Complement Factor B (CFB) Mouse 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.

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)

Small volumes of Cfb recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

MBS961611 is a recombinant protein targeting Cfb. Also known as Recombinant Mouse Complement factor B. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.