Carbonic Anhydrase 1 (CA1) Human Recombinant Protein

MBS950454 is a recombinant protein targeting CA1. Also known as Recombinant Human Carbonic anhydrase 1. Host: E Coli or Yeast or Baculovirus or Mammalian Cell. Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea.

Human carbonic anhydrase I cDNA.Barlow J.H., Lowe N., Edwards Y.H., Butterworth P.H.W.Nucleic Acids Res. 15:2386-2386(1987) Structure and methylation patterns of the gene encoding human carbonic anhydrase I.Lowe N., Brady H.J.M., Barlow J.H., Sowden J.C., Edwards M., Butterworth P.H.W.Gene 93:277-283(1990) Primary structure of human B erythrocyte carbonic anhydrase. 3. Sequence of CNBr fragment I and III (residues 149-260) .Giraud N., Marriq C., Laurent-Tabusse G.Biochimie 56:1031-1043(1974) Amino acid sequence of human erythrocyte carbonic anhydrase B.Andersson B., Nyman P.O., Strid L.Biochem. Biophys. Res. Commun. 48:670-677(1972) Human carbonic anhydrases. XI. The complete primary structure of carbonic anhydrase B.Lin K.-T.D., Deutsch H.F.J. Biol. Chem. 248:1885-1893(1973) Human carbonic anhydrases. XII. The complete primary structure of the C isozyme.Lin K.-T.D., Deutsch H.F.J. Biol. Chem. 249:2329-2337(1974) Carbonic anhydrase catalyzes cyanamide hydration to urea is it mimicking the physiological reaction?Briganti F., Mangani S., Scozzafava A., Vernaglione G., Supuran C.T.J. Biol. Inorg. Chem. 4:528-536(1999) Carbonic anhydrase activators. Activation of isozymes I, II, IV, VA, VII, and XIV with l- and d-histidine and crystallographic analysis of their adducts with isoform II engineering proton-transfer processes within the active site of an enzyme.Temperini C., Scozzafava A., Vullo D., Supuran C.T.Chemistry 12:7057-7066(2006) Carbonic anhydrase activators. Activation of isoforms I, II, IV, VA, VII, and XIV with L- and D-phenylalanine and crystallographic analysis of their adducts with isozyme II stereospecific recognition within the active site of an enzyme and its consequences for the drug design.Temperini C., Scozzafava A., Vullo D., Supuran C.T.J. Med. Chem. 49:3019-3027(2006) Carbonic anhydrase activators L-Adrenaline plugs the active site entrance of isozyme II, activating better isoforms I, IV, VA, VII, and XIV.Temperini C., Innocenti A., Scozzafava A., Mastrolorenzo A., Supuran C.T.Bioorg. Med. Chem. Lett. 17:628-635(2007) A thiabendazole sulfonamide shows potent inhibitory activity against mammalian and nematode alpha-carbonic anhydrases.Crocetti L., Maresca A., Temperini C., Hall R.A., Scozzafava A., Muehlschlegel F.A., Supuran C.T.Bioorg. Med. Chem. Lett. 19:1371-1375(2009) Non-zinc mediated inhibition of carbonic anhydrases coumarins are a new class of suicide inhibitors.Maresca A., Temperini C., Vu H., Pham N.B., Poulsen S.-A., Scozzafava A., Quinn R.J., Supuran C.T.J. Am. Chem. Soc. 131:3057-3062(2009) Crystal structure of human carbonic anhydrase XIII and its complex with the inhibitor acetazolamide.Di Fiore A., Monti S.M., Hilvo M., Parkkila S., Romano V., Scaloni A., Pedone C., Scozzafava A., Supuran C.T., De Simone G.Proteins 74:164-175(2009) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Structure of human carbonic anhydrase B. I. Crystallization and heavy atom modifications.Kannan K.K., Fridborg K., Bergsten P.C., Liljas A., Loevgren S., Petef M., Strandberg B., Waara I., Adler L., Falkbring S.O., Goethe P.O., Nyman P.O.J. Mol. Biol. 63:601-604(1972) Crystal structure of human erythrocyte carbonic anhydrase B. Three-dimensional structure at a nominal 2.2-A resolution.Kannan K.K., Notstrand B., Fridborg K., Loevgren S., Ohlsson A., Petef M.Proc. Natl. Acad. Sci. U.S.A. 72:51-55(1975) Structure, refinement, and function of carbonic anhydrase isozymes refinement of human carbonic anhydrase I.Kannan K.K., Ramanadham M., Jones T.A.Ann. N. Y. Acad. Sci. 429:49-60(1984) Differences in anionic inhibition of human carbonic anhydrase I revealed from the structures of iodide and gold cyanide inhibitor complexes.Kumar V., Kannan K.K., Sathyamurthi P.Acta Crystallogr. D 50:731-738(1994) Enzyme-substrate interactions. Structure of human carbonic anhydrase I complexed with bicarbonate.Kumar V., Kannan K.K.J. Mol. Biol. 241:226-232(1994) Drug-protein interactions. Refined structures of three sulfonamide drug complexes of human carbonic anhydrase I enzyme.Chakravarty S., Kannan K.K.J. Mol. Biol. 243:298-309(1994) Crystal structure of a zinc-activated variant of human carbonic anhydrase I, CA I Michigan 1 evidence for a second zinc binding site involving arginine coordination.Ferraroni M., Tilli S., Briganti F., Chegwidden W.R., Supuran C.T., Wiebauer K.E., Tashian R.E., Scozzafava A.Biochemistry 41:6237-6244(2002) Carbonic anhydrase activators the first X-ray crystallographic study of an adduct of isoform I.Temperini C., Scozzafava A., Supuran C.T.Bioorg. Med. Chem. Lett. 16:5152-5156(2006) Ultrahigh resolution crystal structures of human carbonic anhydrases I and II complexed with 'two-prong' inhibitors reveal the molecular basis of high affinity.Jude K.M., Banerjee A.L., Haldar M.K., Manokaran S., Roy B., Mallik S., Srivastava D.K., Christianson D.W.J. Am. Chem. Soc. 128:3011-3018(2006) Phosph(on) ate as a zinc-binding group in metalloenzyme inhibitors X-ray crystal structure of the antiviral drug foscarnet complexed to human carbonic anhydrase I.Temperini C., Innocenti A., Guerri A., Scozzafava A., Rusconi S., Supuran C.T.Bioorg. Med. Chem. Lett. 17:2210-2215(2007) Structural analysis of charge discrimination in the binding of inhibitors to human carbonic anhydrases I and II.Srivastava D.K., Jude K.M., Banerjee A.L., Haldar M., Manokaran S., Kooren J., Mallik S., Christianson D.W.J. Am. Chem. Soc. 129:5528-5537(2007) Population genetic studies of the Philippine Negritos. III. Identification of the carbonic anhydrase-1 variant with CA1 Guam.Omoto K., Ueda S., Goriki K., Takahashi N., Misawa S., Pagaran I.G.Am. J. Hum. Genet. 33:105-111(1981) Marked zinc activation of ester hydrolysis by a mutation, 67-His (CAT) to Arg (CGT) , in the active site of human carbonic anhydrase I.Chegwidden W.R., Wagner L.E., Venta P.J., Bergenhem N.C.H., Yu Y.-S.L., Tashian R.E.Hum. Mutat. 4:294-296(1994)

Small volumes of CA1 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.