Smedsroed B., Goerdt S., Johansson S., McCourt P.;
"Stabilin-1 and stabilin-2 are both directed into the early endocytic
pathway in hepatic sinusoidal endothelium via interactions with
clathrin/AP-2, independent of ligand binding.";
Exp. Cell Res. 303:160-173(2005).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2503, AND 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]
FUNCTION, AND INTERACTION WITH GULP1.
PubMed=18230608; DOI=10.1074/jbc.M709105200;
Park S.Y., Kang K.B., Thapa N., Kim S.Y., Lee S.J., Kim I.S.;
"Requirement of adaptor protein GULP during stabilin-2-mediated cell
corpse engulfment.";
J. Biol. Chem. 283:10593-10600(2008).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2503, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver, 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: Phosphatidylserine receptor that enhances the engulfment
of apoptotic cells. Hyaluronan receptor that binds to and mediates
endocytosis of hyaluronic acid (HA). Acts also, in different
species, as a primary systemic scavenger receptor for heparin
(Hep), chondroitin sulfate (CS), dermatan sulfate (DS),
nonglycosaminoglycan (GAG), acetylated low-density lipoprotein
(AcLDL), pro-collagen propeptides and advanced glycation end
products (AGE). May serve to maintain tissue integrity by
supporting extracellular matrix turnover or it may contribute to
maintaining fluidity of bodily liquids by resorption of
hyaluronan. Counter receptor which plays an important role in
lymphocyte recruitment in the hepatic vasculature. Binds to both
Gram-positive and Gram-negative bacteria and may play a role in
defense against bacterial infection. The proteolytically processed
short form also functions as an endocytosis receptor for heparin
internalisation as well as HA and CS.
{ECO:0000269|PubMed:15572036, ECO:0000269|PubMed:18230608}.
-!- SUBUNIT: Interacts with heparin, alpha-M/beta-2 integrin (ITGAM
and ITGB2), and thymosin beta 4 (TMSB4X) (By similarity).
Interacts with GULP1. Associates with clathrin and adapter protein
AP-2; in liver sinusoidal endothelial cells (LSECs). {ECO:0000250,
ECO:0000269|PubMed:15572036, ECO:0000269|PubMed:18230608}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q8WWQ8}.
Cell membrane {ECO:0000269|PubMed:15572036}; Single-pass type I
membrane protein {ECO:0000269|PubMed:15572036}.
-!- TISSUE SPECIFICITY: Expressed in endothelial sinuses of liver,
lymph nodes, bone marrow, spleen and in specialised structures of
eye, heart, brain and kidney. Expression is detected in corneal
and lens epithelium, in mesenchymal cells of the heart valves, in
the ependymal cells lining the ventricles in the brain, and in the
prismatic epithelial cells covering the renal papillae.
{ECO:0000269|PubMed:12473645, ECO:0000269|PubMed:14598175}.
-!- DOMAIN: Recognizes phosphatidyl serine via its epidermal growth
factor-like domains.
-!- PTM: Glycosylated. {ECO:0000250}.
-!- PTM: Proteolytically processed to yield a smaller protein.
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EMBL; AF364951; AAL91684.2; -; mRNA.
EMBL; AK034522; BAC28741.1; -; mRNA.
CCDS; CCDS36021.1; -.
RefSeq; NP_619614.1; NM_138673.2.
UniGene; Mm.279611; -.
ProteinModelPortal; Q8R4U0; -.
SMR; Q8R4U0; -.
STRING; 10090.ENSMUSP00000048309; -.
iPTMnet; Q8R4U0; -.
PhosphoSitePlus; Q8R4U0; -.
SwissPalm; Q8R4U0; -.
MaxQB; Q8R4U0; -.
PaxDb; Q8R4U0; -.
PRIDE; Q8R4U0; -.
Ensembl; ENSMUST00000035288; ENSMUSP00000048309; ENSMUSG00000035459.
GeneID; 192188; -.
KEGG; mmu:192188; -.
UCSC; uc007gqo.1; mouse.
CTD; 55576; -.
MGI; MGI:2178743; Stab2.
eggNOG; ENOG410IRWM; Eukaryota.
eggNOG; ENOG4110T5S; LUCA.
GeneTree; ENSGT00890000139439; -.
HOGENOM; HOG000154436; -.
HOVERGEN; HBG079218; -.
InParanoid; Q8R4U0; -.
KO; K19013; -.
OMA; CLYVGPG; -.
OrthoDB; EOG091G002T; -.
PhylomeDB; Q8R4U0; -.
TreeFam; TF331489; -.
Reactome; R-MMU-2160916; Hyaluronan uptake and degradation.
Reactome; R-MMU-3000497; Scavenging by Class H Receptors.
PRO; PR:Q8R4U0; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000035459; -.
CleanEx; MM_STAB2; -.
ExpressionAtlas; Q8R4U0; baseline and differential.
Genevisible; Q8R4U0; MM.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0009897; C:external side of plasma membrane; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISO:MGI.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005540; F:hyaluronic acid binding; ISS:UniProtKB.
GO; GO:0030169; F:low-density lipoprotein particle binding; ISO:MGI.
GO; GO:0005041; F:low-density lipoprotein receptor activity; ISO:MGI.
GO; GO:0005044; F:scavenger receptor activity; ISO:MGI.
GO; GO:0007155; P:cell adhesion; IEA:InterPro.
GO; GO:0042742; P:defense response to bacterium; ISO:MGI.
GO; GO:0006897; P:endocytosis; ISS:UniProtKB.
GO; GO:0030193; P:regulation of blood coagulation; ISO:MGI.
GO; GO:0010468; P:regulation of gene expression; ISO:MGI.
Gene3D; 2.30.180.10; -; 7.
Gene3D; 3.10.100.10; -; 1.
InterPro; IPR016186; C-type_lectin-like/link.
InterPro; IPR016187; CTDL_fold.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR024731; EGF_dom.
InterPro; IPR000782; FAS1_domain.
InterPro; IPR002049; Laminin_EGF.
InterPro; IPR000538; Link_dom.
Pfam; PF12947; EGF_3; 5.
Pfam; PF02469; Fasciclin; 7.
Pfam; PF00193; Xlink; 1.
SMART; SM00181; EGF; 21.
SMART; SM00179; EGF_CA; 7.
SMART; SM00180; EGF_Lam; 5.
SMART; SM00554; FAS1; 7.
SMART; SM00445; LINK; 1.
SUPFAM; SSF56436; SSF56436; 1.
SUPFAM; SSF82153; SSF82153; 7.
PROSITE; PS00022; EGF_1; 7.
PROSITE; PS01186; EGF_2; 16.
PROSITE; PS50026; EGF_3; 21.
PROSITE; PS01248; EGF_LAM_1; 2.
PROSITE; PS50213; FAS1; 7.
PROSITE; PS01241; LINK_1; 1.
PROSITE; PS50963; LINK_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasm; Disulfide bond;
EGF-like domain; Endocytosis; Glycoprotein; Hyaluronic acid;
Laminin EGF-like domain; Membrane; Phosphoprotein; Receptor;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 2559 Stabilin-2.
/FTId=PRO_0000007714.
CHAIN 1136 2551 Short form stabilin-2. {ECO:0000250}.
/FTId=PRO_0000007715.
TOPO_DOM 29 2464 Extracellular. {ECO:0000255}.
TRANSMEM 2465 2485 Helical. {ECO:0000255}.
TOPO_DOM 2486 2559 Cytoplasmic. {ECO:0000255}.
DOMAIN 116 156 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 164 201 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 203 244 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 245 284 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 330 370 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 379 512 FAS1 1. {ECO:0000255|PROSITE-
ProRule:PRU00082}.
DOMAIN 522 659 FAS1 2. {ECO:0000255|PROSITE-
ProRule:PRU00082}.
DOMAIN 743 783 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 833 873 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 874 917 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 918 960 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 961 1002 EGF-like 10. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1002 1135 FAS1 3. {ECO:0000255|PROSITE-
ProRule:PRU00082}.
DOMAIN 1145 1273 FAS1 4. {ECO:0000255|PROSITE-
ProRule:PRU00082}.
DOMAIN 1350 1415 Laminin EGF-like 1. {ECO:0000255}.
DOMAIN 1439 1477 EGF-like 11. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1478 1519 EGF-like 12. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1520 1561 EGF-like 13. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1562 1603 EGF-like 14. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1603 1731 FAS1 5. {ECO:0000255|PROSITE-
ProRule:PRU00082}.
DOMAIN 1747 1888 FAS1 6. {ECO:0000255|PROSITE-
ProRule:PRU00082}.
DOMAIN 1965 2030 Laminin EGF-like 2. {ECO:0000255}.
DOMAIN 2055 2089 EGF-like 15. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 2090 2130 EGF-like 16. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 2131 2173 EGF-like 17. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 2206 2298 Link. {ECO:0000255|PROSITE-
ProRule:PRU00323}.
DOMAIN 2318 2452 FAS1 7. {ECO:0000255|PROSITE-
ProRule:PRU00082}.
REGION 2510 2520 Interaction with TMSB4X. {ECO:0000250}.
MOD_RES 2503 2503 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
CARBOHYD 71 71 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 167 167 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 345 345 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 572 572 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 626 626 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 673 673 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 691 691 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 768 768 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 796 796 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 854 854 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 933 933 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1024 1024 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1036 1036 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1108 1108 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1255 1255 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1283 1283 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1374 1374 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1386 1386 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1444 1444 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1472 1472 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1580 1580 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1750 1750 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2001 2001 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2072 2072 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2287 2287 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2303 2303 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2375 2375 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2391 2391 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2400 2400 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 120 134 {ECO:0000250}.
DISULFID 128 144 {ECO:0000250}.
DISULFID 146 155 {ECO:0000250}.
DISULFID 168 179 {ECO:0000250}.
DISULFID 172 189 {ECO:0000250}.
DISULFID 191 200 {ECO:0000250}.
DISULFID 207 218 {ECO:0000250}.
DISULFID 212 230 {ECO:0000250}.
DISULFID 232 243 {ECO:0000250}.
DISULFID 249 260 {ECO:0000250}.
DISULFID 254 270 {ECO:0000250}.
DISULFID 272 283 {ECO:0000250}.
DISULFID 334 346 {ECO:0000250}.
DISULFID 340 356 {ECO:0000250}.
DISULFID 358 369 {ECO:0000250}.
DISULFID 747 761 {ECO:0000250}.
DISULFID 755 771 {ECO:0000250}.
DISULFID 773 782 {ECO:0000250}.
DISULFID 837 850 {ECO:0000250}.
DISULFID 844 859 {ECO:0000250}.
DISULFID 861 872 {ECO:0000250}.
DISULFID 878 893 {ECO:0000250}.
DISULFID 887 903 {ECO:0000250}.
DISULFID 905 916 {ECO:0000250}.
DISULFID 922 936 {ECO:0000250}.
DISULFID 930 946 {ECO:0000250}.
DISULFID 948 959 {ECO:0000250}.
DISULFID 965 978 {ECO:0000250}.
DISULFID 972 988 {ECO:0000250}.
DISULFID 990 1001 {ECO:0000250}.
DISULFID 1355 1369 {ECO:0000250}.
DISULFID 1363 1379 {ECO:0000250}.
DISULFID 1381 1390 {ECO:0000250}.
DISULFID 1402 1413 {ECO:0000250}.
DISULFID 1406 1423 {ECO:0000250}.
DISULFID 1425 1434 {ECO:0000250}.
DISULFID 1443 1453 {ECO:0000250}.
DISULFID 1447 1463 {ECO:0000250}.
DISULFID 1465 1476 {ECO:0000250}.
DISULFID 1482 1495 {ECO:0000250}.
DISULFID 1489 1505 {ECO:0000250}.
DISULFID 1507 1518 {ECO:0000250}.
DISULFID 1524 1537 {ECO:0000250}.
DISULFID 1531 1547 {ECO:0000250}.
DISULFID 1549 1560 {ECO:0000250}.
DISULFID 1566 1579 {ECO:0000250}.
DISULFID 1573 1589 {ECO:0000250}.
DISULFID 1591 1602 {ECO:0000250}.
DISULFID 1970 1984 {ECO:0000250}.
DISULFID 1978 1994 {ECO:0000250}.
DISULFID 1996 2005 {ECO:0000250}.
DISULFID 2017 2028 {ECO:0000250}.
DISULFID 2022 2038 {ECO:0000250}.
DISULFID 2040 2049 {ECO:0000250}.
DISULFID 2059 2069 {ECO:0000250}.
DISULFID 2063 2075 {ECO:0000250}.
DISULFID 2077 2088 {ECO:0000250}.
DISULFID 2094 2107 {ECO:0000250}.
DISULFID 2101 2116 {ECO:0000250}.
DISULFID 2118 2129 {ECO:0000250}.
DISULFID 2135 2149 {ECO:0000250}.
DISULFID 2143 2159 {ECO:0000250}.
DISULFID 2161 2172 {ECO:0000250}.
DISULFID 2228 2296 {ECO:0000250}.
DISULFID 2252 2273 {ECO:0000250}.
CONFLICT 1666 1666 L -> G (in Ref. 2; BAC28741).
{ECO:0000305}.
SEQUENCE 2559 AA; 277532 MW; 1C9855AD61EFF015 CRC64;
MARSKLLLGK LLPLILIFLG LLVQNACSPT EAPELTKRCD KKSTLTIKTE CQSCSVNIAV
KCPDGYIKIT NGTVGVRDCR YSLKIQSYVL DIPGCRHICR KDYLQPQCCP GHWGPDCMEC
PGGARAPCGG RGVCDEGMEG TGSCSCRAGF RGTACENCAA EDVFGPNCSA VCSCVHGVCN
SGISGDGTCE CLSAYRGPRC DKPIPECAAL LCPENSRCSP SSKDETKLQC KCLPSYKGDG
QTCKPINPCL KNVCHPHASC SYLGPNRHSC VCQKGYQGDG QVCLPVDPCQ TSYGNCPTKS
TVCRYDGPGQ SHCECKEHYR NFVPGVGCSM TDICESKNPC HKNANCSTVS PGQTQCTCQK
GYVGDGLNCY GNIMQRLREL NTEPRGMWQG QLTSFISILD RTYAWPLSNL GPFTVLLPSD
KGLKGVDVKE LLMDKEAARY FVKLHIIAGQ MSTEQMYNLD TFYTLTGKSG EIINKDKDNQ
LKLKLYGSKI VQIIQGNIVA SNGLVHILDR AMDKIEPTLE SNPQQTIMTM LQPRYGKFRS
LLEKTNVGQA LEKGGIDEPY TIFVPSNEAL SNMTAGVLDY LLSPEGSRKL LELVRYHIVA
FTQLEVATLV STLHIRSMAN QIITFNISSK GQILANNVAV DETEVAAKNG RIYTLTGVLI
PPSILPILPH RCNETKREMK LGTCVRCFMK NWSKCPTNSE PTAIFTNKCF YGSRAWNLKI
GCARYCDVTV EIPRCCKGFF GPDCNPCPGG FMNPCSGNGQ CIDGLGGNGT CICEDGFQGS
RCQFCSKPNR YGPQCNRTCQ CVHGICDNRL DSDGSCLPGT CREGTAGRFC DKQTSACGPY
MQFCHIHATC EYSNETASCV CNDGYEGDGT LCSKKDPCLG STSRGGCSPN AECIQASTGT
YSCVCQRGWT GNGRDCVEIN SCLLPSSGGC HDNATCLYVG PGQNECECKK GFRGNGIDCE
PIISCLEQIE KCHPLATCQY TLSGVWSCVC QEGYEGNGVL CYGNVLMELS FLSEAAVFYQ
WINNASLQSM LSATSNLTVL VPSLQAIKDM DQNEKSFWLS RNNIPALIKY HTLLGTYRVA
DLQTLPSSHM LATSLQGSFL RLDKADGNIT IEGASFVDGD NAATNGVVHI INKVLIPQRG
LTGSLPSLLT RLEQMPDYSI FRGYIIHYNL ASAIEAADAY TVFVPNNEAI ESYIREKKAT
SLKEDILQYH VVLGEKLLRN DLHNGMHRET MLGFSYLLAF FLHNDQLYVN EAPINYTNVA
TDKGVIHGLE KVLEIKKNRC DNNDTIIVRG KCGKCSQQTL CPLETKPLSE TRKCIYSVYF
MGKRSIFIGC QLQCVRTIIT SACCAGFFGP QCQACPGKGQ NVCSGNGFCL DGVNGTGTCE
CEQGFNGTAC ETCTEGKYGI HCDQACSCVH GRCNQGPSGD GSCDCDVGWR GVKCDSEITT
DNCNGTCHTS ANCLLDPDGK ASCKCAAGFQ GNGTVCTAIN ACEISNGGCS AKADCKRTIP
GSRVCVCKAG YTGDGIVCLE INPCLENHGG CDRHAECTQT GPNQAVCNCL PKYTGDGKVC
TLINVCLTNN GGCSPFAFCN HTEQDQRTCT CKPDYTGDGI VCRGSIHSEL PKNPSTSQYF
FQLQEHAVQE LAGPGPFTVF VPSSDSFNSE SKLKVWDKQG LMSQILRYHV VACQQLLLEN
LKVITSATTL QGEPISISVS QDTVLINKKA KVLSSDIIST NGVIHVIDTL LSPQNLLITP
KGASGRVLLN LTTVAANHGY TKFSKLIQDS GLLKVITDPM HTPVTLFWPT DKALQALPQE
QQDFLFNEDN KDKLKAYLKF HVIRDTMALA SDLPRSASWK TLQGSELSVR CGTGSDVGEL
FLNGQMCRII QRRLLFDGGV AYGIDCLLMD PTEGGRCDTF TTFNIPGECG SCFSTPRCPL
QSKPKGVRKK CIYNPLPFRR DVEGCQNLCT LVVHVPRCCS GYFMPDCQAC PGGPDTPCNN
RGMCYDQYKP TGQCQCHTGF NGTACELCLP GRFGPDCQPC GCSEHGQCDE GITGSGQCLC
EAGWTGRFCD APTVVIPVCI PACSMHATCM ENNTCVCNLN YEGDGITCTV VDFCKQNNGG
CAKVAKCSQK GTQVSCSCQK GYKGDGHSCT EIDPCANGVN GGCHEHATCR MTGPGKQKCE
CKSHYVGDGR DCEPEQLPLD RCLQDNGQCH PDANCVDLHF QDTTVGVFHL RSPLGQYKLT
FDKAKEACAK EAASIATYNQ LSYAQKAKYH LCSAGWLESG RVAYPTIYAS KKCANIVGIV
DYGTRTNKSE MWDVFCYRMK DVNCTCKAGY VGDGFSCNGN LLQVLMSFPS LTNFLTEVLV
FSRSSAQGRA FLKHLTDLSI SGTLFVPQNS GLPKNKSLSG RDIEHHLTNV NVSFYDDLVN
GTVLKTRLGS QLLITSSQDQ LHQEARFVDG RAILQWDIIA SNGVLHIISE PLKAPPTAAT
AAHSGLGTGI FCAVVLVTGA IALAAYSYFR LNQRTTGFRR FESEDDIDAL AFGKQQPESI
TNPLYETSTP AAPEPSCDPF TDSGERELEN SDPLGALRS


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