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Complement component C9 [Cleaved into: Complement component C9a; Complement component C9b]

 CO9_HUMAN               Reviewed;         559 AA.
P02748;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
12-SEP-2018, entry version 191.
RecName: Full=Complement component C9;
Contains:
RecName: Full=Complement component C9a;
Contains:
RecName: Full=Complement component C9b;
Flags: Precursor;
Name=C9;
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=4018030;
Stanley K.K., Kocher H.-P., Luzio J.P., Jackson P., Tschopp J.;
"The sequence and topology of human complement component C9.";
EMBO J. 4:375-382(1985).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
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).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 2-559, AND PROTEIN SEQUENCE OF
N-TERMINUS.
PubMed=6095282; DOI=10.1073/pnas.81.23.7298;
Discipio R.G., Gehring M.R., Podack E.R., Kan C.C., Hugli T.E.,
Fey G.H.;
"Nucleotide sequence of cDNA and derived amino acid sequence of human
complement component C9.";
Proc. Natl. Acad. Sci. U.S.A. 81:7298-7302(1984).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-159.
PubMed=3219351; DOI=10.1021/bi00417a050;
Marazziti D., Eggertsen G., Fey G.H., Stanley K.K.;
"Relationships between the gene and protein structure in human
complement component C9.";
Biochemistry 27:6529-6534(1988).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-559, VARIANT C9D GLY-119,
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9634479; DOI=10.1007/s002510050415;
Witzel-Schloemp K., Hobart M.J., Fernie B.A., Orren A., Wuerzner R.,
Rittner C., Kaufmann T., Schneider P.M.;
"Heterogeneity in the genetic basis of human complement C9
deficiency.";
Immunogenetics 48:144-147(1998).
[6]
PARTIAL PROTEIN SEQUENCE, ELECTRON MICROSCOPY, FUNCTION, SUBCELLULAR
LOCATION, PROTEOLYTIC CLEAVAGE, AND GLYCOSYLATION AT ASN-277 AND
ASN-415.
PubMed=4055801;
DiScipio R.G., Hugli T.E.;
"The architecture of complement component C9 and poly(C9).";
J. Biol. Chem. 260:14802-14809(1985).
[7]
DISULFIDE BONDS.
PubMed=8603752; DOI=10.1016/0014-5793(95)01541-8;
Lengweiler S., Schaller J., Rickli E.E.;
"Identification of disulfide bonds in the ninth component (C9) of
human complement.";
FEBS Lett. 380:8-12(1996).
[8]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=9212048; DOI=10.1203/00006450-199707000-00020;
Lassiter H.A., Walz B.M., Wilson J.L., Jung E., Calisi C.R.,
Goldsmith L.J., Wilson R.A., Morgan B.P., Feldhoff R.C.;
"The administration of complement component C9 enhances the survival
of neonatal rats with Escherichia coli sepsis.";
Pediatr. Res. 42:128-136(1997).
[9]
GLYCOSYLATION AT TRP-48 AND TRP-51.
PubMed=10551839; DOI=10.1074/jbc.274.46.32786;
Hofsteenge J., Blommers M., Hess D., Furmanek A., Miroshnichenko O.;
"The four terminal components of the complement system are C-
mannosylated on multiple tryptophan residues.";
J. Biol. Chem. 274:32786-32794(1999).
[10]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-415.
TISSUE=Plasma;
PubMed=14760718; DOI=10.1002/pmic.200300556;
Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.;
"Screening for N-glycosylated proteins by liquid chromatography mass
spectrometry.";
Proteomics 4:454-465(2004).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-277 AND ASN-415.
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-415.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[13]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-277 AND ASN-415.
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).
[14]
GLYCOSYLATION AT ASN-415.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[15]
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).
[16]
3D-STRUCTURE MODELING OF MEMBRANE-SPANNING DOMAIN (MSB).
PubMed=2395434; DOI=10.1016/0161-5890(90)90001-G;
Peitsch M.C., Amiguet P., Guy R., Brunner J., Maizel J.V. Jr.,
Tschopp J.;
"Localization and molecular modelling of the membrane-inserted domain
of the ninth component of human complement and perforin.";
Mol. Immunol. 27:589-602(1990).
[17]
ELECTRON MICROSCOPY, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=22832194; DOI=10.1016/j.celrep.2012.02.003;
Hadders M.A., Bubeck D., Roversi P., Hakobyan S., Forneris F.,
Morgan B.P., Pangburn M.K., Llorca O., Lea S.M., Gros P.;
"Assembly and regulation of the membrane attack complex based on
structures of C5b6 and sC5b9.";
Cell Rep. 1:200-207(2012).
[18]
STRUCTURE BY ELECTRON MICROSCOPY (6.70 ANGSTROMS) OF 39-544, FUNCTION,
SUBUNIT, AND SUBCELLULAR LOCATION.
PubMed=26841934; DOI=10.1038/ncomms10588;
Dudkina N.V., Spicer B.A., Reboul C.F., Conroy P.J., Lukoyanova N.,
Elmlund H., Law R.H., Ekkel S.M., Kondos S.C., Goode R.J., Ramm G.,
Whisstock J.C., Saibil H.R., Dunstone M.A.;
"Structure of the poly-C9 component of the complement membrane attack
complex.";
Nat. Commun. 7:10588-10588(2016).
[19]
VARIANT ARMD15 SER-167.
PubMed=24036952; DOI=10.1038/ng.2741;
Seddon J.M., Yu Y., Miller E.C., Reynolds R., Tan P.L.,
Gowrisankar S., Goldstein J.I., Triebwasser M., Anderson H.E.,
Zerbib J., Kavanagh D., Souied E., Katsanis N., Daly M.J.,
Atkinson J.P., Raychaudhuri S.;
"Rare variants in CFI, C3 and C9 are associated with high risk of
advanced age-related macular degeneration.";
Nat. Genet. 45:1366-1370(2013).
-!- FUNCTION: Constituent of the membrane attack complex (MAC) that
plays a key role in the innate and adaptive immune response by
forming pores in the plasma membrane of target cells
(PubMed:9634479, PubMed:9212048, PubMed:26841934). C9 is the pore-
forming subunit of the MAC (PubMed:4055801, PubMed:26841934).
{ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:4055801,
ECO:0000269|PubMed:9212048, ECO:0000269|PubMed:9634479}.
-!- SUBUNIT: Component of the membrane attack complex (MAC). MAC
assembly is initiated by proteolytic cleavage of C5 into C5a and
C5b. C5b binds sequentially C6, C7, C8 and multiple copies of the
pore-forming subunit C9 (PubMed:22832194). About 20 C9 chains
oligomerize to give rise to a huge beta-barrel that forms a 100
Angstrom diameter pore in target membranes (PubMed:26841934).
{ECO:0000269|PubMed:22832194, ECO:0000269|PubMed:26841934}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22832194,
ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:9212048,
ECO:0000269|PubMed:9634479}. Target cell membrane
{ECO:0000269|PubMed:26841934, ECO:0000269|PubMed:9212048}; Multi-
pass membrane protein {ECO:0000269|PubMed:26841934}. Note=Secreted
as soluble monomer. Oligomerizes at target membranes, forming a
pre-pore. A conformation change then leads to the formation of a
100 Angstrom diameter pore. {ECO:0000269|PubMed:26841934,
ECO:0000269|PubMed:4055801, ECO:0000269|PubMed:9634479}.
-!- TISSUE SPECIFICITY: Plasma (at protein level).
{ECO:0000269|PubMed:22832194, ECO:0000269|PubMed:26841934,
ECO:0000269|PubMed:9212048, ECO:0000269|PubMed:9634479}.
-!- PTM: Thrombin cleaves factor C9 to produce C9a and C9b.
{ECO:0000269|PubMed:4055801}.
-!- PTM: Phosphorylation sites are present in the extracellular
medium.
-!- DISEASE: Complement component 9 deficiency (C9D) [MIM:613825]: A
rare defect of the complement classical pathway associated with
susceptibility to severe recurrent infections predominantly by
Neisseria gonorrhoeae or Neisseria meningitidis. Some patients may
develop dermatomyositis. {ECO:0000269|PubMed:9634479}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Macular degeneration, age-related, 15 (ARMD15)
[MIM:615591]: A form of age-related macular degeneration, a
multifactorial eye disease and the most common cause of
irreversible vision loss in the developed world. In most patients,
the disease is manifest as ophthalmoscopically visible yellowish
accumulations of protein and lipid that lie beneath the retinal
pigment epithelium and within an elastin-containing structure
known as Bruch membrane. {ECO:0000269|PubMed:24036952}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the complement C6/C7/C8/C9 family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=C9base; Note=C9 mutation db;
URL="http://structure.bmc.lu.se/idbase/C9base/";
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EMBL; X02176; CAA26117.1; -; mRNA.
EMBL; BC020721; AAH20721.1; -; mRNA.
EMBL; K02766; AAA51889.1; -; mRNA.
EMBL; J02833; AAA51890.1; -; Genomic_DNA.
EMBL; Y08545; CAA69849.1; -; Genomic_DNA.
EMBL; Y08546; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08547; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08548; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08549; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08550; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08551; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08552; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08553; CAA69849.1; JOINED; Genomic_DNA.
EMBL; Y08554; CAA69849.1; JOINED; Genomic_DNA.
CCDS; CCDS3929.1; -.
PIR; A59363; C9HU.
RefSeq; NP_001728.1; NM_001737.4.
UniGene; Hs.654443; -.
PDB; 5FMW; EM; 6.70 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V=39-544.
PDBsum; 5FMW; -.
ProteinModelPortal; P02748; -.
SMR; P02748; -.
BioGrid; 107196; 6.
DIP; DIP-1124N; -.
ELM; P02748; -.
STRING; 9606.ENSP00000263408; -.
iPTMnet; P02748; -.
PhosphoSitePlus; P02748; -.
BioMuta; C9; -.
DMDM; 1352108; -.
MaxQB; P02748; -.
PaxDb; P02748; -.
PeptideAtlas; P02748; -.
PRIDE; P02748; -.
ProteomicsDB; 51564; -.
DNASU; 735; -.
Ensembl; ENST00000263408; ENSP00000263408; ENSG00000113600.
GeneID; 735; -.
KEGG; hsa:735; -.
UCSC; uc003jlv.5; human.
CTD; 735; -.
DisGeNET; 735; -.
EuPathDB; HostDB:ENSG00000113600.10; -.
GeneCards; C9; -.
HGNC; HGNC:1358; C9.
HPA; CAB002151; -.
HPA; HPA029577; -.
MalaCards; C9; -.
MIM; 120940; gene.
MIM; 613825; phenotype.
MIM; 615591; phenotype.
neXtProt; NX_P02748; -.
OpenTargets; ENSG00000113600; -.
Orphanet; 279; Age-related macular degeneration.
Orphanet; 169150; Immunodeficiency due to a late component of complements deficiency.
PharmGKB; PA25968; -.
eggNOG; ENOG410IH3C; Eukaryota.
eggNOG; ENOG410XT9A; LUCA.
GeneTree; ENSGT00550000074478; -.
HOGENOM; HOG000111869; -.
HOVERGEN; HBG106792; -.
InParanoid; P02748; -.
KO; K04000; -.
OMA; GINILGM; -.
OrthoDB; EOG091G07LK; -.
PhylomeDB; P02748; -.
TreeFam; TF330498; -.
Reactome; R-HSA-166665; Terminal pathway of complement.
Reactome; R-HSA-977606; Regulation of Complement cascade.
ChiTaRS; C9; human.
GenomeRNAi; 735; -.
PRO; PR:P02748; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113600; Expressed in 60 organ(s), highest expression level in liver.
CleanEx; HS_C9; -.
Genevisible; P02748; HS.
GO; GO:0072562; C:blood microparticle; HDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB.
GO; GO:0044218; C:other organism cell membrane; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0001906; P:cell killing; IDA:UniProtKB.
GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0019836; P:hemolysis by symbiont of host erythrocytes; TAS:ProtInc.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
CDD; cd00112; LDLa; 1.
Gene3D; 2.20.100.10; -; 1.
InterPro; IPR037567; Complement_C9.
InterPro; IPR009030; Growth_fac_rcpt_cys_sf.
InterPro; IPR036055; LDL_receptor-like_sf.
InterPro; IPR023415; LDLR_class-A_CS.
InterPro; IPR002172; LDrepeatLR_classA_rpt.
InterPro; IPR001862; MAC_perforin.
InterPro; IPR020864; MACPF.
InterPro; IPR020863; MACPF_CS.
InterPro; IPR000884; TSP1_rpt.
InterPro; IPR036383; TSP1_rpt_sf.
PANTHER; PTHR19325:SF362; PTHR19325:SF362; 1.
Pfam; PF00057; Ldl_recept_a; 1.
Pfam; PF01823; MACPF; 1.
Pfam; PF00090; TSP_1; 1.
PRINTS; PR00764; COMPLEMENTC9.
SMART; SM00192; LDLa; 1.
SMART; SM00457; MACPF; 1.
SMART; SM00209; TSP1; 1.
SUPFAM; SSF57184; SSF57184; 2.
SUPFAM; SSF57424; SSF57424; 1.
SUPFAM; SSF82895; SSF82895; 1.
PROSITE; PS00022; EGF_1; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS01209; LDLRA_1; 1.
PROSITE; PS50068; LDLRA_2; 1.
PROSITE; PS00279; MACPF_1; 1.
PROSITE; PS51412; MACPF_2; 1.
PROSITE; PS50092; TSP1; 1.
1: Evidence at protein level;
3D-structure; Age-related macular degeneration;
Complement alternate pathway; Complement pathway; Complete proteome;
Cytolysis; Direct protein sequencing; Disease mutation;
Disulfide bond; EGF-like domain; Glycoprotein; Immunity;
Innate immunity; Membrane; Membrane attack complex; Phosphoprotein;
Polymorphism; Reference proteome; Secreted; Signal;
Target cell membrane; Target membrane; Transmembrane;
Transmembrane beta strand.
SIGNAL 1 21 {ECO:0000269|PubMed:6095282}.
CHAIN 22 559 Complement component C9.
/FTId=PRO_0000023602.
CHAIN 22 265 Complement component C9a.
/FTId=PRO_0000023603.
CHAIN 266 559 Complement component C9b.
/FTId=PRO_0000023604.
TRANSMEM 314 330 Beta stranded. {ECO:0000255}.
TRANSMEM 335 354 Beta stranded. {ECO:0000255}.
DOMAIN 42 95 TSP type-1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 99 136 LDL-receptor class A.
{ECO:0000255|PROSITE-ProRule:PRU00124}.
DOMAIN 138 509 MACPF. {ECO:0000255|PROSITE-
ProRule:PRU00745}.
DOMAIN 510 540 EGF-like.
SITE 265 266 Cleavage; by thrombin.
CARBOHYD 48 48 C-linked (Man) tryptophan.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 51 51 C-linked (Man) tryptophan; partial.
{ECO:0000269|PubMed:10551839}.
CARBOHYD 277 277 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:4055801}.
CARBOHYD 415 415 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:14760718,
ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:4055801}.
DISULFID 43 78 {ECO:0000269|PubMed:8603752}.
DISULFID 54 57 {ECO:0000269|PubMed:8603752}.
DISULFID 88 94 {ECO:0000269|PubMed:8603752}.
DISULFID 101 112 {ECO:0000269|PubMed:8603752}.
DISULFID 107 125 {ECO:0000269|PubMed:8603752}.
DISULFID 119 134 {ECO:0000269|PubMed:8603752}.
DISULFID 142 181 {ECO:0000269|PubMed:8603752}.
DISULFID 254 255 {ECO:0000269|PubMed:8603752}.
DISULFID 380 405 {ECO:0000269|PubMed:8603752}.
DISULFID 510 526 {ECO:0000269|PubMed:8603752}.
DISULFID 513 528 {ECO:0000269|PubMed:8603752}.
DISULFID 530 539 {ECO:0000269|PubMed:8603752}.
VARIANT 5 5 R -> W (in dbSNP:rs700233).
/FTId=VAR_022024.
VARIANT 119 119 C -> G (in C9D; dbSNP:rs121909593).
{ECO:0000269|PubMed:9634479}.
/FTId=VAR_012648.
VARIANT 127 127 D -> Y (in dbSNP:rs696763).
/FTId=VAR_050481.
VARIANT 167 167 P -> S (in ARMD15; dbSNP:rs34882957).
{ECO:0000269|PubMed:24036952}.
/FTId=VAR_070940.
VARIANT 203 203 I -> V (in dbSNP:rs13361416).
/FTId=VAR_027651.
VARIANT 279 279 T -> S (in dbSNP:rs34625111).
/FTId=VAR_033802.
VARIANT 427 427 S -> T (in dbSNP:rs34421659).
/FTId=VAR_061503.
CONFLICT 43 43 C -> R (in Ref. 3; AAA51889).
{ECO:0000305}.
CONFLICT 314 314 Missing (in Ref. 3; AAA51889).
{ECO:0000305}.
CONFLICT 417 417 T -> P (in Ref. 3; AAA51889).
{ECO:0000305}.
SEQUENCE 559 AA; 63173 MW; 7403F6AD77B3ECE1 CRC64;
MSACRSFAVA ICILEISILT AQYTTSYDPE LTESSGSASH IDCRMSPWSE WSQCDPCLRQ
MFRSRSIEVF GQFNGKRCTD AVGDRRQCVP TEPCEDAEDD CGNDFQCSTG RCIKMRLRCN
GDNDCGDFSD EDDCESEPRP PCRDRVVEES ELARTAGYGI NILGMDPLST PFDNEFYNGL
CNRDRDGNTL TYYRRPWNVA SLIYETKGEK NFRTEHYEEQ IEAFKSIIQE KTSNFNAAIS
LKFTPTETNK AEQCCEETAS SISLHGKGSF RFSYSKNETY QLFLSYSSKK EKMFLHVKGE
IHLGRFVMRN RDVVLTTTFV DDIKALPTTY EKGEYFAFLE TYGTHYSSSG SLGGLYELIY
VLDKASMKRK GVELKDIKRC LGYHLDVSLA FSEISVGAEF NKDDCVKRGE GRAVNITSEN
LIDDVVSLIR GGTRKYAFEL KEKLLRGTVI DVTDFVNWAS SINDAPVLIS QKLSPIYNLV
PVKMKNAHLK KQNLERAIED YINEFSVRKC HTCQNGGTVI LMDGKCLCAC PFKFEGIACE
ISKQKISEGL PALEFPNEK


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EIAAB08423 C8b,Complement component 8 subunit beta,Complement component C8 beta chain,Mouse,Mus musculus
EIAAB08422 C8b,Complement component 8 subunit beta,Complement component C8 beta chain,Rat,Rattus norvegicus
orb81042 Human Complement Component C1q protein Human Complement Component C1q produced in Human plasma having a molecular mass of 410 kDa. For research use only. 200
orb21968 Goat Serum Against Human C5 Polyclonal Precipitating polyclonal goat antiserum to the C5 component of human complement. C5 component of human complement is a plasma protein consisting of two polypepti 1 ml
orb21929 Goat Serum Against Human C1Q Polyclonal Precipitating polyclonal goat antiserum to C1q fragment ofC1 component of human complement. C1 component of human complement is a complex of three glycoproteins 1 ml
orb21957 Goat Serum Against Human C1R Polyclonal Precipitating polyclonal goat antiserum to the C1r subunit of C1 component of human complement. C1 component of human complement is a complex of three glycoprot 1 ml
orb21958 Goat Serum Against Human C1S Polyclonal Precipitating polyclonal goat antiserum to the C1s subunit of C1 component of human complement. C1 component of human complement is a complex of three glycoprot 1 ml
20-783-74967 MOUSE ANTI HUMAN C4c - COMPLEMENT COMPONENT 4c; Basic complement C4 Monoclonal 0.1 mg
Y104639 Complement C4, Complement Component, Human Antibody 1 ml
29-980 C1QB is a major constituent of the human complement subcomponent C1q. C1q associates with C1r and C1s in order to yield the first component of the serum complement system. Deficiency of C1q has been a 0.05 mg
Y104639 Complement C4, Complement Component, Human 1 ml


 

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