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Low-density lipoprotein receptor-related protein 2 (LRP-2) (Glycoprotein 330) (gp330) (Megalin)

 LRP2_RAT                Reviewed;        4660 AA.
P98158;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
27-SEP-2017, entry version 151.
RecName: Full=Low-density lipoprotein receptor-related protein 2;
Short=LRP-2;
AltName: Full=Glycoprotein 330;
Short=gp330;
AltName: Full=Megalin;
Flags: Precursor;
Name=Lrp2;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Kidney;
PubMed=7937880; DOI=10.1073/pnas.91.21.9725;
Saito A., Pietromonaco S., Loo A.K.C., Farquhar M.G.;
"Complete cloning and sequencing of rat gp330/'megalin,' a distinctive
member of the low density lipoprotein receptor gene family.";
Proc. Natl. Acad. Sci. U.S.A. 91:9725-9729(1994).
[2]
INTERACTION WITH LRPAP1.
PubMed=1400426;
Kounnas M.Z., Argraves W.S., Strickland D.K.;
"The 39-kDa receptor-associated protein interacts with two members of
the low density lipoprotein receptor family, alpha 2-macroglobulin
receptor and glycoprotein 330.";
J. Biol. Chem. 267:21162-21166(1992).
[3]
FUNCTION IN UPTAKE OF POLYBASIC DRUGS.
PubMed=7544804; DOI=10.1172/JCI118176;
Moestrup S.K., Cui S., Vorum H., Bregengaard C., Bjorn S.E.,
Norris K., Gliemann J., Christensen E.I.;
"Evidence that epithelial glycoprotein 330/megalin mediates uptake of
polybasic drugs.";
J. Clin. Invest. 96:1404-1413(1995).
[4]
TISSUE SPECIFICITY.
PubMed=7510321; DOI=10.1177/42.4.7510321;
Zheng G., Bachinsky D.R., Stamenkovic I., Strickland D.K., Brown D.,
Andres G., McCluskey R.T.;
"Organ distribution in rats of two members of the low-density
lipoprotein receptor gene family, gp330 and LRP/alpa 2MR, and the
receptor-associated protein (RAP).";
J. Histochem. Cytochem. 42:531-542(1994).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4464; SER-4577; SER-4624
AND SER-4658, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
[6]
STRUCTURE BY NMR OF 1185-1229, CALCIUM-BINDING SITE, AND DISULFIDE
BONDS.
PubMed=17245526; DOI=10.1007/s10858-006-9129-3;
Wolf C.A., Dancea F., Shi M., Bade-Noskova V., Ruterjans H.,
Kerjaschki D., Lucke C.;
"Solution structure of the twelfth cysteine-rich ligand-binding repeat
in rat megalin.";
J. Biomol. NMR 37:321-328(2007).
[7]
X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 4455-4465 IN COMPLEX WITH
ANKRA2, INTERACTION WITH ANKRA2, AND MOTIF.
PubMed=22649097; DOI=10.1126/scisignal.2002979;
Xu C., Jin J., Bian C., Lam R., Tian R., Weist R., You L., Nie J.,
Bochkarev A., Tempel W., Tan C.S., Wasney G.A., Vedadi M., Gish G.D.,
Arrowsmith C.H., Pawson T., Yang X.J., Min J.;
"Sequence-specific recognition of a PxLPxI/L motif by an ankyrin
repeat tumbler lock.";
Sci. Signal. 5:RA39-RA39(2012).
-!- FUNCTION: Multiligand endocytic receptor. Acts together with
cubilin to mediate HDL endocytosis. In the kidney, mediates the
tubular uptake and clearance of leptin (By similarity). Mediates
receptor-mediated uptake of polybasic drugs such as aprotinin,
aminoglycosides and polymyxin B (PubMed:7544804).
{ECO:0000250|UniProtKB:A2ARV4, ECO:0000269|PubMed:7544804}.
-!- SUBUNIT: Binds plasminogen, extracellular matrix components,
plasminogen activator-plasminogen activator inhibitor type I
complex, apolipoprotein E-enriched beta-VLDL, lipoprotein lipase,
lactoferrin, CLU/clusterin and calcium. Forms a multimeric complex
together with LRPAP1 (PubMed:1400426). Interacts (via PxLPxI/L
motif) with ANKRA2 (via ankyrin repeats) (PubMed:22649097).
Interacts with LRP2BP. Interacts (via NPXY motif) with DAB2; the
interaction is not affected by tyrosine phosphorylation of the
NPXY motif (By similarity). {ECO:0000250|UniProtKB:P98164,
ECO:0000269|PubMed:1400426, ECO:0000269|PubMed:22649097}.
-!- INTERACTION:
O88797:Dab2; NbExp=2; IntAct=EBI-6306650, EBI-6109302;
D3ZAR1:Ldlrap1; NbExp=3; IntAct=EBI-9251342, EBI-9250714;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Membrane, clathrin-coated pit. Cytoplasm. Note=Expressed
in clathrin-coated pits, a soluble form is possibly derived by
cleavage at the cell surface.
-!- TISSUE SPECIFICITY: Epithelial cells of kidney glomerulus and
proximal tubule, lung, epididymis, yolk sac, among others.
{ECO:0000269|PubMed:7510321}.
-!- DOMAIN: Two overlapping PxLPxI/L motifs mediate interaction with
ankyrin repeats of ANKRA2. {ECO:0000269|PubMed:22649097}.
-!- SIMILARITY: Belongs to the LDLR family. {ECO:0000305}.
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EMBL; L34049; AAA51369.1; -; mRNA.
PIR; T42737; T42737.
RefSeq; NP_110454.1; NM_030827.1.
UniGene; Rn.26430; -.
PDB; 2I1P; NMR; -; A=1185-1229.
PDB; 3V2O; X-ray; 1.89 A; B=4448-4466.
PDB; 3V2X; X-ray; 1.85 A; B=4455-4465.
PDBsum; 2I1P; -.
PDBsum; 3V2O; -.
PDBsum; 3V2X; -.
ProteinModelPortal; P98158; -.
SMR; P98158; -.
BioGrid; 247894; 2.
CORUM; P98158; -.
DIP; DIP-44866N; -.
IntAct; P98158; 4.
MINT; MINT-1541513; -.
STRING; 10116.ENSRNOP00000066394; -.
iPTMnet; P98158; -.
PhosphoSitePlus; P98158; -.
UniCarbKB; P98158; -.
PaxDb; P98158; -.
PRIDE; P98158; -.
GeneID; 29216; -.
KEGG; rno:29216; -.
UCSC; RGD:68407; rat.
CTD; 4036; -.
RGD; 68407; Lrp2.
eggNOG; KOG1215; Eukaryota.
eggNOG; ENOG410XP34; LUCA.
HOGENOM; HOG000231853; -.
HOVERGEN; HBG097941; -.
InParanoid; P98158; -.
KO; K06233; -.
PhylomeDB; P98158; -.
EvolutionaryTrace; P98158; -.
PRO; PR:P98158; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0016324; C:apical plasma membrane; IDA:RGD.
GO; GO:0005903; C:brush border; IDA:RGD.
GO; GO:0031526; C:brush border membrane; IDA:RGD.
GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005768; C:endosome; IDA:RGD.
GO; GO:0005615; C:extracellular space; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0043234; C:protein complex; IDA:RGD.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0030492; F:hemoglobin binding; IDA:RGD.
GO; GO:0042562; F:hormone binding; IPI:RGD.
GO; GO:0050750; F:low-density lipoprotein particle receptor binding; IPI:RGD.
GO; GO:0030165; F:PDZ domain binding; IPI:RGD.
GO; GO:0032403; F:protein complex binding; IPI:RGD.
GO; GO:0004872; F:receptor activity; IMP:RGD.
GO; GO:0017124; F:SH3 domain binding; IEA:UniProtKB-KW.
GO; GO:0007568; P:aging; IEP:RGD.
GO; GO:0031100; P:animal organ regeneration; IEP:RGD.
GO; GO:0016197; P:endosomal transport; IMP:RGD.
GO; GO:0020028; P:hemoglobin import; IMP:RGD.
GO; GO:0046879; P:hormone secretion; IMP:RGD.
GO; GO:0042953; P:lipoprotein transport; IMP:RGD.
GO; GO:0010951; P:negative regulation of endopeptidase activity; IC:BHF-UCL.
GO; GO:0006898; P:receptor-mediated endocytosis; IDA:RGD.
GO; GO:0042493; P:response to drug; IEP:RGD.
GO; GO:0032526; P:response to retinoic acid; IEP:RGD.
GO; GO:0033280; P:response to vitamin D; IEP:RGD.
GO; GO:0010165; P:response to X-ray; IDA:RGD.
GO; GO:0045056; P:transcytosis; IMP:RGD.
GO; GO:0006766; P:vitamin metabolic process; TAS:RGD.
Gene3D; 2.120.10.30; -; 8.
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; IPR009030; Growth_fac_rcpt_.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR000033; LDLR_classB_rpt.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
Pfam; PF12662; cEGF; 2.
Pfam; PF07645; EGF_CA; 1.
Pfam; PF00057; Ldl_recept_a; 35.
Pfam; PF00058; Ldl_recept_b; 14.
PRINTS; PR00261; LDLRECEPTOR.
SMART; SM00181; EGF; 22.
SMART; SM00179; EGF_CA; 9.
SMART; SM00192; LDLa; 36.
SMART; SM00135; LY; 36.
SUPFAM; SSF57184; SSF57184; 5.
SUPFAM; SSF57424; SSF57424; 35.
PROSITE; PS00010; ASX_HYDROXYL; 4.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 8.
PROSITE; PS50026; EGF_3; 8.
PROSITE; PS01187; EGF_CA; 3.
PROSITE; PS01209; LDLRA_1; 31.
PROSITE; PS50068; LDLRA_2; 36.
PROSITE; PS51120; LDLRB; 35.
1: Evidence at protein level;
3D-structure; Calcium; Cell membrane; Coated pit; Complete proteome;
Cytoplasm; Disulfide bond; EGF-like domain; Endocytosis; Glycoprotein;
Membrane; Metal-binding; Phosphoprotein; Receptor; Reference proteome;
Repeat; SH3-binding; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 25 {ECO:0000255}.
CHAIN 26 4660 Low-density lipoprotein receptor-related
protein 2.
/FTId=PRO_0000017322.
TOPO_DOM 26 4425 Extracellular. {ECO:0000255}.
TRANSMEM 4426 4446 Helical. {ECO:0000255}.
TOPO_DOM 4447 4660 Cytoplasmic. {ECO:0000255}.
DOMAIN 26 64 LDL-receptor class A 1.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 65 105 LDL-receptor class A 2.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 106 144 LDL-receptor class A 3.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 145 181 LDL-receptor class A 4.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 181 219 LDL-receptor class A 5.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 220 258 LDL-receptor class A 6.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 263 307 LDL-receptor class A 7.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 308 346 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 347 385 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 435 477 LDL-receptor class B 1.
REPEAT 478 520 LDL-receptor class B 2.
REPEAT 521 567 LDL-receptor class B 3.
REPEAT 568 611 LDL-receptor class B 4.
REPEAT 612 652 LDL-receptor class B 5.
DOMAIN 658 704 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 752 794 LDL-receptor class B 6.
REPEAT 795 836 LDL-receptor class B 7.
REPEAT 837 880 LDL-receptor class B 8.
REPEAT 881 924 LDL-receptor class B 9.
DOMAIN 969 1013 EGF-like 4. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1023 1061 LDL-receptor class A 8.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1064 1103 LDL-receptor class A 9.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1108 1146 LDL-receptor class A 10.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1148 1186 LDL-receptor class A 11.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1186 1225 LDL-receptor class A 12.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1229 1269 LDL-receptor class A 13.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1270 1308 LDL-receptor class A 14.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1311 1351 LDL-receptor class A 15.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 1350 1390 EGF-like 5. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 1391 1430 EGF-like 6; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 1479 1521 LDL-receptor class B 10.
REPEAT 1522 1564 LDL-receptor class B 11.
REPEAT 1567 1610 LDL-receptor class B 12.
REPEAT 1611 1654 LDL-receptor class B 13.
REPEAT 1655 1696 LDL-receptor class B 14.
DOMAIN 1701 1742 EGF-like 7. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 1791 1833 LDL-receptor class B 15.
REPEAT 1834 1883 LDL-receptor class B 16.
REPEAT 1884 1931 LDL-receptor class B 17.
REPEAT 1932 1972 LDL-receptor class B 18.
REPEAT 1973 2014 LDL-receptor class B 19.
DOMAIN 2019 2060 EGF-like 8. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 2108 2157 LDL-receptor class B 20.
REPEAT 2158 2202 LDL-receptor class B 21.
REPEAT 2203 2246 LDL-receptor class B 22.
REPEAT 2247 2290 LDL-receptor class B 23.
REPEAT 2291 2332 LDL-receptor class B 24.
DOMAIN 2343 2384 EGF-like 9. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REPEAT 2433 2478 LDL-receptor class B 25.
REPEAT 2479 2519 LDL-receptor class B 26.
REPEAT 2520 2563 LDL-receptor class B 27.
REPEAT 2564 2604 LDL-receptor class B 28.
REPEAT 2605 2647 LDL-receptor class B 29.
DOMAIN 2652 2694 EGF-like 10. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 2699 2739 LDL-receptor class A 16.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2740 2778 LDL-receptor class A 17.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2779 2820 LDL-receptor class A 18.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2821 2862 LDL-receptor class A 19.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2863 2903 LDL-receptor class A 20.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2906 2947 LDL-receptor class A 21.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2948 2992 LDL-receptor class A 22.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 2993 3031 LDL-receptor class A 23.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3032 3072 LDL-receptor class A 24.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3075 3112 LDL-receptor class A 25.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3113 3153 EGF-like 11. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3154 3194 EGF-like 12; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 3241 3283 LDL-receptor class B 30.
REPEAT 3284 3326 LDL-receptor class B 31.
REPEAT 3335 3378 LDL-receptor class B 32.
REPEAT 3379 3420 LDL-receptor class B 33.
REPEAT 3421 3462 LDL-receptor class B 34.
DOMAIN 3467 3511 EGF-like 13. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 3512 3552 LDL-receptor class A 26.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3553 3593 LDL-receptor class A 27.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3594 3634 LDL-receptor class A 28.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3635 3675 LDL-receptor class A 29.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3678 3718 LDL-receptor class A 30.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3719 3758 LDL-receptor class A 31.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3759 3797 LDL-receptor class A 32.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3798 3836 LDL-receptor class A 33.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3842 3882 LDL-receptor class A 34.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3883 3924 LDL-receptor class A 35.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3928 3966 LDL-receptor class A 36.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 3968 4008 EGF-like 14. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4009 4050 EGF-like 15; calcium-binding.
{ECO:0000255|PROSITE-ProRule:PRU00076}.
REPEAT 4156 4198 LDL-receptor class B 35.
REPEAT 4199 4242 LDL-receptor class B 36.
REPEAT 4244 4285 LDL-receptor class B 37.
DOMAIN 4332 4370 EGF-like 16. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 4379 4413 EGF-like 17. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
REGION 4597 4610 Interaction with DAB2. {ECO:0000250}.
MOTIF 1743 1745 Cell attachment site. {ECO:0000255}.
MOTIF 4454 4463 SH3-binding. {ECO:0000255}.
MOTIF 4457 4462 PxLPxI/L motif 1; mediates interaction
with ANKRA2.
{ECO:0000269|PubMed:22649097}.
MOTIF 4460 4465 PxLPxI/L motif 2; mediates interaction
with ANKRA2.
{ECO:0000269|PubMed:22649097}.
MOTIF 4522 4527 Endocytosis signal. {ECO:0000255}.
MOTIF 4601 4606 NPXY motif.
MOTIF 4606 4609 SH2-binding. {ECO:0000255}.
MOTIF 4619 4630 SH3-binding. {ECO:0000255}.
METAL 1206 1206 Calcium; via carbonyl oxygen.
METAL 1209 1209 Calcium.
METAL 1211 1211 Calcium; via carbonyl oxygen.
METAL 1213 1213 Calcium.
METAL 1219 1219 Calcium.
METAL 1220 1220 Calcium.
MOD_RES 4464 4464 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 4467 4467 Phosphoserine.
{ECO:0000250|UniProtKB:A2ARV4}.
MOD_RES 4577 4577 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 4624 4624 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 4637 4637 Phosphothreonine.
{ECO:0000250|UniProtKB:A2ARV4}.
MOD_RES 4658 4658 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
CARBOHYD 159 159 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 259 259 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 299 299 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 340 340 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 462 462 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 657 657 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 865 865 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1063 1063 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1187 1187 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1328 1328 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1341 1341 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1384 1384 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1451 1451 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1497 1497 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1551 1551 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1676 1676 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1733 1733 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1811 1811 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2134 2134 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2178 2178 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2225 2225 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2396 2396 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2488 2488 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2548 2548 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2782 2782 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2810 2810 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2949 2949 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2989 2989 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3127 3127 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3213 3213 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3259 3259 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3317 3317 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3357 3357 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3448 3448 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3566 3566 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3682 3682 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3840 3840 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3969 3969 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3980 3980 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4070 4070 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4329 4329 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 40 {ECO:0000250}.
DISULFID 35 53 {ECO:0000250}.
DISULFID 47 62 {ECO:0000250}.
DISULFID 67 80 {ECO:0000250}.
DISULFID 74 93 {ECO:0000250}.
DISULFID 87 103 {ECO:0000250}.
DISULFID 108 120 {ECO:0000250}.
DISULFID 115 133 {ECO:0000250}.
DISULFID 127 142 {ECO:0000250}.
DISULFID 147 157 {ECO:0000250}.
DISULFID 152 170 {ECO:0000250}.
DISULFID 164 179 {ECO:0000250}.
DISULFID 183 195 {ECO:0000250}.
DISULFID 190 208 {ECO:0000250}.
DISULFID 202 217 {ECO:0000250}.
DISULFID 222 234 {ECO:0000250}.
DISULFID 229 247 {ECO:0000250}.
DISULFID 241 256 {ECO:0000250}.
DISULFID 265 278 {ECO:0000250}.
DISULFID 272 291 {ECO:0000250}.
DISULFID 285 306 {ECO:0000250}.
DISULFID 311 320 {ECO:0000250}.
DISULFID 316 329 {ECO:0000250}.
DISULFID 331 345 {ECO:0000250}.
DISULFID 351 361 {ECO:0000250}.
DISULFID 357 370 {ECO:0000250}.
DISULFID 372 384 {ECO:0000250}.
DISULFID 662 673 {ECO:0000250}.
DISULFID 669 688 {ECO:0000250}.
DISULFID 690 703 {ECO:0000250}.
DISULFID 973 987 {ECO:0000250}.
DISULFID 983 997 {ECO:0000250}.
DISULFID 999 1012 {ECO:0000250}.
DISULFID 1025 1037 {ECO:0000250}.
DISULFID 1032 1050 {ECO:0000250}.
DISULFID 1044 1059 {ECO:0000250}.
DISULFID 1066 1079 {ECO:0000250}.
DISULFID 1073 1092 {ECO:0000250}.
DISULFID 1086 1101 {ECO:0000250}.
DISULFID 1110 1122 {ECO:0000250}.
DISULFID 1117 1135 {ECO:0000250}.
DISULFID 1129 1144 {ECO:0000250}.
DISULFID 1150 1162 {ECO:0000250}.
DISULFID 1157 1175 {ECO:0000250}.
DISULFID 1169 1184 {ECO:0000250}.
DISULFID 1188 1201 {ECO:0000269|PubMed:17245526}.
DISULFID 1195 1214 {ECO:0000269|PubMed:17245526}.
DISULFID 1208 1223 {ECO:0000269|PubMed:17245526}.
DISULFID 1231 1244 {ECO:0000250}.
DISULFID 1238 1257 {ECO:0000250}.
DISULFID 1251 1267 {ECO:0000250}.
DISULFID 1272 1284 {ECO:0000250}.
DISULFID 1279 1297 {ECO:0000250}.
DISULFID 1291 1306 {ECO:0000250}.
DISULFID 1313 1326 {ECO:0000250}.
DISULFID 1320 1339 {ECO:0000250}.
DISULFID 1333 1349 {ECO:0000250}.
DISULFID 1354 1365 {ECO:0000250}.
DISULFID 1361 1374 {ECO:0000250}.
DISULFID 1376 1389 {ECO:0000250}.
DISULFID 1395 1405 {ECO:0000250}.
DISULFID 1401 1414 {ECO:0000250}.
DISULFID 1416 1429 {ECO:0000250}.
DISULFID 1705 1714 {ECO:0000250}.
DISULFID 1710 1726 {ECO:0000250}.
DISULFID 1728 1741 {ECO:0000250}.
DISULFID 2023 2034 {ECO:0000250}.
DISULFID 2030 2044 {ECO:0000250}.
DISULFID 2046 2059 {ECO:0000250}.
DISULFID 2347 2358 {ECO:0000250}.
DISULFID 2354 2369 {ECO:0000250}.
DISULFID 2371 2383 {ECO:0000250}.
DISULFID 2656 2667 {ECO:0000250}.
DISULFID 2663 2676 {ECO:0000250}.
DISULFID 2678 2693 {ECO:0000250}.
DISULFID 2701 2713 {ECO:0000250}.
DISULFID 2708 2726 {ECO:0000250}.
DISULFID 2720 2737 {ECO:0000250}.
DISULFID 2742 2754 {ECO:0000250}.
DISULFID 2749 2767 {ECO:0000250}.
DISULFID 2761 2776 {ECO:0000250}.
DISULFID 2781 2794 {ECO:0000250}.
DISULFID 2789 2807 {ECO:0000250}.
DISULFID 2801 2818 {ECO:0000250}.
DISULFID 2823 2836 {ECO:0000250}.
DISULFID 2830 2849 {ECO:0000250}.
DISULFID 2843 2860 {ECO:0000250}.
DISULFID 2865 2878 {ECO:0000250}.
DISULFID 2872 2891 {ECO:0000250}.
DISULFID 2885 2901 {ECO:0000250}.
DISULFID 2908 2920 {ECO:0000250}.
DISULFID 2915 2933 {ECO:0000250}.
DISULFID 2927 2945 {ECO:0000250}.
DISULFID 2950 2967 {ECO:0000250}.
DISULFID 2957 2980 {ECO:0000250}.
DISULFID 2974 2990 {ECO:0000250}.
DISULFID 2995 3007 {ECO:0000250}.
DISULFID 3002 3020 {ECO:0000250}.
DISULFID 3014 3029 {ECO:0000250}.
DISULFID 3034 3046 {ECO:0000250}.
DISULFID 3041 3059 {ECO:0000250}.
DISULFID 3053 3070 {ECO:0000250}.
DISULFID 3077 3089 {ECO:0000250}.
DISULFID 3084 3102 {ECO:0000250}.
DISULFID 3096 3111 {ECO:0000250}.
DISULFID 3116 3128 {ECO:0000250}.
DISULFID 3124 3137 {ECO:0000250}.
DISULFID 3139 3152 {ECO:0000250}.
DISULFID 3158 3169 {ECO:0000250}.
DISULFID 3165 3178 {ECO:0000250}.
DISULFID 3180 3193 {ECO:0000250}.
DISULFID 3471 3482 {ECO:0000250}.
DISULFID 3478 3493 {ECO:0000250}.
DISULFID 3495 3510 {ECO:0000250}.
DISULFID 3514 3527 {ECO:0000250}.
DISULFID 3521 3540 {ECO:0000250}.
DISULFID 3534 3550 {ECO:0000250}.
DISULFID 3555 3567 {ECO:0000250}.
DISULFID 3562 3580 {ECO:0000250}.
DISULFID 3574 3591 {ECO:0000250}.
DISULFID 3596 3608 {ECO:0000250}.
DISULFID 3603 3621 {ECO:0000250}.
DISULFID 3615 3632 {ECO:0000250}.
DISULFID 3637 3649 {ECO:0000250}.
DISULFID 3644 3662 {ECO:0000250}.
DISULFID 3656 3673 {ECO:0000250}.
DISULFID 3680 3694 {ECO:0000250}.
DISULFID 3688 3707 {ECO:0000250}.
DISULFID 3701 3716 {ECO:0000250}.
DISULFID 3721 3734 {ECO:0000250}.
DISULFID 3729 3747 {ECO:0000250}.
DISULFID 3741 3756 {ECO:0000250}.
DISULFID 3761 3773 {ECO:0000250}.
DISULFID 3768 3786 {ECO:0000250}.
DISULFID 3780 3795 {ECO:0000250}.
DISULFID 3800 3812 {ECO:0000250}.
DISULFID 3807 3825 {ECO:0000250}.
DISULFID 3819 3834 {ECO:0000250}.
DISULFID 3844 3856 {ECO:0000250}.
DISULFID 3851 3869 {ECO:0000250}.
DISULFID 3863 3880 {ECO:0000250}.
DISULFID 3885 3898 {ECO:0000250}.
DISULFID 3893 3911 {ECO:0000250}.
DISULFID 3905 3922 {ECO:0000250}.
DISULFID 3930 3942 {ECO:0000250}.
DISULFID 3937 3955 {ECO:0000250}.
DISULFID 3949 3964 {ECO:0000250}.
DISULFID 3972 3981 {ECO:0000250}.
DISULFID 3977 3991 {ECO:0000250}.
DISULFID 3993 4007 {ECO:0000250}.
DISULFID 4013 4023 {ECO:0000250}.
DISULFID 4019 4032 {ECO:0000250}.
DISULFID 4034 4049 {ECO:0000250}.
DISULFID 4336 4344 {ECO:0000250}.
DISULFID 4340 4353 {ECO:0000250}.
DISULFID 4355 4369 {ECO:0000250}.
DISULFID 4383 4391 {ECO:0000250}.
DISULFID 4385 4401 {ECO:0000250}.
DISULFID 4403 4412 {ECO:0000250}.
STRAND 1190 1194 {ECO:0000244|PDB:2I1P}.
STRAND 1196 1199 {ECO:0000244|PDB:2I1P}.
HELIX 1204 1206 {ECO:0000244|PDB:2I1P}.
STRAND 1207 1211 {ECO:0000244|PDB:2I1P}.
STRAND 1214 1217 {ECO:0000244|PDB:2I1P}.
HELIX 1218 1221 {ECO:0000244|PDB:2I1P}.
SEQUENCE 4660 AA; 519276 MW; E2A0CFD23D0923C3 CRC64;
MERGAAAAAW MLLLAIAACL EPVSSQECGS GNFRCDNGYC IPASWRCDGT RDCLDDTDEI
GCPPRSCESG LFLCPAEGTC IPSSWVCDED KDCSDGADEQ QNCAGTTCSA QQMTCSNGQC
IPSEYRCDHV SDCPDGSDER NCHYPTCDQL TCANGACYNT SQRCDQKVDC RDSSDEANCT
TLCSQKEFEC GSGECILRAY VCDHDNDCED NSDERNCNYD TCGGHQFTCS NGQCINQNWV
CDGDDDCQDS GDEDGCESNQ SHHRCYPREW ACPGSGRCIS IDKVCDGVPD CPEGDDENNV
TSGRTCGMGV CSVLNCEYQC HQTPFGGECF CPPGHIINSN DSRTCIDFDD CQIWGICDQK
CENRQGRHQC LCEEGYILER GQHCKSSDSF SAASVIFSNG RDLLVGDLHG RNFRILAESK
NRGMVMGVDF HYQKHRVFWT DPMQEKVFST DINGLNTQEI LNVSVDTPEN LAVDWINNKL
YLVETKVNRI DVVNLEGNQR VTLITENLGH PRGIALDPTV GYLFFSDWGS LSGQPKVERA
FMDGSNRKDL VTTKVGWPAG ITLDLVSKRV YWVDSRYDYI ETVTYDGIQR KTVARGGSLV
PHPFGISLFE EHVFFTDWTK MAVMKASKFT ETNPQVYHQS SLRPHGVTVY HALRQPNATN
PCGSNNGGCA QVCVLSHRTD NGGLGYRCKC EFGFELDDDE HRCVAVKNFL LFSSKTAVRG
IPFTLSTQED VMVPVTGSPS FFVGIDFDAQ HSTVFYSDLS KDIIYKQKID GTGKEVITAN
RLESVECLTF DWISRNLYWT DGGLKSVTVL RLADKSRRQI ISNLNNPRSI VVHPTAGYMF
LSDWFRPAKI MRAWSDGSHL MPIVNTSLGW PNGLAIDWSA SRLYWVDAFF DKIEHSTLDG
LDRKRLGHVD QMTHPFGLTV FKDNVFITDW RLGAIIRVRK SDGGDMTVIR RGISSVMHVK
AYDADLQTGS NYCSQTTHAN GDCSHFCFPV PNFQRVCGCP YGMKLQRDQM TCEGDPAREP
PTQQCGSLSF PCNNGKCVPS FFRCDGVDDC HDNSDEHQCG VFNNTCSPSA FACVRGGQCI
PGQWHCDRQN DCLDGSDEQN CPTHATSSTC PSTSFTCDNH VCIPKDWVCD TDNDCSDGSD
EKNCQASGTC QPTQFRCPDH RCISPLYVCD GDKDCADGSD EAGCVLNCTS AQFKCADGSS
CINSRYRCDG VYDCRDNSDE AGCPTRPPGM CHPDEFQCQG DGTCIPNTWE CDGHPDCIHG
SDEHTGCVPK TCSPTHFLCD NGNCIYKAWI CDGDNDCRDM SDEKDCPTQP FHCPSTQWQC
PGYSTCINLS ALCDGVFDCP NGTDESPLCN QDSCSHFNGG CTHQCMQGPF GATCLCPLGY
QLANDTKTCE DINECDIPGF CSQHCVNMRG SFRCACDPEY TLESDGRTCK VTGSENPLLV
VASRDKIIVD NITAHTHNLY SLVQDVSFVV ALDFDSVTGR VFWSDLLQGK TWSVFQNGTD
KRVVHDSGLS VTEMIAVDWI GRNLYWTDYA LETIEVSKID GSHRTVLISK NVTKPRGLAL
DPRMGDNVMF WSDWGHHPRI ERASMDGTMR TVIVQEKIYW PCGLSIDYPN RLIYFMDAYL
DYIEFCDYDG HNRRQVIASD LVLHHPHALT LFEDFVYWTD RGTRQVMQAN KWHGGNQSVV
MYSVHQPLGI TAIHPSRQPP SRNPCASASC SHLCLLSAQA PRHYSCACPS GWNLSDDSVN
CVRGDQPFLM SVRDNIIFGI SLDPEVKSND AMVPISGIQH GYDVEFDDSE QFIYWVENPG
EIHRVKTDGS NRTVFAPLSL LGSSLGLALD WVSRNIYYTT PASRSIEVLT LKGDTRYGKT
LIANDGTPLG VGFPVGIAVD PARGKLYWSD HGTDSGVPAK IASANMDGTS LKILFTGNLQ
HLEVVTLDIQ EQKLYWAVTS RGVIERGNVD GTERMILVHH LAHPWGLVVY GSFLYYSDEQ
YEVIERVDKS SGNNKVVLRD NVPYLRGLRV YHRRNAADSS NGCSNNPNAC QQICLPVPGG
MFSCACASGF KLSPDGRSCS PYNSFMVVSM LPAVRGFSLE LSDHSEAMVP VAGQGRNVLH
ADVDVANGFI YWCDFSSSVR SSNGIRRIKP DGSNFTNVVT YGIGANGIRG VALDWAAGNL
YFTNAFVYET LIEVLRINTT YRRVLLKVSV DMPRHIIVDP KHRYLFWADY GQKPKIERSF
LDCTNRTVLV SEGIVTPRGL AMDHDTGYIY WVDDSLDLIA RIHLDGGESQ VVRYGSRYPT
PYGITVFGES IIWVDRNLKK VFQASKQPGN TDPPVVIRDK INLLRDVTIF DEHAQPLSPA
ELNNNPCLQS NGGCSHFCFA LPELPTPRCG CAFGTLGNDG KSCATSQEDF LIYSLNNSLR
SLHFDPRDHS LPFQVISVAG TAIALDYDRR NNRIFFTQKL NSLRGQISYV SLYSGSSSPT
VLLSNIGVTD GIAFDWINRR IYYSDFSNQT INSMAEDGSN RAVIARVSKP RAIVLDPCRG
YMYWTDWGTN AKIERATLGG NFRVPIVNTS LVWPNGLALD LETDLLYWAD ASLQKIERST
LTGTNREVVV STAFHSFGLT VYGQYIYWTD LYTRKIYRAN KYDGSDLVAM TTRLPTQPSG
ISTVVKTQRQ QCSNPCDQFN GGCSHICAPG PNGAECQCPH EGNWYLANDN KYCVVDTGTR
CNQLQFTCLN GHCINQDWKC DNDNDCGDGS DELPTVCAFH TCRSTAFTCG NGRCVPYHYR
CDYYNDCGDN SDEAGCLFRN CNSTTEFTCS NGRCIPLSYV CNGINNCHDN DTSDEKNCPP
HTCPPDFTKC QTTNICVPRA FLCDGDNDCG DGSDENPIYC ASHTCRSNEF QCLSPQRCIP
SYWFCDGEAD CADGSDEPDT CGHSVNTCRA SQFQCDNGRC ISGNWVCDGD NDCGDMSDED
QRHHCELQNC SSTQFTCVNS RPPNRRCIPQ YWVCDGDADC SDALDELQNC TMRTCSAGEF
SCANGRCVRQ SFRCDRRNDC GDYSDERGCS YPPCHANQFT CQNGRCIPRF FVCDEDNDCG
DGSDEQEHLC HTPEPTCPLH QFRCDNGHCI EMGRVCNHVD DCSDNSDEKG CGINECLDSS
ISRCDHNCTD TITSFYCSCL PGYKLMSDKR SCVDIDECKE SPQLCSQKCE NVVGSYICKC
APGYIREPDG KSCRQNSNIE PYLIFSNRYY IRNLTTDGSS YSLILQGLGN VVALDFDRVE
KRLYWIDAEK QIIERMFLNK TNRETIINHR LRRAESLAVD WVSRKLYWLD AILDCLFVSD
LEGRHRKMIA QHCVDANNTF CFEHPRGIVL HPQRGHVYWA DWGVHAYIGR IGMDGTNKSV
IISTKIEWPN AITIDYTNDL LYWADAHLGY IEFSDLEGHH RHTVYDGSLP HPFALTIFED
TVFWTDWNTR TVEKGNKYDG SGRVVLVNTT HKPFDIHVYH PYRQPIMSNP CGTNNGGCSH
LCLIKAGGRG FTCACPDDFQ TVQLRDRTLC MPMCSSTQFL CGNNEKCIPI WWKCDGQKDC
SDGSDEPDLC PHRFCRLGQF QCRDGNCTSP QALCNARQDC ADGSDEDRVL CEHHRCESNE
WQCANKRCIP QSWQCDSVND CLDNSDEDTS HCASRTCRPG QFKCNNGRCI PQSWKCDVDN
DCGDYSDEPI DECTTAAYNC DNHTEFSCKT NYRCIPQWAV CNGFDDCRDN SDEQGCESVP
CHPSGDFRCA NHHCIPLRWK CDGTDDCGDN SDEENCVPRE CSESEFRCAD QQCIPSRWVC
DQENDCGDNS DERDCEMKTC HPEHFQCTSG HCVPKALACD GRADCLDASD ESACPTRFPN
GTYCPAAMFE CKNHVCIQSF WICDGENDCV DGSDEEIHLC FNIPCESPQR FRCDNSRCVY
GHQLCNGVDD CGDGSDEKEE HCRKPTHKPC TDTEYKCSNG NCISQHYVCD NVNDCGDLSD
ETGCNLGDNR TCAENICEQN CTQLSSGGFI CSCRPGFKPS TSDKNSCQDI NECEEFGICP
QSCRNSKGSY ECFCVDGFKS MSTHYGERCA ADGSPPLLLL PENVRIRKYN TSSEKFSEYL
EEEEHIQTID YDWDPEHIGL SVVYYTVLAQ GSQFGAIKRA YIPNFESGSN NPIREVDLGL
KYLMQPDGLA VDWVGRHIYW SDAKSQRIEV ATLDGRYRKW LITTQLDQPA AIAVNPKLGL
MFWTDQGKQP KIESAWMNGE HRSVLVSENL GWPNGLSIDY LNDDRVYWSD SKEDVIEAIK
YDGTDRRLII NEAMKPFSLD IFEDKLYWVA KEKGEVWRQN KFGKENKEKV LVVNPWLTQV
RIFHQLRYNQ SVSNPCKQVC SHLCLLRPGG YSCACPQGSD FVTGSTVQCD AASELPVTMP
PPCRCMHGGN CYFDENELPK CKCSSGYSGE YCEVGLSRGI PPGTTMAVLL TFVIVIIVGA
LVLVGLFHYR KTGSLLPTLP KLPSLSSLAK PSENGNGVTF RSGADVNMDI GVSPFGPETI
IDRSMAMNEH FVMEVGKQPV IFENPMYAAK DNTSKVALAV QGPSTGAQVT VPENVENQNY
GRPIDPSEIV PEPKPASPGA DEIQGKKWNI FKRKPKQTTN FENPIYAEMD SEVKDAVAVA
PPPSPSLPAK ASKRNLTPGY TATEDTFKDT ANLVKEDSDV


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