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Scavenger receptor class F member 2 (SRECRP-1) (Scavenger receptor expressed by endothelial cells 2 protein) (SREC-II)

 SREC2_HUMAN             Reviewed;         870 AA.
Q96GP6; E5RFB8; Q58A83; Q8IXF3; Q9BW74;
17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
21-MAR-2012, sequence version 4.
20-JUN-2018, entry version 146.
RecName: Full=Scavenger receptor class F member 2;
AltName: Full=SRECRP-1;
AltName: Full=Scavenger receptor expressed by endothelial cells 2 protein;
Short=SREC-II;
Flags: Precursor;
Name=SCARF2; Synonyms=SREC2, SREPCR;
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 2), AND VARIANTS SER-174; GLU-777
AND LEU-778.
Adachi H., Tsujimoto M.;
"cDNA cloning of SRECRP (scavenger receptor expressed by endothelial
cell related protein).";
Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
TISSUE=Epithelium;
PubMed=12154095; DOI=10.1074/jbc.M206140200;
Ishii J., Adachi H., Aoki J., Koizumi H., Tomita S., Suzuki T.,
Tsujimoto M., Inoue K., Arai H.;
"SREC-II, a new member of the scavenger receptor type F family, trans-
interacts with SREC-I through its extracellular domain.";
J. Biol. Chem. 277:39696-39702(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANTS GLU-777 AND
LEU-778.
TISSUE=Vulva;
Kitaura M., Iwagami S., Tsuruta Y., Suzuki R.;
"A novel human nurse cell receptor NSR1.";
Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANTS GLU-777
AND LEU-778.
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 272-870 (ISOFORM 2), AND
VARIANTS GLU-777 AND LEU-778.
TISSUE=Brain;
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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-651; SER-653 AND
SER-718, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-653 AND
SER-742, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[10]
VARIANT [LARGE SCALE ANALYSIS] CYS-499.
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).
[11]
VARIANT VDEGS TYR-258.
PubMed=20887961; DOI=10.1016/j.ajhg.2010.09.005;
Anastasio N., Ben-Omran T., Teebi A., Ha K.C., Lalonde E., Ali R.,
Almureikhi M., Der Kaloustian V.M., Liu J., Rosenblatt D.S.,
Majewski J., Jerome-Majewska L.A.;
"Mutations in SCARF2 are responsible for Van Den Ende-Gupta
syndrome.";
Am. J. Hum. Genet. 87:553-559(2010).
-!- FUNCTION: Probable adhesion protein, which mediates homophilic and
heterophilic interactions. In contrast to SCARF1, it poorly
mediates the binding and degradation of acetylated low density
lipoprotein (Ac-LDL) (By similarity). {ECO:0000250}.
-!- SUBUNIT: Homophilic and heterophilic interaction via its
extracellular domain. Interacts with SCARF1. The heterophilic
interaction with SCARF1, which is stronger than the homophilic
interaction with itself, is suppressed by the presence of SCARF1
ligand such as Ac-LDL (By similarity). {ECO:0000250}.
-!- INTERACTION:
P16333:NCK1; NbExp=2; IntAct=EBI-1752088, EBI-389883;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q96GP6-1; Sequence=Displayed;
Name=2;
IsoId=Q96GP6-2; Sequence=VSP_042462;
-!- TISSUE SPECIFICITY: Predominantly expressed in endothelial cells.
Expressed in heart, placenta, lung, kidney, spleen, small
intestine and ovary. {ECO:0000269|PubMed:12154095}.
-!- DISEASE: Van den Ende-Gupta syndrome (VDEGS) [MIM:600920]: A
syndrome characterized by craniofacial and skeletal abnormalities
that include blepharophimosis, a flat and wide nasal bridge,
narrow and beaked nose, hypoplastic maxilla with or without cleft
palate and everted lower lip, prominent ears, down-slanting eyes,
arachnodactyly, and camptodactyly. Patients present congenital
joint contractures that improve without intervention, and normal
growth and development. Intelligence is normal. Rarely, enlarged
cerebella can be present. Some patients experience respiratory
problems due to laryngeal abnormalities.
{ECO:0000269|PubMed:20887961}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- CAUTION: The conflict at position 750-768 is due to frameshifts.
The frameshifted sequence is found in mouse. {ECO:0000305}.
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EMBL; AB052951; BAC53753.1; -; mRNA.
EMBL; AF522196; AAN45861.1; -; mRNA.
EMBL; AB024433; BAD93345.1; -; mRNA.
EMBL; AC007731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471176; EAX02965.1; -; Genomic_DNA.
EMBL; BC000584; AAH00584.2; -; mRNA.
EMBL; BC009326; AAH09326.2; -; mRNA.
RefSeq; NP_699165.3; NM_153334.6.
RefSeq; NP_878315.2; NM_182895.4.
UniGene; Hs.474251; -.
ProteinModelPortal; Q96GP6; -.
SMR; Q96GP6; -.
BioGrid; 124803; 6.
IntAct; Q96GP6; 4.
STRING; 9606.ENSP00000266214; -.
iPTMnet; Q96GP6; -.
PhosphoSitePlus; Q96GP6; -.
SwissPalm; Q96GP6; -.
BioMuta; SCARF2; -.
DMDM; 380865486; -.
PaxDb; Q96GP6; -.
PeptideAtlas; Q96GP6; -.
PRIDE; Q96GP6; -.
ProteomicsDB; 76651; -.
ProteomicsDB; 76652; -. [Q96GP6-2]
DNASU; 91179; -.
Ensembl; ENST00000622235; ENSP00000477564; ENSG00000244486.
GeneID; 91179; -.
KEGG; hsa:91179; -.
UCSC; uc062bsr.1; human. [Q96GP6-1]
CTD; 91179; -.
DisGeNET; 91179; -.
EuPathDB; HostDB:ENSG00000244486.7; -.
GeneCards; SCARF2; -.
H-InvDB; HIX0213276; -.
HGNC; HGNC:19869; SCARF2.
HPA; HPA035079; -.
MalaCards; SCARF2; -.
MIM; 600920; phenotype.
MIM; 613619; gene.
neXtProt; NX_Q96GP6; -.
Orphanet; 2460; Van den Ende-Gupta syndrome.
PharmGKB; PA134908523; -.
eggNOG; KOG1218; Eukaryota.
eggNOG; ENOG410XQWV; LUCA.
HOGENOM; HOG000015093; -.
HOVERGEN; HBG023166; -.
InParanoid; Q96GP6; -.
PhylomeDB; Q96GP6; -.
TreeFam; TF332598; -.
ChiTaRS; SCARF2; human.
GenomeRNAi; 91179; -.
PRO; PR:Q96GP6; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000244486; -.
CleanEx; HS_SCARF2; -.
ExpressionAtlas; Q96GP6; baseline and differential.
Genevisible; Q96GP6; HS.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:InterPro.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR002049; Laminin_EGF.
InterPro; IPR033327; Scarf2.
PANTHER; PTHR24043:SF5; PTHR24043:SF5; 1.
SMART; SM00181; EGF; 7.
SMART; SM00180; EGF_Lam; 6.
SUPFAM; SSF57184; SSF57184; 1.
PROSITE; PS00022; EGF_1; 7.
PROSITE; PS01186; EGF_2; 4.
PROSITE; PS50026; EGF_3; 3.
1: Evidence at protein level;
Alternative splicing; Cell adhesion; Complete proteome;
Disease mutation; Disulfide bond; EGF-like domain; Glycoprotein;
Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome;
Repeat; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 43 {ECO:0000255}.
CHAIN 44 870 Scavenger receptor class F member 2.
/FTId=PRO_0000007739.
TOPO_DOM 44 441 Extracellular. {ECO:0000255}.
TRANSMEM 442 462 Helical. {ECO:0000255}.
TOPO_DOM 463 870 Cytoplasmic. {ECO:0000255}.
DOMAIN 71 110 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 122 153 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 148 182 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 183 212 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 213 241 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 236 270 EGF-like 6. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 372 403 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
COMPBIAS 648 847 Pro-rich.
MOD_RES 551 551 Phosphoserine.
{ECO:0000250|UniProtKB:P59222}.
MOD_RES 613 613 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 628 628 Phosphotyrosine.
{ECO:0000250|UniProtKB:P59222}.
MOD_RES 651 651 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 653 653 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 710 710 Phosphoserine.
{ECO:0000250|UniProtKB:P59222}.
MOD_RES 718 718 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 742 742 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 310 310 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 365 365 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 403 403 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 75 86 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 80 98 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 100 109 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 126 134 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 128 141 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 143 152 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 156 163 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 158 170 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 172 181 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 185 193 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 187 200 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 202 211 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 215 222 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 217 229 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 231 240 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 244 251 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 246 258 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 260 269 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 376 384 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 379 391 {ECO:0000255|PROSITE-ProRule:PRU00076}.
DISULFID 393 402 {ECO:0000255|PROSITE-ProRule:PRU00076}.
VAR_SEQ 474 478 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.1, ECO:0000303|Ref.3}.
/FTId=VSP_042462.
VARIANT 174 174 P -> S (in dbSNP:rs361566).
{ECO:0000269|Ref.1}.
/FTId=VAR_059274.
VARIANT 258 258 C -> Y (in VDEGS).
{ECO:0000269|PubMed:20887961}.
/FTId=VAR_065302.
VARIANT 425 425 T -> S (in dbSNP:rs2241230).
/FTId=VAR_055776.
VARIANT 499 499 R -> C (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035837.
VARIANT 522 522 H -> L (in dbSNP:rs12484828).
/FTId=VAR_055777.
VARIANT 777 777 D -> E (in dbSNP:rs759611).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.1, ECO:0000269|Ref.3,
ECO:0000269|Ref.5}.
/FTId=VAR_015148.
VARIANT 778 778 V -> L (in dbSNP:rs759612).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.1, ECO:0000269|Ref.3,
ECO:0000269|Ref.5}.
/FTId=VAR_015149.
VARIANT 819 819 A -> G (in dbSNP:rs874100).
/FTId=VAR_015150.
VARIANT 837 837 A -> G (in dbSNP:rs874101).
/FTId=VAR_015151.
CONFLICT 629 641 ARVARREARPARA -> PTTTWITHSTAAS (in Ref.
6; AAH00584). {ECO:0000305}.
CONFLICT 750 768 AAPRPLGAHGRRRSPAKRA -> GRGPGLLEPTDAGGPPRS
AP (in Ref. 1; BAC53753, 3; BAD93345, 5;
EAX02965 and 6; AAH00584/AAH09326).
{ECO:0000305}.
SEQUENCE 870 AA; 92479 MW; DCB735A50E6E9D1F CRC64;
MEGAGPRGAG PARRRGAGGP PSPLLPSLLL LLLLWMLPDT VAPQELNPRG RNVCRAPGSQ
VPTCCAGWRQ QGDECGIAVC EGNSTCSENE VCVRPGECRC RHGYFGANCD TKCPRQFWGP
DCKELCSCHP HGQCEDVTGQ CTCHARRWGA RCEHACQCQH GTCHPRSGAC RCEPGWWGAQ
CASACYCSAT SRCDPQTGAC LCHAGWWGRS CNNQCACNSS PCEQQSGRCQ CRERTFGARC
DRYCQCFRGR CHPVDGTCAC EPGYRGKYCR EPCPAGFYGL GCRRRCGQCK GQQPCTVAEG
RCLTCEPGWN GTKCDQPCAT GFYGEGCSHR CPPCRDGHAC NHVTGKCTRC NAGWIGDRCE
TKCSNGTYGE DCAFVCADCG SGHCDFQSGR CLCSPGVHGP HCNVTCPPGL HGADCAQACS
CHEDTCDPVT GACHLETNQR KGVMGAGALL VLLVCLLLSL LGCCCACRGK DPTRRPRPRR
ELSLGRKKAP HRLCGRFSRI SMKLPRIPLR RQKLPKVVVA HHDLDNTLNC SFLEPPSGLE
QPSPSWSSRA SFSSFDTTDE GPVYCVPHEE APAESRDPEV PTVPAEAPAP SPVPLTTPAS
AEEAIPLPAS SDSERSASSV EGPGGALYAR VARREARPAR ARGEIGGLSL SPSPERRKPP
PPDPATKPKV SWIHGKHSAA AAGRAPSPPP PGSEAAPSPS KRKRTPSDKS AHTVEHGSPR
TRDPTPRPPG LPEEATALAA PSPPRARARA APRPLGAHGR RRSPAKRAEA ASMLAADVRG
KTRSLGRAEV ALGAQGPREK PAPPQKAKRS VPPASPARAP PATETPGPEK AATDLPAPET
PRKKTPIQKP PRKKSREAAG ELGRAGAPTL


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5193 Scavenger receptor class B member 1 0.5 mg
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EH1791 Scavenger receptor class B member 1 Elisa Kit 96T
C532 Scavenger Receptor Class B Member 2 SCARB2 lmg
C532 Scavenger Receptor Class B Member 2 SCARB2 500
E1726h ELISA CD163,Hemoglobin scavenger receptor,Homo sapiens,Human,M130,Scavenger receptor cysteine-rich type 1 protein M130 96T
E1726h ELISA kit CD163,Hemoglobin scavenger receptor,Homo sapiens,Human,M130,Scavenger receptor cysteine-rich type 1 protein M130 96T
U1726h CLIA CD163,Hemoglobin scavenger receptor,Homo sapiens,Human,M130,Scavenger receptor cysteine-rich type 1 protein M130 96T
E9132h Human Scavenger Receptor Class D Member 1 ELISA Ki 96T
E0280m Mouse ELISA Kit FOR Scavenger receptor class F member 1 96T
E8684h Human Scavenger Receptor Class F Member 2 ELISA Ki 96T
201-20-5117 SCARF1{scavenger receptor class F, member 1}rabbit.pAb 0.2ml
G8985 Scavenger receptor class B member 1 (SCARB1), Rat, ELISA Kit 96T


 

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