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Serum amyloid P-component (SAP) (9.5S alpha-1-glycoprotein) [Cleaved into: Serum amyloid P-component(1-203)]

 SAMP_HUMAN              Reviewed;         223 AA.
P02743;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-FEB-1995, sequence version 2.
22-NOV-2017, entry version 198.
RecName: Full=Serum amyloid P-component;
Short=SAP;
AltName: Full=9.5S alpha-1-glycoprotein;
Contains:
RecName: Full=Serum amyloid P-component(1-203);
Flags: Precursor;
Name=APCS; Synonyms=PTX2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2987268;
Mantzouranis E.C., Dowton S.B., Whitehead A.S., Edge M.D.,
Bruns G.A.P., Colten H.R.;
"Human serum amyloid P component. cDNA isolation, complete sequence of
pre-serum amyloid P component, and localization of the gene to
chromosome 1.";
J. Biol. Chem. 260:7752-7756(1985).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=3029048;
Ohnishi S., Maeda S., Shimada K., Arao T.;
"Isolation and characterization of the complete complementary and
genomic DNA sequences of human serum amyloid P component.";
J. Biochem. 100:849-858(1986).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Skeletal muscle;
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]
PROTEIN SEQUENCE OF 20-223.
PubMed=4055725;
Prelli F., Pras M., Frangione B.;
"The primary structure of human tissue amyloid P component from a
patient with primary idiopathic amyloidosis.";
J. Biol. Chem. 260:12895-12898(1985).
[8]
PROTEIN SEQUENCE OF 20-49.
PubMed=81686; DOI=10.1021/bi00613a030;
Thompson A.R., Enfield D.L.;
"Human plasma P component: isolation and characterization.";
Biochemistry 17:4304-4311(1978).
[9]
STRUCTURE OF CARBOHYDRATE, AND MASS SPECTROMETRY.
PubMed=8202534; DOI=10.1073/pnas.91.12.5602;
Pepys M.B., Rademacher T.W., Amatayakul-Chantler S., Williams P.,
Noble G.E., Hutchinson W.L., Hawkins P.N., Nelson S.R.,
Gallimore J.R., Herbert J., Hutton T., Dwek R.A.;
"Human serum amyloid P component is an invariant constituent of
amyloid deposits and has a uniquely homogeneous glycostructure.";
Proc. Natl. Acad. Sci. U.S.A. 91:5602-5606(1994).
[10]
TISSUE SPECIFICITY, AND MASS SPECTROMETRY.
PubMed=15174148; DOI=10.1002/pmic.200300690;
Kiernan U.A., Nedelkov D., Tubbs K.A., Niederkofler E.E., Nelson R.W.;
"Proteomic characterization of novel serum amyloid P component
variants from human plasma and urine.";
Proteomics 4:1825-1829(2004).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-51.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
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).
[15]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=8114934; DOI=10.1038/367338a0;
Emsley J., White H.E., O'Hara B., Oliva G., Srinivasan N.,
Tickle I.J., Blundell T.L., Pepys M.B., Wood S.P.;
"Structure of pentameric human serum amyloid P component.";
Nature 367:338-345(1994).
[16]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=9217261; DOI=10.1006/jmbi.1997.1075;
Hohenester E., Hutchinson W.L., Pepys M.B., Wood S.P.;
"Crystal structure of a decameric complex of human serum amyloid P
component with bound dAMP.";
J. Mol. Biol. 269:570-578(1997).
[17]
VARIANT [LARGE SCALE ANALYSIS] SER-141.
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).
-!- FUNCTION: Can interact with DNA and histones and may scavenge
nuclear material released from damaged circulating cells. May also
function as a calcium-dependent lectin.
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 2 calcium ions per subunit.;
-!- SUBUNIT: Homopentamer. Pentraxin (or pentaxin) have a discoid
arrangement of 5 non-covalently bound subunits.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-2115799, EBI-2115799;
-!- SUBCELLULAR LOCATION: Secreted.
-!- TISSUE SPECIFICITY: Found in serum and urine.
{ECO:0000269|PubMed:15174148}.
-!- PTM: N-glycosylated with a complex biantennary oligosaccharide
chain with a sialic acid at the end (disialo-SAP). Monosialo-SAP
as well as asioalo-SAP are also detected (PubMed:15174148).
{ECO:0000269|PubMed:15174148, ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
-!- MASS SPECTROMETRY: Mass=25462.5; Mass_error=1.1;
Method=Electrospray; Range=20-223;
Evidence={ECO:0000269|PubMed:15174148,
ECO:0000269|PubMed:8202534};
-!- MASS SPECTROMETRY: Mass=25463; Mass_error=3; Method=MALDI;
Range=20-223; Evidence={ECO:0000269|PubMed:15174148,
ECO:0000269|PubMed:8202534};
-!- MASS SPECTROMETRY: Mass=1285.78; Method=MALDI; Range=213-223;
Evidence={ECO:0000269|PubMed:15174148};
-!- MASS SPECTROMETRY: Mass=1186.71; Method=MALDI; Range=213-222;
Evidence={ECO:0000269|PubMed:15174148};
-!- DISEASE: Note=SAP is a precursor of amyloid component P which is
found in basement membrane and associated with amyloid deposits.
-!- SIMILARITY: Belongs to the pentraxin family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Serum amyloid P component
entry;
URL="https://en.wikipedia.org/wiki/Serum_Amyloid_P_Component";
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EMBL; D00097; BAA00060.1; -; Genomic_DNA.
EMBL; M10944; AAA60302.1; -; mRNA.
EMBL; X04608; CAA28275.1; -; mRNA.
EMBL; CR450313; CAG29309.1; -; mRNA.
EMBL; AL445528; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BT006750; AAP35396.1; -; mRNA.
EMBL; BC007039; AAH07039.1; -; mRNA.
EMBL; BC007058; AAH07058.1; -; mRNA.
CCDS; CCDS1186.1; -.
PIR; A25503; YLHUP.
RefSeq; NP_001630.1; NM_001639.3.
UniGene; Hs.507080; -.
PDB; 1GYK; X-ray; 2.20 A; A/B/C/D/E=20-223.
PDB; 1LGN; X-ray; 2.80 A; A/B/C/D/E=20-223.
PDB; 1SAC; X-ray; 2.00 A; A/B/C/D/E=20-223.
PDB; 2A3W; X-ray; 2.20 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=20-223.
PDB; 2A3X; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J=20-223.
PDB; 2A3Y; X-ray; 2.00 A; A/B/C/D/E=20-223.
PDB; 2W08; X-ray; 1.70 A; A/B/C/D/E=20-223.
PDB; 3D5O; X-ray; 2.80 A; A/B/C/D/E=20-223.
PDB; 3KQR; X-ray; 1.50 A; A/B/C/D/E=20-223.
PDB; 4AVS; X-ray; 1.40 A; A/B/C/D/E=20-223.
PDB; 4AVT; X-ray; 3.20 A; A/B/C/D/E/F/G/H/I/J=20-223.
PDB; 4AVV; X-ray; 1.60 A; A/B/C/D/E=20-223.
PDB; 4AYU; X-ray; 1.50 A; A/B/C/D/E=20-223.
PDBsum; 1GYK; -.
PDBsum; 1LGN; -.
PDBsum; 1SAC; -.
PDBsum; 2A3W; -.
PDBsum; 2A3X; -.
PDBsum; 2A3Y; -.
PDBsum; 2W08; -.
PDBsum; 3D5O; -.
PDBsum; 3KQR; -.
PDBsum; 4AVS; -.
PDBsum; 4AVT; -.
PDBsum; 4AVV; -.
PDBsum; 4AYU; -.
ProteinModelPortal; P02743; -.
SMR; P02743; -.
BioGrid; 106822; 13.
DIP; DIP-46911N; -.
IntAct; P02743; 6.
MINT; MINT-4723480; -.
STRING; 9606.ENSP00000255040; -.
ChEMBL; CHEMBL4929; -.
GuidetoPHARMACOLOGY; 2839; -.
TCDB; 1.C.92.1.2; the pentraxin (pentraxin) family.
iPTMnet; P02743; -.
PhosphoSitePlus; P02743; -.
UniCarbKB; P02743; -.
BioMuta; APCS; -.
DMDM; 730704; -.
DOSAC-COBS-2DPAGE; P02743; -.
OGP; P02743; -.
REPRODUCTION-2DPAGE; IPI00022391; -.
REPRODUCTION-2DPAGE; P02743; -.
SWISS-2DPAGE; P02743; -.
PaxDb; P02743; -.
PeptideAtlas; P02743; -.
PRIDE; P02743; -.
DNASU; 325; -.
Ensembl; ENST00000255040; ENSP00000255040; ENSG00000132703.
GeneID; 325; -.
KEGG; hsa:325; -.
CTD; 325; -.
DisGeNET; 325; -.
EuPathDB; HostDB:ENSG00000132703.3; -.
GeneCards; APCS; -.
HGNC; HGNC:584; APCS.
HPA; CAB007817; -.
HPA; HPA053294; -.
MIM; 104770; gene.
neXtProt; NX_P02743; -.
OpenTargets; ENSG00000132703; -.
PharmGKB; PA24877; -.
eggNOG; ENOG410J1FD; Eukaryota.
eggNOG; ENOG410YN8S; LUCA.
GeneTree; ENSGT00760000119128; -.
HOGENOM; HOG000247043; -.
HOVERGEN; HBG005405; -.
InParanoid; P02743; -.
OMA; FTLCFRA; -.
OrthoDB; EOG091G0H6X; -.
PhylomeDB; P02743; -.
TreeFam; TF330208; -.
Reactome; R-HSA-977225; Amyloid fiber formation.
ChiTaRS; APCS; human.
EvolutionaryTrace; P02743; -.
GeneWiki; Serum_amyloid_P_component; -.
GenomeRNAi; 325; -.
PRO; PR:P02743; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000132703; -.
CleanEx; HS_APCS; -.
ExpressionAtlas; P02743; baseline and differential.
Genevisible; P02743; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031012; C:extracellular matrix; IDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; IDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
GO; GO:0001849; F:complement component C1q binding; IDA:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
GO; GO:0046790; F:virion binding; IDA:BHF-UCL.
GO; GO:0006953; P:acute-phase response; TAS:ProtInc.
GO; GO:0044267; P:cellular protein metabolic process; TAS:Reactome.
GO; GO:0051131; P:chaperone-mediated protein complex assembly; TAS:ProtInc.
GO; GO:0045087; P:innate immune response; IDA:BHF-UCL.
GO; GO:0044869; P:negative regulation by host of viral exo-alpha-sialidase activity; IDA:BHF-UCL.
GO; GO:0044871; P:negative regulation by host of viral glycoprotein metabolic process; IDA:BHF-UCL.
GO; GO:0002674; P:negative regulation of acute inflammatory response; IC:BHF-UCL.
GO; GO:1903016; P:negative regulation of exo-alpha-sialidase activity; IDA:BHF-UCL.
GO; GO:1903019; P:negative regulation of glycoprotein metabolic process; IDA:BHF-UCL.
GO; GO:0045656; P:negative regulation of monocyte differentiation; IDA:BHF-UCL.
GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:BHF-UCL.
GO; GO:0048525; P:negative regulation of viral process; IDA:BHF-UCL.
GO; GO:0061045; P:negative regulation of wound healing; IC:BHF-UCL.
GO; GO:0006457; P:protein folding; TAS:ProtInc.
CDD; cd00152; PTX; 1.
InterPro; IPR013320; ConA-like_dom_sf.
InterPro; IPR030476; Pentaxin_CS.
InterPro; IPR001759; Pentraxin-related.
Pfam; PF00354; Pentaxin; 1.
PRINTS; PR00895; PENTAXIN.
SMART; SM00159; PTX; 1.
SUPFAM; SSF49899; SSF49899; 1.
PROSITE; PS00289; PTX_1; 1.
PROSITE; PS51828; PTX_2; 1.
1: Evidence at protein level;
3D-structure; Amyloid; Calcium; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Lectin;
Metal-binding; Polymorphism; Reference proteome; Secreted; Signal.
SIGNAL 1 19 {ECO:0000269|PubMed:4055725,
ECO:0000269|PubMed:81686}.
CHAIN 20 223 Serum amyloid P-component.
/FTId=PRO_0000023540.
CHAIN 20 222 Serum amyloid P-component(1-203).
/FTId=PRO_0000023541.
DOMAIN 24 223 Pentraxin (PTX). {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 77 77 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 78 78 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 155 155 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 155 155 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 156 156 Calcium 1; via carbonyl oxygen.
{ECO:0000255|PROSITE-ProRule:PRU01172}.
METAL 157 157 Calcium 1. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 157 157 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
METAL 167 167 Calcium 2. {ECO:0000255|PROSITE-
ProRule:PRU01172}.
CARBOHYD 51 51 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218}.
/FTId=CAR_000169.
DISULFID 55 114 {ECO:0000255|PROSITE-ProRule:PRU01172,
ECO:0000269|PubMed:4055725}.
VARIANT 141 141 G -> S (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035814.
VARIANT 155 155 E -> G.
/FTId=VAR_006054.
VARIANT 158 158 S -> G.
/FTId=VAR_006055.
CONFLICT 101 101 S -> P (in Ref. 1; AAA60302).
{ECO:0000305}.
STRAND 26 30 {ECO:0000244|PDB:4AVS}.
STRAND 38 41 {ECO:0000244|PDB:4AVS}.
STRAND 49 59 {ECO:0000244|PDB:4AVS}.
STRAND 66 73 {ECO:0000244|PDB:4AVS}.
STRAND 76 86 {ECO:0000244|PDB:4AVS}.
STRAND 89 94 {ECO:0000244|PDB:4AVS}.
STRAND 97 102 {ECO:0000244|PDB:4AVS}.
STRAND 111 118 {ECO:0000244|PDB:4AVS}.
TURN 119 121 {ECO:0000244|PDB:4AVS}.
STRAND 123 128 {ECO:0000244|PDB:4AVS}.
STRAND 149 154 {ECO:0000244|PDB:4AVS}.
STRAND 157 160 {ECO:0000244|PDB:4AVS}.
HELIX 165 167 {ECO:0000244|PDB:4AVS}.
STRAND 171 181 {ECO:0000244|PDB:4AVS}.
HELIX 185 193 {ECO:0000244|PDB:4AVS}.
STRAND 200 203 {ECO:0000244|PDB:4AVS}.
HELIX 204 206 {ECO:0000244|PDB:4AYU}.
STRAND 209 214 {ECO:0000244|PDB:4AVS}.
STRAND 216 219 {ECO:0000244|PDB:4AVS}.
SEQUENCE 223 AA; 25387 MW; 6C88A515FE88B393 CRC64;
MNKPLLWISV LTSLLEAFAH TDLSGKVFVF PRESVTDHVN LITPLEKPLQ NFTLCFRAYS
DLSRAYSLFS YNTQGRDNEL LVYKERVGEY SLYIGRHKVT SKVIEKFPAP VHICVSWESS
SGIAEFWING TPLVKKGLRQ GYFVEAQPKI VLGQEQDSYG GKFDRSQSFV GEIGDLYMWD
SVLPPENILS AYQGTPLPAN ILDWQALNYE IRGYVIIKPL VWV


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E1222m ELISA kit Alpha-synuclein,Mouse,Mus musculus,NACP,Non-A beta component of AD amyloid,Non-A4 component of amyloid precursor,Snca,Syn 96T
10-002-38060 alpha-Synuclein A30P human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38062 alpha-Synuclein 112 human - NACP112; Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38067 alpha-Synuclein E46K human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38059 alpha-Synuclein A53T human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38061 alpha-Synuclein A30P_A53T human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38068 alpha-Synuclein 1-95 (Syn 1-95) human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38066 alpha-Synuclein 1-60 (Syn 1-60) human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-663-45667 alpha-Synuclein Human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 0.1 mg
10-663-45667 alpha-Synuclein Human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38064 alpha-Synuclein 96-140 (Syn 96-140) human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38065 alpha-Synuclein (tri-NAC) human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-002-38063 alpha-Synuclein 61-140 (Syn 61-140) human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 1 mg
10-663-45667 alpha-Synuclein Human - Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP N_A 0.02 mg
U1222h CLIA Alpha-synuclein,Homo sapiens,Human,NACP,NACP,Non-A beta component of AD amyloid,Non-A4 component of amyloid precursor,PARK1,SNCA 96T
E1222h ELISA Alpha-synuclein,Homo sapiens,Human,NACP,NACP,Non-A beta component of AD amyloid,Non-A4 component of amyloid precursor,PARK1,SNCA 96T


 

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