Complement factor B Recombinant Protein | Cfb recombinant protein

Recombinant Mouse Complement factor B

Cat. Num. AAA961611

• Gene Names: CFB; BF; FB; BFD; GBG; CFAB; CFBD; PBF2; AHUS4; FBI12; H2-Bf; ARMD14
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Complement factor B; Recombinant Mouse Complement factor B; C3/C5 convertase; Glycine-rich beta glycoprotein; GBGPBF2; Properdin factor B; Cfb recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 23-761aa; Full Length of Mature Protein
• Sequence: TPVLEARPQVSCSLEGVEIKGGSFQLLQGGQALEYLCPSGFYPYPVQTRTCRSTGSWSDLQTRDQKIVQKAECRAIRCPRPQDFENGEFWPRSPFYNLSDQISFQCYDGYVLRGSANRTCQENGRWDGQTAICDDGAGYCPNPGIPIGTRKVGSQYRLEDIVTYHCSRGLVLRGSQKRKCQEGGSWSGTEPSCQDSFMYDSPQEVAEAFLSSLTETIEGADAEDGHSPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGSSNFTGAKRCLTNLIEKVASYGVRPRYGLLTYATVPKVLVRVSDERSSDADWVTEKLNQISYEDHKLKSGTNTKRALQAVYSMMSWAGDAPPEGWNRTRHVIIIMTDGLHNMGGNPVTVIQDIRALLDIGRDPKNPREDYLDVYVFGVGPLVDSVNINALASKKDNEHHVFKVKDMEDLENVFYQMIDETKSLSLCGMVWEHKKGNDYHKQPWQAKISVTRPLKGHETCMGAVVSEYFVLTAAHCFMVDDQKHSIKVSVGGQRRDLEIEEVLFHPKYNINGKKAEGIPEFYDYDVALVKLKNKLKYGQTLRPICLPCTEGTTRALRLPQTATCKQHKEQLLPVKDVKALFVSEQGKSLTRKEVYIKNGDKKASCERDATKAQGYEKVKDASEVVTPRFLCTGGVDPYADPNTCKGDSGGPLIVHKRSRFIQVGVISWGVVDVCRDQRRQQLVPSYARDFHINLFQVLPWLKDKLKDEDLGFL
• Sequence Length: 761

• Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to [email protected] for more details.
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-Page

Related Product Information for Cfb recombinant protein

Factor B which is part of the alternate pathway of the complent system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complent 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.

References

Molecular characterization of human complement factor B subtypes.Davrinche C., Abbal M., Clerc A.Immunogenetics 32:309-312(1990) Human factor B. Complete cDNA sequence of the BF*S allele.Mejia J.E., Jahn I., de la Salle H., Hauptmann G.Hum. Immunol. 39:49-53(1994) Human complement factor B functional properties of a recombinant zymogen of the alternative activation pathway convertase.Schwaeble W., Luettig B., Sokolowski T., Estaller C., Weiss E.H., Meyer Zum Bueschenfelde K.-H., Whaley K., Dippold W.Immunobiology 188:221-232(1993) Human complement factor B cDNA cloning, nucleotide sequencing, phenotypic conversion by site-directed mutagenesis and expression.Horiuchi T., Kim S., Matsumoto M., Watanabe I., Fujita S., Volanakis J.E.Mol. Immunol. 30:1587-1592(1993) Expression and alternative splicing of human factor B gene in leukemic mononuclear cells.Jaatinen T., Kanerva J., Poutanen K.E., Saarinen-Pihkala U., Lokki M.-L.Analysis of the gene-dense major histocompatibility complex class III region and its comparison to mouse.Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D., Hood L.Genome Res. 13:2621-2636(2003) SeattleSNPs variation discovery resourceTotoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.The DNA sequence and analysis of human chromosome 6.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.Nature 425:805-811(2003) 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. Complete primary structure for the zymogen of human complement factor B.Mole J.E., Anderson J.K., Davison E.A., Woods D.E.J. Biol. Chem. 259:3407-3412(1984) 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.Christie D.L., Gagnon J.Biochem. J. 209:61-70(1983) Molecular cloning and characterization of the gene coding for human complement protein factor B.Campbell R.D., Porter R.R.Proc. Natl. Acad. Sci. U.S.A. 80:4464-4468(1983) Isolation of cDNA clones for the human complement protein factor B, a class III major histocompatibility complex gene product.Woods D.E., Markham A.F., Ricker A.T., Goldberger G., Colten H.R.Proc. Natl. Acad. Sci. U.S.A. 79:5661-5665(1982) Internal homologies of the Ba fragment from human complement component Factor B, a class III MHC antigen.Morley B.J., Campbell R.D.EMBO J. 3:153-157(1984) Cell-specific expression of the human complement protein factor B gene evidence for the role of two distinct 5'-flanking elements.Wu L.C., Morley B.J., Campbell R.D.Cell 48:331-342(1987) The principal site of glycation of human complement factor B.Niemann M.A., Bhown A.S., Miller E.J.Biochem. J. 274:473-480(1991) Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry.Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.J. Proteome Res. 4:2070-2080(2005) Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry.Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.J. Proteome Res. 8:651-661(2009) Deficiency in complement factor B.Slade C., Bosco J., Unglik G., Bleasel K., Nagel M., Winship I.N. Engl. J. Med. 369:1667-1669(2013) New structural motifs on the chymotrypsin fold and their potential roles in complement factor B.Jing H., Xu Y., Carson M., Moore D., Macon K.J., Volanakis J.E., Narayana S.V.L.EMBO J. 19:164-173(2000) Factor B structure provides insights into activation of the central protease of the complement system.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.Nat. Struct. Mol. Biol. 14:224-228(2007) Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex.Janssen B.J., Gomes L., Koning R.I., Svergun D.I., Koster A.J., Fritzinger D.C., Vogel C.-W., Gros P.EMBO J. 28:2469-2478(2009) Variation in factor B (BF) and complement component 2 (C2) genes is associated with age-related macular degeneration.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.Nat. Genet. 38:458-462(2006) Gain-of-function mutations in complement factor B are associated with atypical hemolytic uremic syndrome.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.Proc. Natl. Acad. Sci. U.S.A. 104:240-245(2007) Mutations in alternative pathway complement proteins in American patients with atypical hemolytic uremic syndrome.Maga T.K., Nishimura C.J., Weaver A.E., Frees K.L., Smith R.J.H.Hum. Mutat. 31:E1445-E1460(2010)

NCBI and Uniprot Product Information

• NCBI GI #: 67782358
• NCBI GeneID: 629
• NCBI Accession #: NP_001701.2
• NCBI GenBank Nucleotide #: NM_001710.5
• UniProt Accession #: P00751; O15006; Q29944; Q53F89; Q5JP67; Q5ST50; Q96HX6; Q9BTF5; Q9BX92; B0QZQ6
• Molecular Weight: 87 kDa
• NCBI Official Full Name: complement factor B preproprotein
• NCBI Official Synonym Full Names: complement factor B
• NCBI Official Symbol: CFB
• NCBI Official Synonym Symbols: BF; FB; BFD; GBG; CFAB; CFBD; PBF2; AHUS4; FBI12; H2-Bf; ARMD14
• NCBI Protein Information: complement factor B
• UniProt Protein Name: Complement factor B
• Protein Family: Complement factor
• UniProt Gene Name: CFB
• UniProt Synonym Gene Names: BF; BFD; GBG
• UniProt Entry Name: CFAB_HUMAN

NCBI Description

This gene encodes complement factor B, a component of the alternative pathway of complement activation. Factor B circulates in the blood as a single chain polypeptide. Upon activation of the alternative pathway, it is cleaved by complement factor D yielding the noncatalytic chain Ba and the catalytic subunit Bb. The active subunit Bb is a serine protease which associates with C3b to form the alternative pathway C3 convertase. Bb is involved in the proliferation of preactivated B lymphocytes, while Ba inhibits their proliferation. This gene localizes to the major histocompatibility complex (MHC) class III region on chromosome 6. This cluster includes several genes involved in regulation of the immune reaction. Polymorphisms in this gene are associated with a reduced risk of age-related macular degeneration. The polyadenylation site of this gene is 421 bp from the 5' end of the gene for complement component 2. [provided by RefSeq, Jul 2008]

Uniprot Description

CFB: 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. Defects in CFB are a cause of susceptibility to hemolytic uremic syndrome atypical type 4 (AHUS4). 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. 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. Belongs to the peptidase S1 family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Secreted; Protease; EC 3.4.21.47; Secreted, signal peptide

Chromosomal Location of Human Ortholog: 6p21.3

Cellular Component: extracellular region; extracellular space; plasma membrane

Molecular Function: complement binding; serine-type endopeptidase activity

Biological Process: complement activation; complement activation, alternative pathway; innate immune response; proteolysis; regulation of complement activation

Disease: Complement Factor B Deficiency; Hemolytic Uremic Syndrome, Atypical, Susceptibility To, 4; Macular Degeneration, Age-related, 14