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Complement factor B (EC 3.4.21.47) (C3/C5 convertase) (Glycine-rich beta glycoprotein) (GBG) (PBF2) (Properdin factor B) [Cleaved into: Complement factor B Ba fragment; Complement factor B Bb fragment]

 CFAB_HUMAN              Reviewed;         764 AA.
P00751; B0QZQ6; O15006; Q29944; Q53F89; Q5JP67; Q5ST50; Q96HX6;
Q9BTF5; Q9BX92;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
01-OCT-1994, sequence version 2.
25-OCT-2017, entry version 224.
RecName: Full=Complement factor B;
EC=3.4.21.47;
AltName: Full=C3/C5 convertase;
AltName: Full=Glycine-rich beta glycoprotein;
Short=GBG;
AltName: Full=PBF2;
AltName: Full=Properdin factor B;
Contains:
RecName: Full=Complement factor B Ba fragment;
Contains:
RecName: Full=Complement factor B Bb fragment;
Flags: Precursor;
Name=CFB; Synonyms=BF, BFD;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28; GLN-28;
GLN-32 AND SER-736.
PubMed=2249879; DOI=10.1007/BF00211644;
Davrinche C., Abbal M., Clerc A.;
"Molecular characterization of human complement factor B subtypes.";
Immunogenetics 32:309-312(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28 AND
GLN-32.
TISSUE=Liver;
PubMed=8181962; DOI=10.1016/0198-8859(94)90100-7;
Mejia J.E., Jahn I., de la Salle H., Hauptmann G.;
"Human factor B. Complete cDNA sequence of the BF*S allele.";
Hum. Immunol. 39:49-53(1994).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28 AND
GLN-32.
TISSUE=Liver;
PubMed=8225386;
Schwaeble W., Luettig B., Sokolowski T., Estaller C., Weiss E.H.,
Meyer Zum Bueschenfelde K.-H., Whaley K., Dippold W.;
"Human complement factor B: functional properties of a recombinant
zymogen of the alternative activation pathway convertase.";
Immunobiology 188:221-232(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS ARG-28 AND
GLN-32.
PubMed=8247029; DOI=10.1016/0161-5890(93)90450-P;
Horiuchi T., Kim S., Matsumoto M., Watanabe I., Fujita S.,
Volanakis J.E.;
"Human complement factor B: cDNA cloning, nucleotide sequencing,
phenotypic conversion by site-directed mutagenesis and expression.";
Mol. Immunol. 30:1587-1592(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Jaatinen T., Kanerva J., Poutanen K.E., Saarinen-Pihkala U.,
Lokki M.-L.;
"Expression and alternative splicing of human factor B gene in
leukemic mononuclear cells.";
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14656967; DOI=10.1101/gr.1736803;
Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S.,
Campbell R.D., Hood L.;
"Analysis of the gene-dense major histocompatibility complex class III
region and its comparison to mouse.";
Genome Res. 13:2621-2636(2003).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS HIS-9; GLN-32; TRP-32;
SER-252; GLU-565 AND GLU-651.
SeattleSNPs variation discovery resource;
Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
TRP-32.
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT GLU-565.
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).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT TRP-32.
Mural R.J., Istrail S., Sutton 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.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
TRP-32.
TISSUE=Colon;
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).
[12]
PROTEIN SEQUENCE OF 26-764, PARTIAL NUCLEOTIDE SEQUENCE [MRNA], AND
GLYCOSYLATION AT ASN-122; ASN-142; ASN-285 AND ASN-378.
PubMed=6546754;
Mole J.E., Anderson J.K., Davison E.A., Woods D.E.;
"Complete primary structure for the zymogen of human complement factor
B.";
J. Biol. Chem. 259:3407-3412(1984).
[13]
PROTEIN SEQUENCE OF 260-764.
PubMed=6342610; DOI=10.1042/bj2090061;
Christie D.L., Gagnon J.;
"Amino acid sequence of the Bb fragment from complement Factor B.
Sequence of the major cyanogen bromide-cleavage peptide (CB-II) and
completion of the sequence of the Bb fragment.";
Biochem. J. 209:61-70(1983).
[14]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 339-764.
PubMed=6308626; DOI=10.1073/pnas.80.14.4464;
Campbell R.D., Porter R.R.;
"Molecular cloning and characterization of the gene coding for human
complement protein factor B.";
Proc. Natl. Acad. Sci. U.S.A. 80:4464-4468(1983).
[15]
NUCLEOTIDE SEQUENCE [MRNA] OF 467-595 AND 752-764.
PubMed=6957884; DOI=10.1073/pnas.79.18.5661;
Woods D.E., Markham A.F., Ricker A.T., Goldberger G., Colten H.R.;
"Isolation of cDNA clones for the human complement protein factor B, a
class III major histocompatibility complex gene product.";
Proc. Natl. Acad. Sci. U.S.A. 79:5661-5665(1982).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 16-259.
PubMed=6323161;
Morley B.J., Campbell R.D.;
"Internal homologies of the Ba fragment from human complement
component Factor B, a class III MHC antigen.";
EMBO J. 3:153-157(1984).
[17]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-99.
TISSUE=Blood;
PubMed=3643061; DOI=10.1016/0092-8674(87)90436-3;
Wu L.C., Morley B.J., Campbell R.D.;
"Cell-specific expression of the human complement protein factor B
gene: evidence for the role of two distinct 5'-flanking elements.";
Cell 48:331-342(1987).
[18]
GLYCATION AT LYS-291.
PubMed=2006911; DOI=10.1042/bj2740473;
Niemann M.A., Bhown A.S., Miller E.J.;
"The principal site of glycation of human complement factor B.";
Biochem. J. 274:473-480(1991).
[19]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-122; ASN-285 AND ASN-378.
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).
[20]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-122 AND ASN-285.
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).
[21]
INVOLVEMENT IN CFBD.
PubMed=24152280; DOI=10.1056/NEJMc1306326;
Slade C., Bosco J., Unglik G., Bleasel K., Nagel M., Winship I.;
"Deficiency in complement factor B.";
N. Engl. J. Med. 369:1667-1669(2013).
[22]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 467-764.
PubMed=10637221; DOI=10.1093/emboj/19.2.164;
Jing H., Xu Y., Carson M., Moore D., Macon K.J., Volanakis J.E.,
Narayana S.V.L.;
"New structural motifs on the chymotrypsin fold and their potential
roles in complement factor B.";
EMBO J. 19:164-173(2000).
[23]
X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 26-764, DOMAIN ARCHITECTURE,
AND GLYCOSYLATION AT ASN-122; ASN-142; ASN-285 AND ASN-378.
PubMed=17310251; DOI=10.1038/nsmb1210;
Milder F.J., Gomes L., Schouten A., Janssen B.J., Huizinga E.G.,
Romijn R.A., Hemrika W., Roos A., Daha M.R., Gros P.;
"Factor B structure provides insights into activation of the central
protease of the complement system.";
Nat. Struct. Mol. Biol. 14:224-228(2007).
[24]
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 26-764 IN COMPLEX WITH COBRA
VENOM FACTOR, GLYCOSYLATION AT ASN-142 AND ASN-378, AND DISULFIDE
BONDS.
PubMed=19574954; DOI=10.1038/emboj.2009.184;
Janssen B.J., Gomes L., Koning R.I., Svergun D.I., Koster A.J.,
Fritzinger D.C., Vogel C.-W., Gros P.;
"Insights into complement convertase formation based on the structure
of the factor B-cobra venom factor complex.";
EMBO J. 28:2469-2478(2009).
[25]
VARIANTS HIS-9 AND GLN-32, AND INVOLVEMENT IN REDUCED RISK OF ARMD.
PubMed=16518403; DOI=10.1038/ng1750;
Gold B., Merriam J.E., Zernant J., Hancox L.S., Taiber A.J., Gehrs K.,
Cramer K., Neel J., Bergeron J., Barile G.R., Smith R.T.,
Hageman G.S., Dean M., Allikmets R.;
"Variation in factor B (BF) and complement component 2 (C2) genes is
associated with age-related macular degeneration.";
Nat. Genet. 38:458-462(2006).
[26]
VARIANTS AHUS4 LEU-286 AND GLU-323, AND CHARACTERIZATION OF VARIANTS
AHUS4 LEU-286 AND GLU-323.
PubMed=17182750; DOI=10.1073/pnas.0603420103;
Goicoechea de Jorge E., Harris C.L., Esparza-Gordillo J., Carreras L.,
Arranz E.A., Garrido C.A., Lopez-Trascasa M., Sanchez-Corral P.,
Morgan B.P., Rodriguez de Cordoba S.;
"Gain-of-function mutations in complement factor B are associated with
atypical hemolytic uremic syndrome.";
Proc. Natl. Acad. Sci. U.S.A. 104:240-245(2007).
[27]
VARIANTS AHUS4 PRO-166; GLN-203; LEU-242; GLN-323; ILE-458 AND
ARG-533.
PubMed=20513133; DOI=10.1002/humu.21256;
Maga T.K., Nishimura C.J., Weaver A.E., Frees K.L., Smith R.J.H.;
"Mutations in alternative pathway complement proteins in American
patients with atypical hemolytic uremic syndrome.";
Hum. Mutat. 31:E1445-E1460(2010).
-!- FUNCTION: Factor B which is part of the alternate pathway of the
complement system is cleaved by factor D into 2 fragments: Ba and
Bb. Bb, a serine protease, then combines with complement factor 3b
to generate the C3 or C5 convertase. It has also been implicated
in proliferation and differentiation of preactivated B-
lymphocytes, rapid spreading of peripheral blood monocytes,
stimulation of lymphocyte blastogenesis and lysis of erythrocytes.
Ba inhibits the proliferation of preactivated B-lymphocytes.
-!- CATALYTIC ACTIVITY: Cleavage of Arg-|-Ser bond in complement
component C3 alpha-chain to yield C3a and C3b, and Arg-|-Xaa bond
in complement component C5 alpha-chain to yield C5a and C5b.
-!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19574954}.
-!- INTERACTION:
P01024:C3; NbExp=3; IntAct=EBI-1223668, EBI-905851;
-!- SUBCELLULAR LOCATION: Secreted.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P00751-1; Sequence=Displayed;
Name=2;
IsoId=P00751-2; Sequence=VSP_005380, VSP_005381;
-!- DOMAIN: The unliganded VWA domain has an inactive 'locked'
conformation whereby the scissile Arg-259|Lys-260 bond is
protected from proteolytic activation.
{ECO:0000269|PubMed:17310251}.
-!- POLYMORPHISM: Two major variants, F and S, and 2 minor variants,
as well as at least 14 very rare variants, have been identified.
The variants His-9 and Gln-32 are associated with a reduced risk
of age-related macular degeneration (ARMD) [MIM:603075]. ARMD is a
multifactorial eye disease and the most common cause of
irreversible vision loss in the developed world.
{ECO:0000269|PubMed:16518403}.
-!- DISEASE: Hemolytic uremic syndrome atypical 4 (AHUS4)
[MIM:612924]: An atypical form of hemolytic uremic syndrome. It is
a complex genetic disease characterized by microangiopathic
hemolytic anemia, thrombocytopenia, renal failure and absence of
episodes of enterocolitis and diarrhea. In contrast to typical
hemolytic uremic syndrome, atypical forms have a poorer prognosis,
with higher death rates and frequent progression to end-stage
renal disease. {ECO:0000269|PubMed:17182750,
ECO:0000269|PubMed:20513133}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry. Susceptibility to the development of atypical hemolytic
uremic syndrome can be conferred by mutations in various
components of or regulatory factors in the complement cascade
system. Other genes may play a role in modifying the phenotype.
-!- DISEASE: Complement factor B deficiency (CFBD) [MIM:615561]: An
immunologic disorder characterized by increased susceptibility to
bacterial infections, particularly Neisseria infections, due to a
defect in the alternative complement pathway.
{ECO:0000269|PubMed:24152280}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/bf/";
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EMBL; X72875; CAA51389.1; -; mRNA.
EMBL; S67310; AAD13989.1; -; mRNA.
EMBL; L15702; AAA16820.1; -; mRNA.
EMBL; X00284; CAA25077.1; -; mRNA.
EMBL; AF349679; AAK30167.1; -; mRNA.
EMBL; AF019413; AAB67977.1; -; Genomic_DNA.
EMBL; AF551848; AAN71991.1; -; Genomic_DNA.
EMBL; AL844853; CAI41860.1; -; Genomic_DNA.
EMBL; AL662849; CAI17456.1; -; Genomic_DNA.
EMBL; BX005143; CAM25864.1; -; Genomic_DNA.
EMBL; CR759782; CAQ07113.1; -; Genomic_DNA.
EMBL; CR388219; CAQ07483.1; -; Genomic_DNA.
EMBL; AK223400; BAD97120.1; -; mRNA.
EMBL; AL645922; CAQ09274.1; -; Genomic_DNA.
EMBL; CH471081; EAX03550.1; -; Genomic_DNA.
EMBL; BC004143; AAH04143.1; -; mRNA.
EMBL; BC007990; AAH07990.1; -; mRNA.
EMBL; K01566; AAA36225.2; -; mRNA.
EMBL; J00125; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; J00126; AAA36226.1; -; mRNA.
EMBL; J00185; AAA36219.1; ALT_SEQ; mRNA.
EMBL; J00186; AAA36220.1; -; mRNA.
EMBL; M15082; AAA59625.1; -; Genomic_DNA.
CCDS; CCDS4729.1; -. [P00751-1]
PIR; S34075; BBHU.
RefSeq; NP_001701.2; NM_001710.5. [P00751-1]
UniGene; Hs.69771; -.
PDB; 1DLE; X-ray; 2.10 A; A/B=470-764.
PDB; 1Q0P; X-ray; 1.80 A; A=254-476.
PDB; 1RRK; X-ray; 2.00 A; A=268-764.
PDB; 1RS0; X-ray; 2.60 A; A=268-764.
PDB; 1RTK; X-ray; 2.30 A; A=268-764.
PDB; 2OK5; X-ray; 2.30 A; A=26-764.
PDB; 2WIN; X-ray; 3.90 A; I/J/K/L=260-764.
PDB; 2XWB; X-ray; 3.49 A; F/H=35-764.
PDB; 2XWJ; X-ray; 4.00 A; I/J/K/L=26-764.
PDB; 3HRZ; X-ray; 2.20 A; D=26-764.
PDB; 3HS0; X-ray; 3.00 A; D/I=26-764.
PDB; 5M6W; X-ray; 6.00 A; J/L=260-764.
PDBsum; 1DLE; -.
PDBsum; 1Q0P; -.
PDBsum; 1RRK; -.
PDBsum; 1RS0; -.
PDBsum; 1RTK; -.
PDBsum; 2OK5; -.
PDBsum; 2WIN; -.
PDBsum; 2XWB; -.
PDBsum; 2XWJ; -.
PDBsum; 3HRZ; -.
PDBsum; 3HS0; -.
PDBsum; 5M6W; -.
ProteinModelPortal; P00751; -.
SMR; P00751; -.
BioGrid; 107098; 16.
DIP; DIP-38319N; -.
IntAct; P00751; 6.
MINT; MINT-3003542; -.
STRING; 9606.ENSP00000416561; -.
BindingDB; P00751; -.
ChEMBL; CHEMBL5731; -.
DrugBank; DB02459; 4-Guanidinobenzoic Acid.
DrugBank; DB04491; Diisopropylphosphono Group.
GuidetoPHARMACOLOGY; 2339; -.
MEROPS; S01.196; -.
iPTMnet; P00751; -.
PhosphoSitePlus; P00751; -.
BioMuta; CFB; -.
DMDM; 584908; -.
DOSAC-COBS-2DPAGE; P00751; -.
REPRODUCTION-2DPAGE; P00751; -.
SWISS-2DPAGE; P00751; -.
MaxQB; P00751; -.
PaxDb; P00751; -.
PeptideAtlas; P00751; -.
PRIDE; P00751; -.
DNASU; 629; -.
Ensembl; ENST00000399981; ENSP00000382862; ENSG00000241253.
Ensembl; ENST00000417261; ENSP00000414889; ENSG00000239754. [P00751-1]
Ensembl; ENST00000419411; ENSP00000391902; ENSG00000242335. [P00751-1]
Ensembl; ENST00000419920; ENSP00000411474; ENSG00000241253.
Ensembl; ENST00000424727; ENSP00000401719; ENSG00000243570. [P00751-1]
Ensembl; ENST00000425368; ENSP00000416561; ENSG00000243649. [P00751-1]
Ensembl; ENST00000426239; ENSP00000413351; ENSG00000242335. [P00751-1]
Ensembl; ENST00000427888; ENSP00000411515; ENSG00000239754. [P00751-1]
Ensembl; ENST00000433503; ENSP00000388352; ENSG00000241534. [P00751-1]
Ensembl; ENST00000436692; ENSP00000389604; ENSG00000243570. [P00751-1]
Ensembl; ENST00000455591; ENSP00000414341; ENSG00000241534. [P00751-1]
GeneID; 629; -.
KEGG; hsa:629; -.
UCSC; uc003nyj.5; human. [P00751-1]
CTD; 629; -.
DisGeNET; 629; -.
EuPathDB; HostDB:ENSG00000243649.8; -.
GeneCards; CFB; -.
GeneReviews; CFB; -.
H-InvDB; HIX0038706; -.
HGNC; HGNC:1037; CFB.
HPA; CAB016381; -.
HPA; HPA000951; -.
HPA; HPA001817; -.
HPA; HPA001832; -.
MalaCards; CFB; -.
MIM; 138470; gene.
MIM; 603075; phenotype.
MIM; 612924; phenotype.
MIM; 615561; phenotype.
neXtProt; NX_P00751; -.
OpenTargets; ENSG00000243649; -.
Orphanet; 279; Age-related macular degeneration.
Orphanet; 93578; Atypical hemolytic-uremic syndrome with B factor anomaly.
PharmGKB; PA25341; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00530000063826; -.
HOVERGEN; HBG002567; -.
InParanoid; P00751; -.
KO; K01335; -.
OrthoDB; EOG091G02G8; -.
PhylomeDB; P00751; -.
TreeFam; TF330194; -.
BRENDA; 3.4.21.47; 2681.
Reactome; R-HSA-173736; Alternative complement activation.
Reactome; R-HSA-174577; Activation of C3 and C5.
Reactome; R-HSA-977606; Regulation of Complement cascade.
SIGNOR; P00751; -.
ChiTaRS; CFB; human.
EvolutionaryTrace; P00751; -.
GeneWiki; Complement_factor_B; -.
GenomeRNAi; 629; -.
PRO; PR:P00751; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000243649; -.
CleanEx; HS_CFB; -.
ExpressionAtlas; P00751; baseline and differential.
Genevisible; P00751; HS.
GO; GO:0072562; C:blood microparticle; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0001848; F:complement binding; TAS:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:Reactome.
GO; GO:0006956; P:complement activation; TAS:Reactome.
GO; GO:0006957; P:complement activation, alternative pathway; TAS:Reactome.
GO; GO:0030449; P:regulation of complement activation; TAS:Reactome.
CDD; cd00033; CCP; 3.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 3.40.50.410; -; 1.
InterPro; IPR011360; Compl_C2_B.
InterPro; IPR028341; Complement_B.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR035976; Sushi/SCR/CCP_sf.
InterPro; IPR000436; Sushi_SCR_CCP_dom.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
InterPro; IPR002035; VWF_A.
InterPro; IPR036465; vWFA_dom_sf.
PANTHER; PTHR19325:SF394; PTHR19325:SF394; 1.
Pfam; PF00084; Sushi; 3.
Pfam; PF00089; Trypsin; 1.
Pfam; PF00092; VWA; 1.
PIRSF; PIRSF001154; Compl_C2_B; 1.
PIRSF; PIRSF500181; Complement_B; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00032; CCP; 3.
SMART; SM00020; Tryp_SPc; 1.
SMART; SM00327; VWA; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF53300; SSF53300; 1.
SUPFAM; SSF57535; SSF57535; 3.
PROSITE; PS50923; SUSHI; 3.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
PROSITE; PS50234; VWFA; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing;
Cleavage on pair of basic residues; Complement alternate pathway;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Glycation; Glycoprotein; Hemolytic uremic syndrome;
Hydrolase; Immunity; Innate immunity; Polymorphism; Protease;
Reference proteome; Repeat; Secreted; Serine protease; Signal; Sushi;
Zymogen.
SIGNAL 1 25 {ECO:0000269|PubMed:6546754}.
CHAIN 26 764 Complement factor B.
/FTId=PRO_0000027545.
CHAIN 26 259 Complement factor B Ba fragment.
/FTId=PRO_0000027546.
CHAIN 260 764 Complement factor B Bb fragment.
/FTId=PRO_0000027547.
DOMAIN 35 100 Sushi 1. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 101 160 Sushi 2. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 163 220 Sushi 3. {ECO:0000255|PROSITE-
ProRule:PRU00302}.
DOMAIN 270 469 VWFA. {ECO:0000255|PROSITE-
ProRule:PRU00219}.
DOMAIN 477 757 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 526 526 Charge relay system.
ACT_SITE 576 576 Charge relay system.
ACT_SITE 699 699 Charge relay system.
CARBOHYD 122 122 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:17310251,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:6546754}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:17310251,
ECO:0000269|PubMed:19574954,
ECO:0000269|PubMed:6546754}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:17310251,
ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:6546754}.
CARBOHYD 291 291 N-linked (Glc) (glycation) lysine.
{ECO:0000269|PubMed:6546754}.
CARBOHYD 378 378 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:17310251,
ECO:0000269|PubMed:19574954,
ECO:0000269|PubMed:6546754}.
DISULFID 37 76 {ECO:0000269|PubMed:19574954}.
DISULFID 62 98 {ECO:0000269|PubMed:19574954}.
DISULFID 103 145 {ECO:0000269|PubMed:19574954}.
DISULFID 131 158 {ECO:0000269|PubMed:19574954}.
DISULFID 165 205 {ECO:0000269|PubMed:19574954}.
DISULFID 191 218 {ECO:0000269|PubMed:19574954}.
DISULFID 478 596 {ECO:0000269|PubMed:19574954}.
DISULFID 511 527 {ECO:0000269|PubMed:19574954}.
DISULFID 599 615 {ECO:0000269|PubMed:19574954}.
DISULFID 656 682 {ECO:0000269|PubMed:19574954}.
DISULFID 695 725 {ECO:0000269|PubMed:19574954}.
VAR_SEQ 543 621 GEKRDLEIEVVLFHPNYNINGKKEAGIPEFYDYDVALIKLK
NKLKYGQTIRPICLPCTEGTTRALRLPPTTTCQQQKEE ->
KDATEGPGLHLCSPGNTSHFLQILHSTHPQCSPIPCTPDQS
GMGEDVKLGMTRGQRQEAAHKEVVPTLLLQEGRSGTWR
(in isoform 2). {ECO:0000303|Ref.5}.
/FTId=VSP_005380.
VAR_SEQ 622 764 Missing (in isoform 2).
{ECO:0000303|Ref.5}.
/FTId=VSP_005381.
VARIANT 9 9 L -> H (in dbSNP:rs4151667).
{ECO:0000269|PubMed:16518403,
ECO:0000269|Ref.7}.
/FTId=VAR_016274.
VARIANT 28 28 W -> Q (in allele FA; requires 2
nucleotide substitutions).
{ECO:0000269|PubMed:2249879}.
/FTId=VAR_006493.
VARIANT 28 28 W -> R (in allele S).
{ECO:0000269|PubMed:2249879,
ECO:0000269|PubMed:8181962,
ECO:0000269|PubMed:8225386,
ECO:0000269|PubMed:8247029}.
/FTId=VAR_006492.
VARIANT 32 32 R -> Q (in allele S; dbSNP:rs641153).
{ECO:0000269|PubMed:16518403,
ECO:0000269|PubMed:2249879,
ECO:0000269|PubMed:8181962,
ECO:0000269|PubMed:8225386,
ECO:0000269|PubMed:8247029,
ECO:0000269|Ref.7}.
/FTId=VAR_006494.
VARIANT 32 32 R -> W (in dbSNP:rs12614).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.10, ECO:0000269|Ref.7,
ECO:0000269|Ref.8}.
/FTId=VAR_016275.
VARIANT 166 166 S -> P (in AHUS4).
{ECO:0000269|PubMed:20513133}.
/FTId=VAR_063659.
VARIANT 203 203 R -> Q (in AHUS4; dbSNP:rs745794224).
{ECO:0000269|PubMed:20513133}.
/FTId=VAR_063660.
VARIANT 242 242 I -> L (in AHUS4; dbSNP:rs144812066).
{ECO:0000269|PubMed:20513133}.
/FTId=VAR_063661.
VARIANT 252 252 G -> S (in dbSNP:rs4151651).
{ECO:0000269|Ref.7}.
/FTId=VAR_016276.
VARIANT 286 286 F -> L (in AHUS4; gain-of-function
mutation that results in enhanced
formation of the C3bBb;
dbSNP:rs117905900).
{ECO:0000269|PubMed:17182750}.
/FTId=VAR_063221.
VARIANT 323 323 K -> E (in AHUS4; gain-of-function
mutation that results in enhanced
formation of the C3bBb;
dbSNP:rs121909748).
{ECO:0000269|PubMed:17182750}.
/FTId=VAR_063222.
VARIANT 323 323 K -> Q (in AHUS4).
{ECO:0000269|PubMed:20513133}.
/FTId=VAR_063662.
VARIANT 458 458 M -> I (in AHUS4; dbSNP:rs200837114).
{ECO:0000269|PubMed:20513133}.
/FTId=VAR_063663.
VARIANT 533 533 K -> R (in AHUS4; dbSNP:rs149101394).
{ECO:0000269|PubMed:20513133}.
/FTId=VAR_063664.
VARIANT 565 565 K -> E (in dbSNP:rs4151659).
{ECO:0000269|PubMed:14574404,
ECO:0000269|Ref.7}.
/FTId=VAR_016277.
VARIANT 651 651 D -> E (in dbSNP:rs4151660).
{ECO:0000269|Ref.7}.
/FTId=VAR_016278.
VARIANT 736 736 A -> S (in allele FA).
{ECO:0000269|PubMed:2249879}.
/FTId=VAR_006495.
CONFLICT 297 297 I -> T (in Ref. 13; AA sequence).
{ECO:0000305}.
CONFLICT 300 300 V -> L (in Ref. 12; AAA36225).
{ECO:0000305}.
CONFLICT 328 328 D -> V (in Ref. 12; AAA36225).
{ECO:0000305}.
CONFLICT 356 357 KK -> EE (in Ref. 12; AAA36225).
{ECO:0000305}.
CONFLICT 537 537 I -> T (in Ref. 15; AAA36219).
{ECO:0000305}.
CONFLICT 764 764 L -> H (in Ref. 15; AAA36220).
{ECO:0000305}.
STRAND 47 51 {ECO:0000244|PDB:3HRZ}.
HELIX 53 55 {ECO:0000244|PDB:3HRZ}.
STRAND 56 61 {ECO:0000244|PDB:3HRZ}.
STRAND 66 70 {ECO:0000244|PDB:3HRZ}.
STRAND 72 76 {ECO:0000244|PDB:3HRZ}.
STRAND 77 79 {ECO:0000244|PDB:2OK5}.
STRAND 80 82 {ECO:0000244|PDB:2XWB}.
STRAND 88 90 {ECO:0000244|PDB:2XWB}.
STRAND 92 94 {ECO:0000244|PDB:3HRZ}.
STRAND 97 100 {ECO:0000244|PDB:3HRZ}.
STRAND 112 115 {ECO:0000244|PDB:3HRZ}.
STRAND 119 122 {ECO:0000244|PDB:3HRZ}.
STRAND 126 131 {ECO:0000244|PDB:3HRZ}.
STRAND 136 139 {ECO:0000244|PDB:3HRZ}.
STRAND 141 145 {ECO:0000244|PDB:3HRZ}.
STRAND 148 150 {ECO:0000244|PDB:2OK5}.
STRAND 151 153 {ECO:0000244|PDB:3HRZ}.
STRAND 154 156 {ECO:0000244|PDB:2OK5}.
STRAND 157 159 {ECO:0000244|PDB:3HRZ}.
STRAND 160 162 {ECO:0000244|PDB:2OK5}.
STRAND 163 165 {ECO:0000244|PDB:3HRZ}.
STRAND 174 177 {ECO:0000244|PDB:3HRZ}.
STRAND 186 191 {ECO:0000244|PDB:3HRZ}.
STRAND 195 199 {ECO:0000244|PDB:3HRZ}.
STRAND 201 205 {ECO:0000244|PDB:3HRZ}.
STRAND 209 213 {ECO:0000244|PDB:3HRZ}.
STRAND 214 216 {ECO:0000244|PDB:2OK5}.
STRAND 217 219 {ECO:0000244|PDB:3HRZ}.
HELIX 227 238 {ECO:0000244|PDB:3HRZ}.
HELIX 240 243 {ECO:0000244|PDB:2XWB}.
STRAND 269 276 {ECO:0000244|PDB:1Q0P}.
TURN 279 281 {ECO:0000244|PDB:1Q0P}.
HELIX 283 301 {ECO:0000244|PDB:1Q0P}.
TURN 302 304 {ECO:0000244|PDB:1Q0P}.
STRAND 308 322 {ECO:0000244|PDB:1Q0P}.
STRAND 324 326 {ECO:0000244|PDB:3HS0}.
HELIX 327 330 {ECO:0000244|PDB:1Q0P}.
HELIX 332 340 {ECO:0000244|PDB:1Q0P}.
HELIX 344 346 {ECO:0000244|PDB:1RRK}.
STRAND 348 350 {ECO:0000244|PDB:3HRZ}.
HELIX 355 366 {ECO:0000244|PDB:1Q0P}.
STRAND 369 372 {ECO:0000244|PDB:3HS0}.
HELIX 374 376 {ECO:0000244|PDB:2OK5}.
HELIX 377 379 {ECO:0000244|PDB:1Q0P}.
STRAND 381 388 {ECO:0000244|PDB:1Q0P}.
STRAND 394 396 {ECO:0000244|PDB:1Q0P}.
HELIX 399 408 {ECO:0000244|PDB:1Q0P}.
STRAND 412 414 {ECO:0000244|PDB:1RTK}.
HELIX 417 419 {ECO:0000244|PDB:2OK5}.
HELIX 420 422 {ECO:0000244|PDB:1Q0P}.
STRAND 423 429 {ECO:0000244|PDB:1Q0P}.
STRAND 431 433 {ECO:0000244|PDB:1RRK}.
HELIX 436 442 {ECO:0000244|PDB:1Q0P}.
STRAND 452 454 {ECO:0000244|PDB:1Q0P}.
STRAND 455 457 {ECO:0000244|PDB:3HRZ}.
HELIX 458 468 {ECO:0000244|PDB:1RRK}.
HELIX 471 474 {ECO:0000244|PDB:1RRK}.
STRAND 483 485 {ECO:0000244|PDB:1DLE}.
HELIX 489 492 {ECO:0000244|PDB:1RRK}.
STRAND 496 501 {ECO:0000244|PDB:1RRK}.
TURN 504 506 {ECO:0000244|PDB:2XWB}.
STRAND 509 515 {ECO:0000244|PDB:1RRK}.
STRAND 517 523 {ECO:0000244|PDB:1RRK}.
HELIX 525 527 {ECO:0000244|PDB:1RRK}.
HELIX 531 533 {ECO:0000244|PDB:2OK5}.
HELIX 534 536 {ECO:0000244|PDB:1RRK}.
STRAND 537 541 {ECO:0000244|PDB:1RRK}.
STRAND 548 555 {ECO:0000244|PDB:1RRK}.
TURN 561 564 {ECO:0000244|PDB:1RRK}.
HELIX 565 567 {ECO:0000244|PDB:1RRK}.
STRAND 578 584 {ECO:0000244|PDB:1RRK}.
STRAND 595 597 {ECO:0000244|PDB:2OK5}.
STRAND 598 600 {ECO:0000244|PDB:1DLE}.
HELIX 601 606 {ECO:0000244|PDB:1RRK}.
HELIX 615 622 {ECO:0000244|PDB:1RRK}.
STRAND 625 638 {ECO:0000244|PDB:1RRK}.
STRAND 640 648 {ECO:0000244|PDB:1RRK}.
HELIX 653 658 {ECO:0000244|PDB:1RRK}.
HELIX 659 662 {ECO:0000244|PDB:1RRK}.
HELIX 666 668 {ECO:0000244|PDB:3HS0}.
HELIX 669 671 {ECO:0000244|PDB:2OK5}.
HELIX 672 674 {ECO:0000244|PDB:1RRK}.
STRAND 680 689 {ECO:0000244|PDB:1RRK}.
HELIX 693 695 {ECO:0000244|PDB:2OK5}.
HELIX 696 698 {ECO:0000244|PDB:1RRK}.
STRAND 702 707 {ECO:0000244|PDB:1RRK}.
STRAND 710 721 {ECO:0000244|PDB:1RRK}.
HELIX 722 724 {ECO:0000244|PDB:2OK5}.
TURN 725 727 {ECO:0000244|PDB:2OK5}.
HELIX 735 737 {ECO:0000244|PDB:1DLE}.
STRAND 739 744 {ECO:0000244|PDB:1RRK}.
HELIX 745 748 {ECO:0000244|PDB:1RRK}.
HELIX 749 755 {ECO:0000244|PDB:1RRK}.
TURN 756 758 {ECO:0000244|PDB:1RRK}.
SEQUENCE 764 AA; 85533 MW; 8BB6C101CC6AC200 CRC64;
MGSNLSPQLC LMPFILGLLS GGVTTTPWSL ARPQGSCSLE GVEIKGGSFR LLQEGQALEY
VCPSGFYPYP VQTRTCRSTG SWSTLKTQDQ KTVRKAECRA IHCPRPHDFE NGEYWPRSPY
YNVSDEISFH CYDGYTLRGS ANRTCQVNGR WSGQTAICDN GAGYCSNPGI PIGTRKVGSQ
YRLEDSVTYH CSRGLTLRGS QRRTCQEGGS WSGTEPSCQD SFMYDTPQEV AEAFLSSLTE
TIEGVDAEDG HGPGEQQKRK IVLDPSGSMN IYLVLDGSDS IGASNFTGAK KCLVNLIEKV
ASYGVKPRYG LVTYATYPKI WVKVSEADSS NADWVTKQLN EINYEDHKLK SGTNTKKALQ
AVYSMMSWPD DVPPEGWNRT RHVIILMTDG LHNMGGDPIT VIDEIRDLLY IGKDRKNPRE
DYLDVYVFGV GPLVNQVNIN ALASKKDNEQ HVFKVKDMEN LEDVFYQMID ESQSLSLCGM
VWEHRKGTDY HKQPWQAKIS VIRPSKGHES CMGAVVSEYF VLTAAHCFTV DDKEHSIKVS
VGGEKRDLEI EVVLFHPNYN INGKKEAGIP EFYDYDVALI KLKNKLKYGQ TIRPICLPCT
EGTTRALRLP PTTTCQQQKE ELLPAQDIKA LFVSEEEKKL TRKEVYIKNG DKKGSCERDA
QYAPGYDKVK DISEVVTPRF LCTGGVSPYA DPNTCRGDSG GPLIVHKRSR FIQVGVISWG
VVDVCKNQKR QKQVPAHARD FHINLFQVLP WLKEKLQDED LGFL


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