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Complement C5 (C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4) [Cleaved into: Complement C5 beta chain; Complement C5 alpha chain; C5a anaphylatoxin; Complement C5 alpha' chain]

 CO5_HUMAN               Reviewed;        1676 AA.
P01031; Q14CJ0; Q27I61;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
05-FEB-2008, sequence version 4.
05-DEC-2018, entry version 212.
RecName: Full=Complement C5;
AltName: Full=C3 and PZP-like alpha-2-macroglobulin domain-containing protein 4;
Contains:
RecName: Full=Complement C5 beta chain;
Contains:
RecName: Full=Complement C5 alpha chain;
Contains:
RecName: Full=C5a anaphylatoxin;
Contains:
RecName: Full=Complement C5 alpha' chain;
Flags: Precursor;
Name=C5; Synonyms=CPAMD4;
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 VARIANTS ILE-389 AND ILE-802.
PubMed=1984448;
Haviland D.L., Haviland J.C., Fleischer D.T., Hunt A., Wetsel R.A.;
"Complete cDNA sequence of human complement pro-C5. Evidence of
truncated transcripts derived from a single copy gene.";
J. Immunol. 146:362-368(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-145; GLY-449;
ILE-802; GLN-928; VAL-933; THR-1033; ASN-1037; LYS-1043; ASN-1310 AND
ASP-1437.
SeattleSNPs variation discovery resource;
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-802.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-802.
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 412-1676, AND VARIANT ILE-802.
PubMed=3365401; DOI=10.1021/bi00405a012;
Wetsel R.A., Lemons R.S., Lebeau M.M., Barnum S.R., Noack D.,
Tack B.F.;
"Molecular analysis of human complement component C5: localization of
the structural gene to chromosome 9.";
Biochemistry 27:1474-1482(1988).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 412-1676, AND VARIANT ILE-802.
PubMed=2579066;
Lundwall A.B., Wetsel R.A., Kristensen T., Whitehead A.S., Woods D.E.,
Ogden R.C., Colten H.R., Tack B.F.;
"Isolation and sequence analysis of a cDNA clone encoding the fifth
complement component.";
J. Biol. Chem. 260:2108-2112(1985).
[7]
PROTEIN SEQUENCE OF 678-751.
PubMed=690134;
Fernandez H.N., Hugli T.E.;
"Primary structural analysis of the polypeptide portion of human C5a
anaphylatoxin. Polypeptide sequence determination and assignment of
the oligosaccharide attachment site in C5a.";
J. Biol. Chem. 253:6955-6964(1978).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 678-751.
PubMed=1996961; DOI=10.1042/bj2730635;
Bohnsack J.F., Mollison K.W., Buko A.M., Ashworth J.C., Hill H.R.;
"Group B streptococci inactivate complement component C5a by enzymic
cleavage at the C-terminus.";
Biochem. J. 273:635-640(1991).
[9]
FUNCTION, AND INTERACTION WITH C5AR1.
PubMed=8182049;
DeMartino J.A., Van Riper G., Siciliano S.J., Molineaux C.J.,
Konteatis Z.D., Rosen H., Springer M.S.;
"The amino terminus of the human C5a receptor is required for high
affinity C5a binding and for receptor activation by C5a but not C5a
analogs.";
J. Biol. Chem. 269:14446-14450(1994).
[10]
INTERACTION WITH C5AR1.
PubMed=9553099; DOI=10.1074/jbc.273.17.10411;
Chen Z., Zhang X., Gonnella N.C., Pellas T.C., Boyar W.C., Ni F.;
"Residues 21-30 within the extracellular N-terminal region of the C5a
receptor represent a binding domain for the C5a anaphylatoxin.";
J. Biol. Chem. 273:10411-10419(1998).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-741; ASN-911 AND ASN-1630.
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]
STRUCTURE BY NMR OF C5A.
PubMed=3408713; DOI=10.1021/bi00410a007;
Zuiderweg E.R.P., Mollison K.W., Henkin J., Carter G.W.;
"Sequence-specific assignments in the 1H NMR spectrum of the human
inflammatory protein C5a.";
Biochemistry 27:3568-3580(1988).
[13]
STRUCTURE BY NMR OF C5A.
PubMed=2784981; DOI=10.1021/bi00427a025;
Zuiderweg E.R.P., Nettesheim D.G., Mollison K.W., Carter G.W.;
"Tertiary structure of human complement component C5a in solution from
nuclear magnetic resonance data.";
Biochemistry 28:172-185(1989).
[14]
STRUCTURE BY NMR OF C5A.
PubMed=2730871; DOI=10.1021/bi00432a008;
Zuiderweg E.R.P., Fesik S.W.;
"Heteronuclear three-dimensional NMR spectroscopy of the inflammatory
protein C5a.";
Biochemistry 28:2387-2391(1989).
[15]
STRUCTURE BY NMR OF 679-747 OF C5A, AND DISULFIDE BONDS.
PubMed=9007977; DOI=10.1002/pro.5560060107;
Zhang X., Boyar W., Galakatos N., Gonnella N.C.;
"Solution structure of a unique C5a semi-synthetic antagonist:
implications in receptor binding.";
Protein Sci. 6:65-72(1997).
[16]
STRUCTURE BY NMR OF 679-751 OF C5A, AND DISULFIDE BONDS.
PubMed=9188742;
DOI=10.1002/(SICI)1097-0134(199706)28:2<261::AID-PROT13>3.0.CO;2-G;
Zhang X., Boyar W., Toth M.J., Wennogle L., Gonnella N.C.;
"Structural definition of the C5a C-terminus by two-dimensional
nuclear magnetic resonance spectroscopy.";
Proteins 28:261-267(1997).
[17]
INVOLVEMENT IN COMPLEMENT C5 DEFICIENCY.
PubMed=7730648;
Wang X., Fleischer D.T., Whitehead W.T., Haviland D.L.,
Rosenfeld S.I., Leddy J.P., Snyderman R., Wetsel R.A.;
"Inherited human complement C5 deficiency. Nonsense mutations in exons
1 (Gln1 to Stop) and 36 (Arg1458 to Stop) and compound heterozygosity
in three African-American families.";
J. Immunol. 154:5464-5471(1995).
[18]
INVOLVEMENT IN COMPLEMENT C5 DEFICIENCY.
PubMed=15778377; DOI=10.4049/jimmunol.174.7.4172;
Pfarr N., Prawitt D., Kirschfink M., Schroff C., Knuf M.,
Habermehl P., Mannhardt W., Zepp F., Fairbrother W., Loos M.,
Burge C.B., Pohlenz J.;
"Linking C5 deficiency to an exonic splicing enhancer mutation.";
J. Immunol. 174:4172-4177(2005).
[19]
INVOLVEMENT IN COMPLEMENT C5 DEFICIENCY, AND VARIANTS ILE-389 AND
ILE-802.
PubMed=15488949; DOI=10.1016/S0161-5890(04)00255-X;
Delgado-Cervino E., Fontan G., Lopez-Trascasa M.;
"C5 complement deficiency in a Spanish family. Molecular
characterization of the double mutation responsible for the defect.";
Mol. Immunol. 42:105-111(2005).
[20]
ASSOCIATION WITH SUSCEPTIBILITY TO LIVER FIBROSIS.
PubMed=15995705; DOI=10.1038/ng1599;
Hillebrandt S., Wasmuth H.E., Weiskirchen R., Hellerbrand C.,
Keppeler H., Werth A., Schirin-Sokhan R., Wilkens G., Geier A.,
Lorenzen J., Koehl J., Gressner A.M., Matern S., Lammert F.;
"Complement factor 5 is a quantitative trait gene that modifies liver
fibrogenesis in mice and humans.";
Nat. Genet. 37:835-843(2005).
[21]
STRUCTURE BY NMR OF 1530-1676, AND DISULFIDE BONDS.
PubMed=15598652; DOI=10.1074/jbc.M413126200;
Bramham J., Thai C.-T., Soares D.C., Uhrin D., Ogata R.T.,
Barlow P.N.;
"Functional insights from the structure of the multifunctional C345C
domain of C5 of complement.";
J. Biol. Chem. 280:10636-10645(2005).
[22]
X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS), INTERACTION WITH TICK
COMPLEMENT INHIBITOR, GLYCOSYLATION AT ASN-741 AND ASN-911, AND
DISULFIDE BONDS.
PubMed=18536718; DOI=10.1038/ni.1625;
Fredslund F., Laursen N.S., Roversi P., Jenner L., Oliveira C.L.P.,
Pedersen J.S., Nunn M.A., Lea S.M., Discipio R., Sottrup-Jensen L.,
Andersen G.R.;
"Structure of and influence of a tick complement inhibitor on human
complement component 5.";
Nat. Immunol. 9:753-760(2008).
[23]
X-RAY CRYSTALLOGRAPHY (4.30 ANGSTROMS) OF 20-1676 IN COMPLEX WITH
COBRA VENOM FACTOR, GLYCOSYLATION AT ASN-911, AND DISULFIDE BONDS.
PubMed=21217642; DOI=10.1038/emboj.2010.341;
Laursen N.S., Andersen K.R., Braren I., Spillner E.,
Sottrup-Jensen L., Andersen G.R.;
"Substrate recognition by complement convertases revealed in the C5-
cobra venom factor complex.";
EMBO J. 30:606-616(2011).
[24]
VARIANT TYR-966, AND IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22028381; DOI=10.1093/jmcb/mjr024;
Su Z.D., Sun L., Yu D.X., Li R.X., Li H.X., Yu Z.J., Sheng Q.H.,
Lin X., Zeng R., Wu J.R.;
"Quantitative detection of single amino acid polymorphisms by targeted
proteomics.";
J. Mol. Cell Biol. 3:309-315(2011).
[25]
VARIANTS CYS-885 AND HIS-885, AND INVOLVEMENT IN POOR RESPONSE TO
ECULIZUMAB.
PubMed=24521109; DOI=10.1056/NEJMoa1311084;
Nishimura J., Yamamoto M., Hayashi S., Ohyashiki K., Ando K.,
Brodsky A.L., Noji H., Kitamura K., Eto T., Takahashi T., Masuko M.,
Matsumoto T., Wano Y., Shichishima T., Shibayama H., Hase M., Li L.,
Johnson K., Lazarowski A., Tamburini P., Inazawa J., Kinoshita T.,
Kanakura Y.;
"Genetic variants in C5 and poor response to eculizumab.";
N. Engl. J. Med. 370:632-639(2014).
-!- FUNCTION: Activation of C5 by a C5 convertase initiates the
spontaneous assembly of the late complement components, C5-C9,
into the membrane attack complex. C5b has a transient binding site
for C6. The C5b-C6 complex is the foundation upon which the lytic
complex is assembled.
-!- FUNCTION: Derived from proteolytic degradation of complement C5,
C5 anaphylatoxin is a mediator of local inflammatory process.
Binding to the receptor C5AR1 induces a variety of responses
including intracellular calcium release, contraction of smooth
muscle, increased vascular permeability, and histamine release
from mast cells and basophilic leukocytes (PubMed:8182049). C5a is
also a potent chemokine which stimulates the locomotion of
polymorphonuclear leukocytes and directs their migration toward
sites of inflammation. {ECO:0000269|PubMed:8182049}.
-!- SUBUNIT: C5 precursor is first processed by the removal of 4 basic
residues, forming two chains, beta and alpha, linked by a
disulfide bond. C5 convertase activates C5 by cleaving the alpha
chain, releasing C5a anaphylatoxin and generating C5b (beta chain
+ alpha' chain). The C5a anaphylatoxin interacts with C5AR1.
Interacts with tick complement inhibitor.
{ECO:0000269|PubMed:18536718, ECO:0000269|PubMed:21217642,
ECO:0000269|PubMed:8182049, ECO:0000269|PubMed:9553099}.
-!- INTERACTION:
Q91132:- (xeno); NbExp=2; IntAct=EBI-8558308, EBI-7081824;
Q96BA8:CREB3L1; NbExp=3; IntAct=EBI-8558308, EBI-6942903;
-!- SUBCELLULAR LOCATION: Secreted.
-!- POLYMORPHISM: C5 variants are responsible for poor response to
eculizumab [MIM:615749]. Eculizumab is a monoclonal antibody
highly effective in reducing intravascular hemolysis in patients
with paroxysmal nocturnal hemoglobinuria. It specifically binds to
the terminal complement protein C5, inhibits its cleavage into C5a
and C5b, and prevents the formations of the cytolytic complement
pore (PubMed:24521109). {ECO:0000269|PubMed:24521109}.
-!- DISEASE: Complement component 5 deficiency (C5D) [MIM:609536]: A
rare defect of the complement classical pathway associated with
susceptibility to severe recurrent infections, predominantly by
Neisseria gonorrhoeae or Neisseria meningitidis. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Note=An association study of C5 haplotypes and genotypes
in individuals with chronic hepatitis C virus infection shows that
individuals homozygous for the C5_1 haplotype have a significantly
higher stage of liver fibrosis than individuals carrying at least
1 other allele. {ECO:0000269|PubMed:15995705}.
-!- WEB RESOURCE: Name=C5base; Note=C5 mutation db;
URL="http://structure.bmc.lu.se/idbase/C5base/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Complement C5 entry;
URL="https://en.wikipedia.org/wiki/Complement_component_5";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/c5/";
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EMBL; M57729; AAA51925.1; -; mRNA.
EMBL; DQ400449; ABD48959.1; -; Genomic_DNA.
EMBL; CH471090; EAW87480.1; -; Genomic_DNA.
EMBL; BC113738; AAI13739.1; -; mRNA.
EMBL; BC113740; AAI13741.1; -; mRNA.
EMBL; M65134; AAA51856.1; -; mRNA.
CCDS; CCDS6826.1; -.
PIR; A40075; C5HU.
RefSeq; NP_001304092.1; NM_001317163.1.
RefSeq; NP_001726.2; NM_001735.2.
UniGene; Hs.494997; -.
PDB; 1CFA; NMR; -; A=679-747.
PDB; 1KJS; NMR; -; A=679-751.
PDB; 1XWE; NMR; -; A=1530-1676.
PDB; 3CU7; X-ray; 3.10 A; A/B=1-1676.
PDB; 3HQA; X-ray; 2.59 A; A/B=679-750.
PDB; 3HQB; X-ray; 3.30 A; A/B=679-750.
PDB; 3KLS; X-ray; 3.60 A; A/B=1-1676.
PDB; 3KM9; X-ray; 4.20 A; A/B=1-1676.
PDB; 3PRX; X-ray; 4.30 A; A/C=1-1676.
PDB; 3PVM; X-ray; 4.30 A; A/C=1-1676.
PDB; 4A5W; X-ray; 3.50 A; A=19-1676.
PDB; 4E0S; X-ray; 4.21 A; A=1-1676.
PDB; 4P39; X-ray; 2.40 A; A/B/C/D=678-747.
PDB; 4UU9; X-ray; 2.12 A; C/D=678-751.
PDB; 5B4P; X-ray; 2.40 A; B/D=678-751.
PDB; 5B71; X-ray; 2.11 A; E/F=20-124.
PDB; 5HCC; X-ray; 2.59 A; A=679-1676, B=19-674.
PDB; 5HCD; X-ray; 2.98 A; A=679-1676, B=19-674.
PDB; 5HCE; X-ray; 3.12 A; A=679-1676, B=19-674.
PDB; 5I5K; X-ray; 4.20 A; A/B=1-1676.
PDBsum; 1CFA; -.
PDBsum; 1KJS; -.
PDBsum; 1XWE; -.
PDBsum; 3CU7; -.
PDBsum; 3HQA; -.
PDBsum; 3HQB; -.
PDBsum; 3KLS; -.
PDBsum; 3KM9; -.
PDBsum; 3PRX; -.
PDBsum; 3PVM; -.
PDBsum; 4A5W; -.
PDBsum; 4E0S; -.
PDBsum; 4P39; -.
PDBsum; 4UU9; -.
PDBsum; 5B4P; -.
PDBsum; 5B71; -.
PDBsum; 5HCC; -.
PDBsum; 5HCD; -.
PDBsum; 5HCE; -.
PDBsum; 5I5K; -.
ProteinModelPortal; P01031; -.
SMR; P01031; -.
BioGrid; 107188; 8.
IntAct; P01031; 11.
MINT; P01031; -.
STRING; 9606.ENSP00000223642; -.
ChEMBL; CHEMBL2364163; -.
DrugBank; DB01257; Eculizumab.
DrugBank; DB00028; Immune Globulin Human.
MEROPS; I39.952; -.
CarbonylDB; P01031; -.
GlyConnect; 1147; -.
iPTMnet; P01031; -.
PhosphoSitePlus; P01031; -.
BioMuta; C5; -.
DMDM; 166900096; -.
EPD; P01031; -.
MaxQB; P01031; -.
PaxDb; P01031; -.
PeptideAtlas; P01031; -.
PRIDE; P01031; -.
ProteomicsDB; 12624; -.
ProteomicsDB; 51309; -.
Ensembl; ENST00000223642; ENSP00000223642; ENSG00000106804.
GeneID; 727; -.
KEGG; hsa:727; -.
UCSC; uc004bkv.4; human.
CTD; 727; -.
DisGeNET; 727; -.
EuPathDB; HostDB:ENSG00000106804.7; -.
GeneCards; C5; -.
H-InvDB; HIX0025739; -.
HGNC; HGNC:1331; C5.
HPA; HPA029339; -.
MalaCards; C5; -.
MIM; 120900; gene.
MIM; 609536; phenotype.
MIM; 615749; phenotype.
neXtProt; NX_P01031; -.
OpenTargets; ENSG00000106804; -.
Orphanet; 169150; Immunodeficiency due to a late component of complement deficiency.
PharmGKB; PA25911; -.
eggNOG; KOG1366; Eukaryota.
eggNOG; ENOG410XRED; LUCA.
GeneTree; ENSGT00940000155670; -.
HOGENOM; HOG000231860; -.
HOVERGEN; HBG098067; -.
InParanoid; P01031; -.
KO; K03994; -.
OMA; YVFHYLE; -.
OrthoDB; EOG091G00BU; -.
PhylomeDB; P01031; -.
TreeFam; TF313285; -.
BRENDA; 3.4.21.43; 2681.
Reactome; R-HSA-166665; Terminal pathway of complement.
Reactome; R-HSA-174577; Activation of C3 and C5.
Reactome; R-HSA-375276; Peptide ligand-binding receptors.
Reactome; R-HSA-418594; G alpha (i) signalling events.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SIGNOR; P01031; -.
EvolutionaryTrace; P01031; -.
GeneWiki; Complement_component_5; -.
GenomeRNAi; 727; -.
PMAP-CutDB; P01031; -.
PRO; PR:P01031; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000106804; Expressed in 179 organ(s), highest expression level in liver.
CleanEx; HS_C5; -.
Genevisible; P01031; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0005579; C:membrane attack complex; IDA:UniProtKB.
GO; GO:0008009; F:chemokine activity; TAS:ProtInc.
GO; GO:0004866; F:endopeptidase inhibitor activity; IEA:InterPro.
GO; GO:0005102; F:signaling receptor binding; TAS:ProtInc.
GO; GO:0000187; P:activation of MAPK activity; TAS:ProtInc.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
GO; GO:0006957; P:complement activation, alternative pathway; IEA:UniProtKB-KW.
GO; GO:0006958; P:complement activation, classical pathway; IEA:UniProtKB-KW.
GO; GO:0019835; P:cytolysis; IEA:UniProtKB-KW.
GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:Reactome.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
GO; GO:0010760; P:negative regulation of macrophage chemotaxis; IDA:BHF-UCL.
GO; GO:0045766; P:positive regulation of angiogenesis; IEA:Ensembl.
GO; GO:0090197; P:positive regulation of chemokine secretion; IDA:BHF-UCL.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IDA:BHF-UCL.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
CDD; cd00017; ANATO; 1.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 2.60.40.690; -; 1.
InterPro; IPR009048; A-macroglobulin_rcpt-bd.
InterPro; IPR036595; A-macroglobulin_rcpt-bd_sf.
InterPro; IPR011625; A2M_N_BRD.
InterPro; IPR011626; Alpha-macroglobulin_TED.
InterPro; IPR000020; Anaphylatoxin/fibulin.
InterPro; IPR018081; Anaphylatoxin_comp_syst.
InterPro; IPR001840; Anaphylatoxn_comp_syst_dom.
InterPro; IPR037562; Complement_C5.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR001599; Macroglobln_a2.
InterPro; IPR002890; MG2.
InterPro; IPR001134; Netrin_domain.
InterPro; IPR018933; Netrin_module_non-TIMP.
InterPro; IPR008930; Terpenoid_cyclase/PrenylTrfase.
InterPro; IPR008993; TIMP-like_OB-fold.
PANTHER; PTHR11412:SF83; PTHR11412:SF83; 1.
Pfam; PF00207; A2M; 1.
Pfam; PF07703; A2M_BRD; 1.
Pfam; PF07677; A2M_recep; 1.
Pfam; PF01821; ANATO; 1.
Pfam; PF01835; MG2; 1.
Pfam; PF01759; NTR; 1.
Pfam; PF07678; TED_complement; 1.
PRINTS; PR00004; ANAPHYLATOXN.
SMART; SM01360; A2M; 1.
SMART; SM01359; A2M_N_2; 1.
SMART; SM01361; A2M_recep; 1.
SMART; SM00104; ANATO; 1.
SMART; SM00643; C345C; 1.
SUPFAM; SSF47686; SSF47686; 1.
SUPFAM; SSF48239; SSF48239; 1.
SUPFAM; SSF49410; SSF49410; 1.
SUPFAM; SSF50242; SSF50242; 1.
PROSITE; PS01177; ANAPHYLATOXIN_1; 1.
PROSITE; PS01178; ANAPHYLATOXIN_2; 1.
PROSITE; PS50189; NTR; 1.
1: Evidence at protein level;
3D-structure; Cleavage on pair of basic residues;
Complement alternate pathway; Complement pathway; Complete proteome;
Cytolysis; Direct protein sequencing; Disulfide bond; Glycoprotein;
Immunity; Inflammatory response; Innate immunity;
Membrane attack complex; Polymorphism; Reference proteome; Secreted;
Signal.
SIGNAL 1 18 {ECO:0000255}.
CHAIN 19 673 Complement C5 beta chain.
/FTId=PRO_0000005985.
PROPEP 674 677 {ECO:0000269|PubMed:690134}.
/FTId=PRO_0000005986.
CHAIN 678 1676 Complement C5 alpha chain.
/FTId=PRO_0000005987.
CHAIN 678 751 C5a anaphylatoxin.
/FTId=PRO_0000005988.
CHAIN 752 1676 Complement C5 alpha' chain.
/FTId=PRO_0000005989.
DOMAIN 698 732 Anaphylatoxin-like. {ECO:0000255|PROSITE-
ProRule:PRU00022}.
DOMAIN 1532 1676 NTR. {ECO:0000255|PROSITE-
ProRule:PRU00295}.
REGION 692 721 Involved in C5AR1 binding.
{ECO:0000269|PubMed:9553099}.
CARBOHYD 741 741 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:18536718}.
CARBOHYD 911 911 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:18536718,
ECO:0000269|PubMed:21217642}.
CARBOHYD 1115 1115 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1630 1630 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 567 810
DISULFID 634 669
DISULFID 698 724
DISULFID 699 731
DISULFID 711 732
DISULFID 856 883
DISULFID 866 1527
DISULFID 1101 1159
DISULFID 1375 1505
DISULFID 1405 1474
DISULFID 1520 1525
DISULFID 1532 1606
DISULFID 1553 1676
DISULFID 1654 1657
VARIANT 145 145 V -> I (in dbSNP:rs17216529).
{ECO:0000269|Ref.2}.
/FTId=VAR_038735.
VARIANT 354 354 L -> M (in dbSNP:rs34552775).
/FTId=VAR_048822.
VARIANT 389 389 T -> I. {ECO:0000269|PubMed:15488949,
ECO:0000269|PubMed:1984448}.
/FTId=VAR_023946.
VARIANT 449 449 R -> G (in dbSNP:rs2230213).
{ECO:0000269|Ref.2}.
/FTId=VAR_038736.
VARIANT 518 518 F -> S.
/FTId=VAR_001996.
VARIANT 802 802 V -> I (in dbSNP:rs17611).
{ECO:0000269|PubMed:15488949,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:1984448,
ECO:0000269|PubMed:2579066,
ECO:0000269|PubMed:3365401,
ECO:0000269|Ref.2, ECO:0000269|Ref.3}.
/FTId=VAR_014574.
VARIANT 885 885 R -> C (polymorphism associated with poor
response to eculizumab in PNH patients;
dbSNP:rs373359894).
{ECO:0000269|PubMed:24521109}.
/FTId=VAR_071067.
VARIANT 885 885 R -> H (polymorphism associated with poor
response to eculizumab in PNH patients;
dbSNP:rs56040400).
{ECO:0000269|PubMed:24521109}.
/FTId=VAR_071068.
VARIANT 928 928 R -> Q (in dbSNP:rs41309892).
{ECO:0000269|Ref.2}.
/FTId=VAR_038737.
VARIANT 933 933 G -> V (in dbSNP:rs41309902).
{ECO:0000269|Ref.2}.
/FTId=VAR_038738.
VARIANT 966 966 D -> Y (polymorphism; confirmed at
protein level; dbSNP:rs2230212).
{ECO:0000269|PubMed:22028381}.
/FTId=VAR_048823.
VARIANT 1033 1033 I -> T (in dbSNP:rs41311881).
{ECO:0000269|Ref.2}.
/FTId=VAR_038739.
VARIANT 1037 1037 D -> N (in dbSNP:rs41311883).
{ECO:0000269|Ref.2}.
/FTId=VAR_038740.
VARIANT 1043 1043 Q -> K (in dbSNP:rs41311887).
{ECO:0000269|Ref.2}.
/FTId=VAR_038741.
VARIANT 1053 1053 M -> L (in dbSNP:rs17609).
/FTId=VAR_014575.
VARIANT 1310 1310 S -> N (in dbSNP:rs17610).
{ECO:0000269|Ref.2}.
/FTId=VAR_014576.
VARIANT 1365 1365 V -> A (in dbSNP:rs16910245).
/FTId=VAR_048824.
VARIANT 1437 1437 E -> D (in dbSNP:rs17612).
{ECO:0000269|Ref.2}.
/FTId=VAR_014577.
STRAND 22 26 {ECO:0000244|PDB:5B71}.
STRAND 29 45 {ECO:0000244|PDB:5B71}.
STRAND 50 58 {ECO:0000244|PDB:5B71}.
TURN 59 61 {ECO:0000244|PDB:5B71}.
STRAND 65 73 {ECO:0000244|PDB:5B71}.
TURN 75 79 {ECO:0000244|PDB:5B71}.
STRAND 80 87 {ECO:0000244|PDB:5B71}.
HELIX 89 91 {ECO:0000244|PDB:5HCC}.
STRAND 95 97 {ECO:0000244|PDB:5HCC}.
STRAND 101 107 {ECO:0000244|PDB:5B71}.
STRAND 112 120 {ECO:0000244|PDB:5B71}.
STRAND 124 131 {ECO:0000244|PDB:5HCC}.
STRAND 133 135 {ECO:0000244|PDB:5HCC}.
STRAND 143 148 {ECO:0000244|PDB:5HCC}.
STRAND 152 154 {ECO:0000244|PDB:5HCC}.
STRAND 159 164 {ECO:0000244|PDB:5HCC}.
STRAND 170 176 {ECO:0000244|PDB:5HCC}.
STRAND 179 184 {ECO:0000244|PDB:5HCC}.
STRAND 197 208 {ECO:0000244|PDB:5HCC}.
STRAND 212 219 {ECO:0000244|PDB:5HCC}.
STRAND 226 234 {ECO:0000244|PDB:5HCC}.
STRAND 236 238 {ECO:0000244|PDB:5HCC}.
TURN 241 244 {ECO:0000244|PDB:4A5W}.
STRAND 246 254 {ECO:0000244|PDB:5HCC}.
TURN 255 257 {ECO:0000244|PDB:5HCC}.
STRAND 262 273 {ECO:0000244|PDB:5HCC}.
STRAND 275 277 {ECO:0000244|PDB:5HCC}.
STRAND 281 283 {ECO:0000244|PDB:5HCC}.
STRAND 289 293 {ECO:0000244|PDB:5HCC}.
STRAND 296 301 {ECO:0000244|PDB:5HCC}.
HELIX 303 307 {ECO:0000244|PDB:5HCC}.
TURN 308 310 {ECO:0000244|PDB:5HCC}.
STRAND 314 318 {ECO:0000244|PDB:5HCC}.
STRAND 322 331 {ECO:0000244|PDB:5HCC}.
TURN 332 334 {ECO:0000244|PDB:5HCC}.
STRAND 337 347 {ECO:0000244|PDB:5HCC}.
STRAND 353 356 {ECO:0000244|PDB:5HCC}.
STRAND 361 363 {ECO:0000244|PDB:5HCC}.
STRAND 365 367 {ECO:0000244|PDB:3CU7}.
STRAND 369 376 {ECO:0000244|PDB:5HCC}.
STRAND 378 380 {ECO:0000244|PDB:4A5W}.
STRAND 387 396 {ECO:0000244|PDB:5HCC}.
STRAND 401 403 {ECO:0000244|PDB:5HCC}.
STRAND 407 410 {ECO:0000244|PDB:5HCC}.
TURN 413 415 {ECO:0000244|PDB:5HCC}.
STRAND 416 422 {ECO:0000244|PDB:5HCC}.
STRAND 428 437 {ECO:0000244|PDB:5HCC}.
HELIX 444 446 {ECO:0000244|PDB:3CU7}.
STRAND 449 456 {ECO:0000244|PDB:5HCC}.
STRAND 464 468 {ECO:0000244|PDB:5HCC}.
STRAND 472 476 {ECO:0000244|PDB:3CU7}.
STRAND 480 492 {ECO:0000244|PDB:5HCC}.
HELIX 493 495 {ECO:0000244|PDB:5HCC}.
STRAND 498 505 {ECO:0000244|PDB:5HCC}.
STRAND 508 516 {ECO:0000244|PDB:5HCC}.
STRAND 519 522 {ECO:0000244|PDB:3CU7}.
STRAND 524 529 {ECO:0000244|PDB:5HCC}.
HELIX 532 534 {ECO:0000244|PDB:5HCC}.
STRAND 536 546 {ECO:0000244|PDB:5HCC}.
STRAND 548 550 {ECO:0000244|PDB:5HCC}.
STRAND 553 563 {ECO:0000244|PDB:5HCC}.
STRAND 571 577 {ECO:0000244|PDB:5HCC}.
STRAND 580 582 {ECO:0000244|PDB:3CU7}.
STRAND 587 606 {ECO:0000244|PDB:5HCC}.
HELIX 607 610 {ECO:0000244|PDB:5HCC}.
HELIX 614 616 {ECO:0000244|PDB:4A5W}.
HELIX 623 627 {ECO:0000244|PDB:5HCC}.
HELIX 628 630 {ECO:0000244|PDB:4A5W}.
STRAND 635 637 {ECO:0000244|PDB:5HCC}.
HELIX 642 648 {ECO:0000244|PDB:5HCC}.
STRAND 651 657 {ECO:0000244|PDB:5HCC}.
TURN 663 666 {ECO:0000244|PDB:5HCD}.
HELIX 678 687 {ECO:0000244|PDB:4UU9}.
TURN 689 692 {ECO:0000244|PDB:3HQB}.
HELIX 693 703 {ECO:0000244|PDB:4UU9}.
STRAND 707 709 {ECO:0000244|PDB:4UU9}.
HELIX 711 715 {ECO:0000244|PDB:4UU9}.
HELIX 722 740 {ECO:0000244|PDB:4UU9}.
TURN 744 746 {ECO:0000244|PDB:5B4P}.
STRAND 764 767 {ECO:0000244|PDB:5HCC}.
STRAND 777 789 {ECO:0000244|PDB:5HCC}.
STRAND 795 805 {ECO:0000244|PDB:5HCC}.
STRAND 808 811 {ECO:0000244|PDB:5HCC}.
STRAND 815 819 {ECO:0000244|PDB:5HCC}.
STRAND 822 828 {ECO:0000244|PDB:5HCC}.
STRAND 838 847 {ECO:0000244|PDB:5HCC}.
STRAND 849 851 {ECO:0000244|PDB:5HCC}.
STRAND 853 859 {ECO:0000244|PDB:5HCC}.
STRAND 863 869 {ECO:0000244|PDB:5HCC}.
STRAND 874 877 {ECO:0000244|PDB:4A5W}.
STRAND 886 888 {ECO:0000244|PDB:5HCC}.
STRAND 892 902 {ECO:0000244|PDB:5HCC}.
STRAND 906 916 {ECO:0000244|PDB:5HCC}.
STRAND 919 930 {ECO:0000244|PDB:5HCC}.
STRAND 932 945 {ECO:0000244|PDB:5HCC}.
STRAND 949 952 {ECO:0000244|PDB:5HCC}.
STRAND 956 959 {ECO:0000244|PDB:5HCC}.
STRAND 974 982 {ECO:0000244|PDB:5HCC}.
HELIX 985 992 {ECO:0000244|PDB:5HCC}.
STRAND 993 996 {ECO:0000244|PDB:3CU7}.
TURN 999 1002 {ECO:0000244|PDB:5HCC}.
HELIX 1008 1013 {ECO:0000244|PDB:5HCC}.
HELIX 1016 1027 {ECO:0000244|PDB:5HCC}.
HELIX 1031 1033 {ECO:0000244|PDB:5HCC}.
STRAND 1034 1036 {ECO:0000244|PDB:5HCC}.
HELIX 1038 1054 {ECO:0000244|PDB:5HCC}.
HELIX 1055 1059 {ECO:0000244|PDB:5HCC}.
STRAND 1066 1069 {ECO:0000244|PDB:5HCC}.
HELIX 1076 1089 {ECO:0000244|PDB:5HCC}.
TURN 1090 1092 {ECO:0000244|PDB:5HCC}.
HELIX 1097 1110 {ECO:0000244|PDB:5HCC}.
STRAND 1121 1123 {ECO:0000244|PDB:5HCC}.
HELIX 1133 1154 {ECO:0000244|PDB:5HCC}.
HELIX 1155 1158 {ECO:0000244|PDB:5HCC}.
HELIX 1162 1178 {ECO:0000244|PDB:5HCC}.
HELIX 1185 1196 {ECO:0000244|PDB:5HCC}.
HELIX 1203 1214 {ECO:0000244|PDB:5HCC}.
STRAND 1217 1219 {ECO:0000244|PDB:5HCC}.
TURN 1220 1223 {ECO:0000244|PDB:5HCC}.
STRAND 1224 1227 {ECO:0000244|PDB:5HCC}.
TURN 1233 1235 {ECO:0000244|PDB:5HCC}.
HELIX 1245 1260 {ECO:0000244|PDB:5HCC}.
HELIX 1264 1277 {ECO:0000244|PDB:5HCC}.
STRAND 1280 1282 {ECO:0000244|PDB:3CU7}.
HELIX 1287 1303 {ECO:0000244|PDB:5HCC}.
STRAND 1310 1317 {ECO:0000244|PDB:5HCC}.
STRAND 1324 1332 {ECO:0000244|PDB:5HCC}.
STRAND 1338 1340 {ECO:0000244|PDB:4A5W}.
STRAND 1342 1344 {ECO:0000244|PDB:5HCC}.
STRAND 1346 1350 {ECO:0000244|PDB:5HCC}.
STRAND 1357 1368 {ECO:0000244|PDB:5HCC}.
STRAND 1371 1373 {ECO:0000244|PDB:3CU7}.
STRAND 1376 1384 {ECO:0000244|PDB:5HCC}.
STRAND 1401 1408 {ECO:0000244|PDB:5HCC}.
STRAND 1420 1427 {ECO:0000244|PDB:5HCC}.
STRAND 1432 1434 {ECO:0000244|PDB:5HCC}.
HELIX 1436 1443 {ECO:0000244|PDB:5HCC}.
STRAND 1451 1456 {ECO:0000244|PDB:5HCC}.
STRAND 1459 1465 {ECO:0000244|PDB:5HCC}.
STRAND 1469 1471 {ECO:0000244|PDB:5HCC}.
STRAND 1473 1483 {ECO:0000244|PDB:5HCC}.
STRAND 1485 1487 {ECO:0000244|PDB:5HCC}.
STRAND 1491 1497 {ECO:0000244|PDB:5HCC}.
STRAND 1500 1509 {ECO:0000244|PDB:5HCC}.
STRAND 1522 1524 {ECO:0000244|PDB:5HCC}.
TURN 1526 1529 {ECO:0000244|PDB:5HCC}.
STRAND 1530 1532 {ECO:0000244|PDB:5HCC}.
HELIX 1547 1550 {ECO:0000244|PDB:5HCC}.
STRAND 1559 1571 {ECO:0000244|PDB:5HCC}.
STRAND 1574 1590 {ECO:0000244|PDB:5HCC}.
STRAND 1597 1605 {ECO:0000244|PDB:5HCC}.
STRAND 1616 1622 {ECO:0000244|PDB:5HCC}.
STRAND 1625 1629 {ECO:0000244|PDB:5HCC}.
STRAND 1632 1638 {ECO:0000244|PDB:5HCC}.
STRAND 1644 1647 {ECO:0000244|PDB:5HCC}.
STRAND 1650 1652 {ECO:0000244|PDB:5HCC}.
HELIX 1657 1672 {ECO:0000244|PDB:5HCC}.
SEQUENCE 1676 AA; 188305 MW; A7589E352F74672A CRC64;
MGLLGILCFL IFLGKTWGQE QTYVISAPKI FRVGASENIV IQVYGYTEAF DATISIKSYP
DKKFSYSSGH VHLSSENKFQ NSAILTIQPK QLPGGQNPVS YVYLEVVSKH FSKSKRMPIT
YDNGFLFIHT DKPVYTPDQS VKVRVYSLND DLKPAKRETV LTFIDPEGSE VDMVEEIDHI
GIISFPDFKI PSNPRYGMWT IKAKYKEDFS TTGTAYFEVK EYVLPHFSVS IEPEYNFIGY
KNFKNFEITI KARYFYNKVV TEADVYITFG IREDLKDDQK EMMQTAMQNT MLINGIAQVT
FDSETAVKEL SYYSLEDLNN KYLYIAVTVI ESTGGFSEEA EIPGIKYVLS PYKLNLVATP
LFLKPGIPYP IKVQVKDSLD QLVGGVPVTL NAQTIDVNQE TSDLDPSKSV TRVDDGVASF
VLNLPSGVTV LEFNVKTDAP DLPEENQARE GYRAIAYSSL SQSYLYIDWT DNHKALLVGE
HLNIIVTPKS PYIDKITHYN YLILSKGKII HFGTREKFSD ASYQSINIPV TQNMVPSSRL
LVYYIVTGEQ TAELVSDSVW LNIEEKCGNQ LQVHLSPDAD AYSPGQTVSL NMATGMDSWV
ALAAVDSAVY GVQRGAKKPL ERVFQFLEKS DLGCGAGGGL NNANVFHLAG LTFLTNANAD
DSQENDEPCK EILRPRRTLQ KKIEEIAAKY KHSVVKKCCY DGACVNNDET CEQRAARISL
GPRCIKAFTE CCVVASQLRA NISHKDMQLG RLHMKTLLPV SKPEIRSYFP ESWLWEVHLV
PRRKQLQFAL PDSLTTWEIQ GVGISNTGIC VADTVKAKVF KDVFLEMNIP YSVVRGEQIQ
LKGTVYNYRT SGMQFCVKMS AVEGICTSES PVIDHQGTKS SKCVRQKVEG SSSHLVTFTV
LPLEIGLHNI NFSLETWFGK EILVKTLRVV PEGVKRESYS GVTLDPRGIY GTISRRKEFP
YRIPLDLVPK TEIKRILSVK GLLVGEILSA VLSQEGINIL THLPKGSAEA ELMSVVPVFY
VFHYLETGNH WNIFHSDPLI EKQKLKKKLK EGMLSIMSYR NADYSYSVWK GGSASTWLTA
FALRVLGQVN KYVEQNQNSI CNSLLWLVEN YQLDNGSFKE NSQYQPIKLQ GTLPVEAREN
SLYLTAFTVI GIRKAFDICP LVKIDTALIK ADNFLLENTL PAQSTFTLAI SAYALSLGDK
THPQFRSIVS ALKREALVKG NPPIYRFWKD NLQHKDSSVP NTGTARMVET TAYALLTSLN
LKDINYVNPV IKWLSEEQRY GGGFYSTQDT INAIEGLTEY SLLVKQLRLS MDIDVSYKHK
GALHNYKMTD KNFLGRPVEV LLNDDLIVST GFGSGLATVH VTTVVHKTST SEEVCSFYLK
IDTQDIEASH YRGYGNSDYK RIVACASYKP SREESSSGSS HAVMDISLPT GISANEEDLK
ALVEGVDQLF TDYQIKDGHV ILQLNSIPSS DFLCVRFRIF ELFEVGFLSP ATFTVYEYHR
PDKQCTMFYS TSNIKIQKVC EGAACKCVEA DCGQMQEELD LTISAETRKQ TACKPEIAYA
YKVSITSITV ENVFVKYKAT LLDIYKTGEA VAEKDSEITF IKKVTCTNAE LVKGRQYLIM
GKEALQIKYN FSFRYIYPLD SLTWIEYWPR DTTCSSCQAF LANLDEFAED IFLNGC


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