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Apolipoprotein(a) (Apo(a)) (Lp(a)) (EC 3.4.21.-)

 APOA_HUMAN              Reviewed;        4548 AA.
P08519; Q5VTD7; Q9UD88;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
01-AUG-1988, sequence version 1.
25-APR-2018, entry version 172.
RecName: Full=Apolipoprotein(a);
Short=Apo(a);
Short=Lp(a);
EC=3.4.21.-;
Flags: Precursor;
Name=LPA;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND POLYMORPHISM.
PubMed=3670400; DOI=10.1038/330132a0;
McLean J.W., Tomlison J.E., Kuang W.-J., Eaton D.L., Chen E.Y.,
Fless G.M., Scanu A.M., Lawn R.M.;
"cDNA sequence of human apolipoprotein(a) is homologous to
plasminogen.";
Nature 330:132-137(1987).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 4184-4208.
TISSUE=Lymphocyte;
PubMed=7848387; DOI=10.1016/0925-4439(93)90130-S;
Pfaffinger D., Mc Lean J., Scanu A.M.;
"Amplification of human APO(a) kringle 4-37 from blood lymphocyte
DNA.";
Biochim. Biophys. Acta 1225:107-109(1993).
[4]
FUNCTION AS A SERINE PROTEASE.
PubMed=2531657;
Salonen E.-M., Jauhiainen M., Zardi L., Vaheri A., Ehnholm C.;
"Lipoprotein(a) binds to fibronectin and has serine proteinase
activity capable of cleaving it.";
EMBO J. 8:4035-4040(1989).
[5]
REVIEW.
PubMed=2530631; DOI=10.1126/science.2530631;
Utermann G.;
"The mysteries of lipoprotein(a).";
Science 246:904-910(1989).
[6]
STRUCTURE OF N-LINKED AND O-LINKED CARBOHYDRATES, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=11294842; DOI=10.1074/jbc.M102150200;
Garner B., Merry A.H., Royle L., Harvey D.J., Rudd P.M., Thillet J.;
"Structural elucidation of the N- and O-glycans of human
apolipoprotein(a): role of o-glycans in conferring protease
resistance.";
J. Biol. Chem. 276:22200-22208(2001).
[7]
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).
[8]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 4121-4208.
PubMed=8642595; DOI=10.1006/jmbi.1996.0122;
Mikol V., Lograsso P.V., Boettcher B.R.;
"Crystal structures of apolipoprotein(a) kringle IV37 free and
complexed with 6-aminohexanoic acid and with p-aminomethylbenzoic
acid: existence of novel and expected binding modes.";
J. Mol. Biol. 256:751-761(1996).
[9]
VARIANT ARG-4193.
PubMed=7918682; DOI=10.1016/0925-4439(94)90104-X;
Scanu A.M., Pfaffinger D., Lee J.C., Hinman J.;
"A single point mutation (Trp72-->Arg) in human apo(a) kringle 4-37
associated with a lysine binding defect in Lp(a).";
Biochim. Biophys. Acta 1227:41-45(1994).
-!- FUNCTION: Apo(a) is the main constituent of lipoprotein(a)
(Lp(a)). It has serine proteinase activity and is able of
autoproteolysis. Inhibits tissue-type plasminogen activator 1.
Lp(a) may be a ligand for megalin/Gp 330.
{ECO:0000269|PubMed:2531657}.
-!- SUBUNIT: Disulfide-linked to apo-B100. Binds to fibronectin and
decorin.
-!- INTERACTION:
P02749:APOH; NbExp=4; IntAct=EBI-9232288, EBI-2114682;
P02751:FN1; NbExp=2; IntAct=EBI-9232288, EBI-1220319;
-!- PTM: N- and O-glycosylated. The N-glycans are complex biantennary
structures present in either a mono- or disialylated state. The O-
glycans are mostly (80%) represented by the monosialylated core
type I structure, NeuNAcalpha2-3Galbeta1-3GalNAc, with smaller
amounts of disialylated and non-sialylated O-glycans also
detected. {ECO:0000269|PubMed:11294842}.
-!- POLYMORPHISM: The reference genome sequence encodes a variant that
contains 16 Kringle domains and that lack residues 533 to 3040.
Depending on the individual, the encoded protein contains 2-43
copies of kringle-type domains. The allele represented here
contains 38 copies of the kringle-type repeats.
{ECO:0000269|PubMed:3670400}.
-!- MISCELLANEOUS: Apo(a) is known to be proteolytically cleaved,
leading to the formation of the so-called mini-Lp(a). Apo(a)
fragments accumulate in atherosclerotic lesions, where they may
promote thrombogenesis. O-glycosylation may limit the extent of
proteolytic fragmentation. Homology with plasminogen kringles IV
and V is thought to underlie the atherogenicity of the protein,
because the fragments are competing with plasminogen for
fibrin(ogen) binding.
-!- SIMILARITY: Belongs to the peptidase S1 family. Plasminogen
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=SHMPD; Note=The Singapore human mutation and
polymorphism database;
URL="http://shmpd.bii.a-star.edu.sg/gene.php?genestart=A&genename=APOA";
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EMBL; X06290; CAA29618.1; -; mRNA.
EMBL; AL109933; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL596089; -; NOT_ANNOTATED_CDS; Genomic_DNA.
PIR; S00657; S00657.
UniGene; Hs.520120; -.
PDB; 1I71; X-ray; 1.45 A; A=3781-3863.
PDB; 1JFN; NMR; -; A=3665-3770.
PDB; 1KIV; X-ray; 2.10 A; A=4124-4201.
PDB; 2FEB; NMR; -; A=3885-3980.
PDB; 3KIV; X-ray; 1.80 A; A=4123-4201.
PDB; 4BV5; X-ray; 2.10 A; A/B=4123-4201.
PDB; 4BV7; X-ray; 1.70 A; A=4123-4201.
PDB; 4BVC; X-ray; 1.60 A; A=4123-4201.
PDB; 4BVD; X-ray; 1.68 A; A=4123-4201.
PDB; 4BVV; X-ray; 1.80 A; A=4227-4307.
PDB; 4BVW; X-ray; 2.00 A; A/B=3781-3859.
PDB; 4KIV; X-ray; 2.20 A; A=4123-4201.
PDBsum; 1I71; -.
PDBsum; 1JFN; -.
PDBsum; 1KIV; -.
PDBsum; 2FEB; -.
PDBsum; 3KIV; -.
PDBsum; 4BV5; -.
PDBsum; 4BV7; -.
PDBsum; 4BVC; -.
PDBsum; 4BVD; -.
PDBsum; 4BVV; -.
PDBsum; 4BVW; -.
PDBsum; 4KIV; -.
ProteinModelPortal; P08519; -.
SMR; P08519; -.
IntAct; P08519; 2.
STRING; 9606.ENSP00000321334; -.
DrugBank; DB00513; Aminocaproic Acid.
MEROPS; S01.999; -.
GlyConnect; 56; -.
iPTMnet; P08519; -.
PhosphoSitePlus; P08519; -.
UniCarbKB; P08519; -.
DMDM; 114062; -.
PaxDb; P08519; -.
PeptideAtlas; P08519; -.
PRIDE; P08519; -.
Ensembl; ENST00000316300; ENSP00000321334; ENSG00000198670.
Ensembl; ENST00000447678; ENSP00000395608; ENSG00000198670.
UCSC; uc063sqy.1; human.
DisGeNET; 4018; -.
EuPathDB; HostDB:ENSG00000198670.11; -.
GeneCards; LPA; -.
H-InvDB; HIX0057735; -.
HGNC; HGNC:6667; LPA.
HPA; CAB016072; -.
HPA; HPA060604; -.
MIM; 152200; gene+phenotype.
neXtProt; NX_P08519; -.
PharmGKB; PA30432; -.
eggNOG; ENOG410IDXR; Eukaryota.
eggNOG; COG5640; LUCA.
HOGENOM; HOG000170962; -.
HOVERGEN; HBG004270; -.
OrthoDB; EOG091G0AH5; -.
TreeFam; TF329901; -.
Reactome; R-HSA-8964041; LDL remodeling.
ChiTaRS; LPA; human.
EvolutionaryTrace; P08519; -.
PRO; PR:P08519; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000198670; -.
CleanEx; HS_LPA; -.
ExpressionAtlas; P08519; baseline and differential.
Genevisible; P08519; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0034358; C:plasma lipoprotein particle; IDA:BHF-UCL.
GO; GO:0034185; F:apolipoprotein binding; IPI:BHF-UCL.
GO; GO:0004866; F:endopeptidase inhibitor activity; TAS:ProtInc.
GO; GO:0001968; F:fibronectin binding; IPI:BHF-UCL.
GO; GO:0008201; F:heparin binding; NAS:BHF-UCL.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:BHF-UCL.
GO; GO:0008015; P:blood circulation; TAS:ProtInc.
GO; GO:0006629; P:lipid metabolic process; NAS:ProtInc.
GO; GO:0006869; P:lipid transport; IEA:UniProtKB-KW.
GO; GO:0034374; P:low-density lipoprotein particle remodeling; TAS:Reactome.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.20.10; -; 38.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR038178; Kringle_sf.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00051; Kringle; 38.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00130; KR; 38.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57440; SSF57440; 38.
PROSITE; PS00021; KRINGLE_1; 38.
PROSITE; PS50070; KRINGLE_2; 38.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
3D-structure; Atherosclerosis; Autocatalytic cleavage;
Complete proteome; Disulfide bond; Glycoprotein; Hydrolase; Kringle;
Lipid transport; Polymorphism; Protease; Reference proteome; Repeat;
Serine protease; Signal; Transport.
SIGNAL 1 19
CHAIN 20 4548 Apolipoprotein(a).
/FTId=PRO_0000028097.
DOMAIN 20 130 Kringle 1. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 131 244 Kringle 2. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 245 358 Kringle 3. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 359 472 Kringle 4. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 473 586 Kringle 5. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 587 700 Kringle 6. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 701 814 Kringle 7. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 815 928 Kringle 8. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 929 1042 Kringle 9. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 1043 1156 Kringle 10. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 1157 1270 Kringle 11. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 1271 1384 Kringle 12. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 1385 1498 Kringle 13. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 1499 1612 Kringle 14. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 1613 1726 Kringle 15. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 1727 1840 Kringle 16. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 1841 1954 Kringle 17. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 1955 2068 Kringle 18. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 2069 2182 Kringle 19. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 2183 2296 Kringle 20. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 2297 2410 Kringle 21. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 2411 2524 Kringle 22. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 2525 2638 Kringle 23. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 2639 2752 Kringle 24. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 2753 2866 Kringle 25. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 2867 2980 Kringle 26. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 2981 3094 Kringle 27. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 3095 3208 Kringle 28. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 3209 3322 Kringle 29. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 3323 3436 Kringle 30. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 3437 3550 Kringle 31. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 3551 3664 Kringle 32. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 3665 3770 Kringle 33. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 3771 3884 Kringle 34. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 3885 3998 Kringle 35. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 3999 4112 Kringle 36. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 4113 4226 Kringle 37. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 4227 4327 Kringle 38. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 4328 4546 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 4369 4369 Charge relay system.
ACT_SITE 4412 4412 Charge relay system.
ACT_SITE 4498 4498 Charge relay system.
CARBOHYD 61 61 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 101 101 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 215 215 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 329 329 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 443 443 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 557 557 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 671 671 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 785 785 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 899 899 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1013 1013 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1127 1127 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1241 1241 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1355 1355 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1469 1469 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1583 1583 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1697 1697 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1811 1811 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1925 1925 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2039 2039 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2153 2153 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2267 2267 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2381 2381 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2495 2495 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2609 2609 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2723 2723 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2837 2837 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 2951 2951 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3065 3065 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3179 3179 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3293 3293 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3407 3407 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3521 3521 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3635 3635 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3749 3749 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3855 3855 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3889 3889 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 3969 3969 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4083 4083 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 4197 4197 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 28 105 {ECO:0000250}.
DISULFID 49 88 {ECO:0000250}.
DISULFID 77 100 {ECO:0000250}.
DISULFID 142 219 {ECO:0000250}.
DISULFID 163 202 {ECO:0000250}.
DISULFID 191 214 {ECO:0000250}.
DISULFID 256 333 {ECO:0000250}.
DISULFID 277 316 {ECO:0000250}.
DISULFID 305 328 {ECO:0000250}.
DISULFID 370 447 {ECO:0000250}.
DISULFID 391 430 {ECO:0000250}.
DISULFID 419 442 {ECO:0000250}.
DISULFID 484 561 {ECO:0000250}.
DISULFID 505 544 {ECO:0000250}.
DISULFID 533 556 {ECO:0000250}.
DISULFID 598 675 {ECO:0000250}.
DISULFID 619 658 {ECO:0000250}.
DISULFID 647 670 {ECO:0000250}.
DISULFID 712 789 {ECO:0000250}.
DISULFID 733 772 {ECO:0000250}.
DISULFID 761 784 {ECO:0000250}.
DISULFID 826 903 {ECO:0000250}.
DISULFID 847 886 {ECO:0000250}.
DISULFID 875 898 {ECO:0000250}.
DISULFID 940 1017 {ECO:0000250}.
DISULFID 961 1000 {ECO:0000250}.
DISULFID 989 1012 {ECO:0000250}.
DISULFID 1054 1131 {ECO:0000250}.
DISULFID 1075 1114 {ECO:0000250}.
DISULFID 1103 1126 {ECO:0000250}.
DISULFID 1168 1245 {ECO:0000250}.
DISULFID 1189 1228 {ECO:0000250}.
DISULFID 1217 1240 {ECO:0000250}.
DISULFID 1282 1359 {ECO:0000250}.
DISULFID 1303 1342 {ECO:0000250}.
DISULFID 1331 1354 {ECO:0000250}.
DISULFID 1396 1473 {ECO:0000250}.
DISULFID 1417 1456 {ECO:0000250}.
DISULFID 1445 1468 {ECO:0000250}.
DISULFID 1510 1587 {ECO:0000250}.
DISULFID 1531 1570 {ECO:0000250}.
DISULFID 1559 1582 {ECO:0000250}.
DISULFID 1624 1701 {ECO:0000250}.
DISULFID 1645 1684 {ECO:0000250}.
DISULFID 1673 1696 {ECO:0000250}.
DISULFID 1738 1815 {ECO:0000250}.
DISULFID 1759 1798 {ECO:0000250}.
DISULFID 1787 1810 {ECO:0000250}.
DISULFID 1852 1929 {ECO:0000250}.
DISULFID 1873 1912 {ECO:0000250}.
DISULFID 1901 1924 {ECO:0000250}.
DISULFID 1966 2043 {ECO:0000250}.
DISULFID 1987 2026 {ECO:0000250}.
DISULFID 2015 2038 {ECO:0000250}.
DISULFID 2080 2157 {ECO:0000250}.
DISULFID 2101 2140 {ECO:0000250}.
DISULFID 2129 2152 {ECO:0000250}.
DISULFID 2194 2271 {ECO:0000250}.
DISULFID 2215 2254 {ECO:0000250}.
DISULFID 2243 2266 {ECO:0000250}.
DISULFID 2308 2385 {ECO:0000250}.
DISULFID 2329 2368 {ECO:0000250}.
DISULFID 2357 2380 {ECO:0000250}.
DISULFID 2422 2499 {ECO:0000250}.
DISULFID 2443 2482 {ECO:0000250}.
DISULFID 2471 2494 {ECO:0000250}.
DISULFID 2536 2613 {ECO:0000250}.
DISULFID 2557 2596 {ECO:0000250}.
DISULFID 2585 2608 {ECO:0000250}.
DISULFID 2650 2727 {ECO:0000250}.
DISULFID 2671 2710 {ECO:0000250}.
DISULFID 2699 2722 {ECO:0000250}.
DISULFID 2764 2841 {ECO:0000250}.
DISULFID 2785 2824 {ECO:0000250}.
DISULFID 2813 2836 {ECO:0000250}.
DISULFID 2878 2955 {ECO:0000250}.
DISULFID 2899 2938 {ECO:0000250}.
DISULFID 2927 2950 {ECO:0000250}.
DISULFID 2992 3069 {ECO:0000250}.
DISULFID 3013 3052 {ECO:0000250}.
DISULFID 3041 3064 {ECO:0000250}.
DISULFID 3106 3183 {ECO:0000250}.
DISULFID 3127 3166 {ECO:0000250}.
DISULFID 3155 3178 {ECO:0000250}.
DISULFID 3220 3297 {ECO:0000250}.
DISULFID 3241 3280 {ECO:0000250}.
DISULFID 3269 3292 {ECO:0000250}.
DISULFID 3334 3411 {ECO:0000250}.
DISULFID 3355 3394 {ECO:0000250}.
DISULFID 3383 3406 {ECO:0000250}.
DISULFID 3448 3525 {ECO:0000250}.
DISULFID 3469 3508 {ECO:0000250}.
DISULFID 3497 3520 {ECO:0000250}.
DISULFID 3562 3639 {ECO:0000250}.
DISULFID 3583 3622 {ECO:0000250}.
DISULFID 3611 3634 {ECO:0000250}.
DISULFID 3676 3753
DISULFID 3697 3736
DISULFID 3725 3748
DISULFID 3782 3859
DISULFID 3803 3842
DISULFID 3831 3854
DISULFID 3896 3973 {ECO:0000250}.
DISULFID 3917 3956 {ECO:0000250}.
DISULFID 3945 3968 {ECO:0000250}.
DISULFID 4010 4087 {ECO:0000250}.
DISULFID 4031 4070 {ECO:0000250}.
DISULFID 4059 4082 {ECO:0000250}.
DISULFID 4124 4201 {ECO:0000250}.
DISULFID 4145 4184 {ECO:0000250}.
DISULFID 4173 4196 {ECO:0000250}.
DISULFID 4228 4307 {ECO:0000250}.
DISULFID 4249 4290 {ECO:0000250}.
DISULFID 4278 4302 {ECO:0000250}.
DISULFID 4354 4370 {ECO:0000250}.
DISULFID 4446 4504 {ECO:0000250}.
DISULFID 4476 4483 {ECO:0000250}.
DISULFID 4494 4522 {ECO:0000250}.
VARIANT 3498 3498 R -> Q (in dbSNP:rs41259144).
/FTId=VAR_047293.
VARIANT 3866 3866 L -> V (in dbSNP:rs7765803).
/FTId=VAR_047294.
VARIANT 3880 3880 L -> V (in dbSNP:rs7765781).
/FTId=VAR_047295.
VARIANT 3907 3907 T -> P (in dbSNP:rs41272110).
/FTId=VAR_047296.
VARIANT 3929 3929 R -> Q (in dbSNP:rs41272112).
/FTId=VAR_047297.
VARIANT 4106 4106 M -> T (in dbSNP:rs41264308).
/FTId=VAR_047298.
VARIANT 4187 4187 M -> T (in dbSNP:rs1801693).
/FTId=VAR_047299.
VARIANT 4193 4193 W -> R (loss of lysine-sepharose
binding). {ECO:0000269|PubMed:7918682}.
/FTId=VAR_006633.
VARIANT 4330 4330 G -> A (in dbSNP:rs41265936).
/FTId=VAR_047300.
VARIANT 4399 4399 I -> M (in dbSNP:rs3798220).
/FTId=VAR_047301.
VARIANT 4524 4524 R -> C (in dbSNP:rs3124784).
/FTId=VAR_047302.
STRAND 3665 3667 {ECO:0000244|PDB:1JFN}.
TURN 3679 3683 {ECO:0000244|PDB:1JFN}.
STRAND 3704 3706 {ECO:0000244|PDB:1JFN}.
HELIX 3712 3714 {ECO:0000244|PDB:1JFN}.
TURN 3716 3718 {ECO:0000244|PDB:1JFN}.
STRAND 3735 3740 {ECO:0000244|PDB:1JFN}.
STRAND 3745 3749 {ECO:0000244|PDB:1JFN}.
STRAND 3782 3784 {ECO:0000244|PDB:4BVW}.
STRAND 3810 3812 {ECO:0000244|PDB:4BVW}.
TURN 3818 3820 {ECO:0000244|PDB:1I71}.
TURN 3822 3825 {ECO:0000244|PDB:1I71}.
STRAND 3834 3836 {ECO:0000244|PDB:1I71}.
STRAND 3841 3846 {ECO:0000244|PDB:1I71}.
STRAND 3851 3855 {ECO:0000244|PDB:1I71}.
STRAND 3889 3893 {ECO:0000244|PDB:2FEB}.
STRAND 3912 3914 {ECO:0000244|PDB:2FEB}.
STRAND 3924 3926 {ECO:0000244|PDB:2FEB}.
STRAND 3951 3953 {ECO:0000244|PDB:2FEB}.
STRAND 4124 4126 {ECO:0000244|PDB:4BV7}.
STRAND 4129 4131 {ECO:0000244|PDB:1KIV}.
STRAND 4152 4154 {ECO:0000244|PDB:3KIV}.
TURN 4160 4162 {ECO:0000244|PDB:4BVC}.
TURN 4164 4167 {ECO:0000244|PDB:3KIV}.
STRAND 4183 4188 {ECO:0000244|PDB:4BVC}.
STRAND 4193 4197 {ECO:0000244|PDB:4BVC}.
STRAND 4256 4258 {ECO:0000244|PDB:4BVV}.
STRAND 4261 4263 {ECO:0000244|PDB:4BVV}.
TURN 4265 4267 {ECO:0000244|PDB:4BVV}.
STRAND 4289 4293 {ECO:0000244|PDB:4BVV}.
STRAND 4299 4301 {ECO:0000244|PDB:4BVV}.
SEQUENCE 4548 AA; 501319 MW; 96921BE96A465C5F CRC64;
MEHKEVVLLL LLFLKSAAPE QSHVVQDCYH GDGQSYRGTY STTVTGRTCQ AWSSMTPHQH
NRTTENYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP
VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY
YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA
PSEQAPTEQR PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL
IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP
TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR
NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG
VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA
APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE QRPGVQECYH
GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT
RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY
RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR
WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR PGVQECYHGN GQSYRGTYST
TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL
TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT
CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA
EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS
MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA
PPTVTPVPSL EAPSEQAPTE QRPGVQECYH GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH
SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP
VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY
YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA
PSEQAPTEQR PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL
IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP
TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR
NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG
VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA
APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE QRPGVQECYH
GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT
RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY
RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR
WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR PGVQECYHGN GQSYRGTYST
TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL
TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT
CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA
EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS
MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA
PPTVTPVPSL EAPSEQAPTE QRPGVQECYH GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH
SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP
VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY
YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA
PSEQAPTEQR PGVQECYHGN GQSYRGTYST TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL
IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP
TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR
NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG
VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS MTPHSHSRTP EYYPNAGLIM NYCRNPDAVA
APYCYTRDPG VRWEYCNLTQ CSDAEGTAVA PPTVTPVPSL EAPSEQAPTE QRPGVQECYH
GNGQSYRGTY STTVTGRTCQ AWSSMTPHSH SRTPEYYPNA GLIMNYCRNP DAVAAPYCYT
RDPGVRWEYC NLTQCSDAEG TAVAPPTVTP VPSLEAPSEQ APTEQRPGVQ ECYHGNGQSY
RGTYSTTVTG RTCQAWSSMT PHSHSRTPEY YPNAGLIMNY CRNPDAVAAP YCYTRDPGVR
WEYCNLTQCS DAEGTAVAPP TVTPVPSLEA PSEQAPTEQR PGVQECYHGN GQSYRGTYST
TVTGRTCQAW SSMTPHSHSR TPEYYPNAGL IMNYCRNPDA VAAPYCYTRD PGVRWEYCNL
TQCSDAEGTA VAPPTVTPVP SLEAPSEQAP TEQRPGVQEC YHGNGQSYRG TYSTTVTGRT
CQAWSSMTPH SHSRTPEYYP NAGLIMNYCR NPDAVAAPYC YTRDPGVRWE YCNLTQCSDA
EGTAVAPPTV TPVPSLEAPS EQAPTEQRPG VQECYHGNGQ SYRGTYSTTV TGRTCQAWSS
MTPHSHSRTP EYYPNAGLIM NYCRNPDPVA APYCYTRDPS VRWEYCNLTQ CSDAEGTAVA
PPTITPIPSL EAPSEQAPTE QRPGVQECYH GNGQSYQGTY FITVTGRTCQ AWSSMTPHSH
SRTPAYYPNA GLIKNYCRNP DPVAAPWCYT TDPSVRWEYC NLTRCSDAEW TAFVPPNVIL
APSLEAFFEQ ALTEETPGVQ DCYYHYGQSY RGTYSTTVTG RTCQAWSSMT PHQHSRTPEN
YPNAGLTRNY CRNPDAEIRP WCYTMDPSVR WEYCNLTQCL VTESSVLATL TVVPDPSTEA
SSEEAPTEQS PGVQDCYHGD GQSYRGSFST TVTGRTCQSW SSMTPHWHQR TTEYYPNGGL
TRNYCRNPDA EISPWCYTMD PNVRWEYCNL TQCPVTESSV LATSTAVSEQ APTEQSPTVQ
DCYHGDGQSY RGSFSTTVTG RTCQSWSSMT PHWHQRTTEY YPNGGLTRNY CRNPDAEIRP
WCYTMDPSVR WEYCNLTQCP VMESTLLTTP TVVPVPSTEL PSEEAPTENS TGVQDCYRGD
GQSYRGTLST TITGRTCQSW SSMTPHWHRR IPLYYPNAGL TRNYCRNPDA EIRPWCYTMD
PSVRWEYCNL TRCPVTESSV LTTPTVAPVP STEAPSEQAP PEKSPVVQDC YHGDGRSYRG
ISSTTVTGRT CQSWSSMIPH WHQRTPENYP NAGLTENYCR NPDSGKQPWC YTTDPCVRWE
YCNLTQCSET ESGVLETPTV VPVPSMEAHS EAAPTEQTPV VRQCYHGNGQ SYRGTFSTTV
TGRTCQSWSS MTPHRHQRTP ENYPNDGLTM NYCRNPDADT GPWCFTMDPS IRWEYCNLTR
CSDTEGTVVA PPTVIQVPSL GPPSEQDCMF GNGKGYRGKK ATTVTGTPCQ EWAAQEPHRH
STFIPGTNKW AGLEKNYCRN PDGDINGPWC YTMNPRKLFD YCDIPLCASS SFDCGKPQVE
PKKCPGSIVG GCVAHPHSWP WQVSLRTRFG KHFCGGTLIS PEWVLTAAHC LKKSSRPSSY
KVILGAHQEV NLESHVQEIE VSRLFLEPTQ ADIALLKLSR PAVITDKVMP ACLPSPDYMV
TARTECYITG WGETQGTFGT GLLKEAQLLV IENEVCNHYK YICAEHLARG TDSCQGDSGG
PLVCFEKDKY ILQGVTSWGL GCARPNKPGV YARVSRFVTW IEGMMRNN


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