Complement C4-B Recombinant Protein | C4B recombinant protein

Recombinant Human Complement C4-B

Cat. Num. AAA114327

• Gene Names: C4B; CH; C4F; CO4; C4B1; C4B2; C4B3; C4B5; C4BD; C4B12; C4B_2; CPAMD3
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Complement C4-B; N/A; Recombinant Human Complement C4-B; Basic complement C4C3 and PZP-like alpha-2-macroglobulin domain-containing protein 3; C4B 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: 1454-1744aa. Partial
• Sequence: EAPKVVEEQESRVHYTVCIWRNGKVGLSGMAIADVTLLSGFHALRADLEKLTSLSDRYVSHFETEGPHVLLYFDSVPTSRECVGFEAVQEVPVGLVQPASATLYDYYNPERRCSVFYGAPSKSRLLATLCSAEVCQCAEGKCPRQRRALERGLQDEDGYRMKFACYYPRVEYGFQVKVLREDSRAAFRLFETKITQVLHFTKDVKAAANQMRNFLVRASCRLRLEPGKEYLIMGLDGATYDLEGHPQYLLDSNSWIEEMPSERLCRSTRQRAACAQLNDFLQEYGTQGCQV

• 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 or email to 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 C4B recombinant protein

Non-enzymatic component of the C3 and C5 convertases and thus essential for the propagation of the classical complent pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes. C4A isotype is responsible for effective binding to form amide bonds with immune aggregates or protein antigens, while C4B isotype catalyzes the transacylation of the thioester carbonyl group to form ester bonds with carbohydrate antigens. Derived from proteolytic degradation of complent C4, C4a anaphylatoxin is a mediator of local inflammatory process. It induces the contraction of smooth muscle, increases vascular permeability and causes histamine release from mast cells and basophilic leukocytes.

Product Categories/Family for C4B recombinant protein

Immunology

References

Complete sequence of the complement C4 gene from the HLA-A1, B8, C4AQ0, C4B1, DR3 haplotype.Ulgiati D., Townend D.C., Christiansen F.T., Dawkins R.L., Abraham L.J.Immunogenetics 43:250-252(1996) Sequence determination of 300 kilobases of the human class III MHC locus.Rowen L., Dankers C., Baskin D., Faust J., Loretz C., Ahearn M.E., Banta A., Swartzell S., Smith T.M., Spies T., Hood L.Molecular genetics of complement C4 implications for MHC evolution and disease susceptibility gene mapping.Sayer D., Puschendorf M., Wetherall J.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) Complete primary structure of human C4a anaphylatoxin.Moon K.E., Gorski J.P., Hugli T.E.J. Biol. Chem. 256:8685-8692(1981) Importance of the alpha 3-fragment of complement C4 for the binding with C4b-binding protein.Hessing M., van 't Veer C., Hackeng T.M., Bouma B.N., Iwanaga S.FEBS Lett. 271:131-136(1990) The structural basis of the multiple forms of human complement component C4.Belt K.T., Carroll M.C., Porter R.R.Cell 36:907-914(1984) Amino acid sequence around the thiol and reactive acyl groups of human complement component C4.Campbell R.D., Gagnon J., Porter R.R.Biochem. J. 199:359-370(1981) The chemical structure of the C4d fragment of the human complement component C4.Chakravarti D.N., Campbell R.D., Porter R.R.Mol. Immunol. 24:1187-1197(1987) Sequence determination of the thiolester site of the fourth component of human complement.Harrison R.A., Thomas M.L., Tack B.F.Proc. Natl. Acad. Sci. U.S.A. 78:7388-7392(1981) C4d DNA sequences of two infrequent human allotypes (C4A13 and C4B12) and the presence of signal sequences enhancing recombination.Martinez-Quiles N., Paz-Artal E., Moreno-Pelayo M.A., Longas J., Ferre-Lopez S., Rosal M., Arnaiz-Villena A.J. Immunol. 161:3438-3443(1998) C4d DNA sequence of complement C4B93 and recombination mechanisms for its generation.Lopez-Goyanes A., Moreno M.A., Ferre S., Paz-Artal E.Tissue Antigens 63:260-262(2004) Amino acid sequence of a polymorphic segment from fragment C4d of human complement component C4.Chakravarti D.N., Campbell R.D., Gagnon J.FEBS Lett. 154:387-390(1983) Identification of the site of sulfation of the fourth component of human complement.Hortin G., Sims H., Strauss A.W.J. Biol. Chem. 261:1786-1793(1986) Complete C4B deficiency in black Americans with systemic lupus erythematosus.Wilson W.A., Perez M.C.J. Rheumatol. 15:1855-1858(1988) Substitution of a single amino acid (aspartic acid for histidine) converts the functional activity of human complement C4B to C4A.Carroll M.C., Fathallah D.M., Bergamaschini L., Alicot E.M., Isenman D.E.Proc. Natl. Acad. Sci. U.S.A. 87:6868-6872(1990) The reaction mechanism of the internal thioester in the human complement component C4.Dodds A.W., Ren X.D., Willis A.C., Law S.K.Nature 379:177-179(1996) Deficiency of human complement protein C4 due to identical frameshift mutations in the C4A and C4B genes.Lokki M.L., Circolo A., Ahokas P., Rupert K.L., Yu C.Y., Colten H.R.J. Immunol. 162:3687-3693(1999) Genetic, structural and functional diversities of human complement components C4A and C4B and their mouse homologues, Slp and C4.Blanchong C.A., Chung E.K., Rupert K.L., Yang Y., Yang Z., Zhou B., Moulds J.M., Yu C.Y.Int. Immunopharmacol. 1:365-392(2001) Identification and quantification of N-linked glycoproteins using hydrazide chemistry, stable isotope labeling and mass spectrometry.Zhang H., Li X.-J., Martin D.B., Aebersold R.Nat. Biotechnol. 21:660-666(2003) Screening for N-glycosylated proteins by liquid chromatography mass spectrometry.Bunkenborg J., Pilch B.J., Podtelejnikov A.V., Wisniewski J.R.Proteomics 4:454-465(2004) Identification of N-linked glycoproteins in human saliva by glycoprotein capture and mass spectrometry.Ramachandran P., Boontheung P., Xie Y., Sondej M., Wong D.T., Loo J.A.J. Proteome Res. 5:1493-1503(2006) Structural basis of the polymorphism of human complement components C4A and C4B gene size, reactivity and antigenicity.Yu C.Y., Belt K.T., Giles C.M., Campbell R.D., Porter R.R.EMBO J. 5:2873-2881(1986) Gene copy-number variation and associated polymorphisms of complement component C4 in human systemic lupus erythematosus (SLE) low copy number is a risk factor for and high copy number is a protective factor against SLE susceptibility in European Americans.Yang Y., Chung E.K., Wu Y.L., Savelli S.L., Nagaraja H.N., Zhou B., Hebert M., Jones K.N., Shu Y., Kitzmiller K., Blanchong C.A., McBride K.L., Higgins G.C., Rennebohm R.M., Rice R.R., Hackshaw K.V., Roubey R.A., Grossman J.M., Tsao B.P., Birmingham D.J., Rovin B.H., Hebert L.A., Yu C.Y.Am. J. Hum. Genet. 80:1037-1054(2007)

NCBI and Uniprot Product Information

• NCBI GI #: 178557739
• NCBI GeneID: 721
• NCBI Accession #: NP_001002029.3
• NCBI GenBank Nucleotide #: NM_001002029.3
• UniProt Accession #: P0C0L5; P01028; P78445; Q13160; Q13906; Q14033; Q14835; Q6U2E9; Q6U2G1; Q6U2I5; Q6U2L1; A2BHY4
• Molecular Weight: 35.1 kDa
• NCBI Official Full Name: complement C4-B preproprotein
• NCBI Official Synonym Full Names: complement component 4B (Chido blood group)
• NCBI Official Symbol: C4B
• NCBI Official Synonym Symbols: CH; C4F; CO4; C4B1; C4B2; C4B3; C4B5; C4BD; C4B12; C4B_2; CPAMD3
• NCBI Protein Information: complement C4-B
• UniProt Protein Name: Complement C4-B
• UniProt Gene Name: C4B
• UniProt Synonym Gene Names: CO4; CPAMD3
• UniProt Entry Name: CO4B_HUMAN