Carbonic anhydrase 1 Recombinant Protein | CA1 recombinant protein

Recombinant Human Carbonic anhydrase 1

Cat. Num. AAA950454

• Gene Names: CA1; CAB; CA-I; Car1; HEL-S-11
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Carbonic anhydrase 1; Recombinant Human Carbonic anhydrase 1; Carbonate dehydratase I; Carbonic anhydrase B; CAB; Carbonic anhydrase I; CA-I; CA1 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: 2-261aa; Full Length
• Sequence: ASPDWGYDDKNGPEQWSKLYPIANGNNQSPVDIKTSETKHDTSLKPISVSYNPATAKEIINVGHSFHVNFEDNDNRSVLKGGPFSDSYRLFQFHFHWGSTNEHGSEHTVDGVKYSAELHVAHWNSAKYSSLAEAASKADGLAVIGVLMKVGEANPKLQKVLDALQAIKTKGKRAPFTNFDPSTLLPSSLDFWTYPGSLTHPPLYESVTWIICKESISVSSEQLAQFRSLLSNVEGDNAVPMQHNNRPTQPLKGRTVRASF
• Sequence Length: 261

• 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 CA1 recombinant protein

Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea.

Product Categories/Family for CA1 recombinant protein

Cardiovascular

References

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)

NCBI and Uniprot Product Information

• NCBI GI #: 192447430
• NCBI GeneID: 759
• NCBI Accession #: NP_001122301.1
• NCBI GenBank Nucleotide #: NM_001128829.3
• UniProt Accession #: P00915
• Molecular Weight: 30.7 kDa
• NCBI Official Full Name: carbonic anhydrase 1 isoform a
• NCBI Official Synonym Full Names: carbonic anhydrase I
• NCBI Official Symbol: CA1
• NCBI Official Synonym Symbols: CAB; CA-I; Car1; HEL-S-11
• NCBI Protein Information: carbonic anhydrase 1
• UniProt Protein Name: Carbonic anhydrase 1
• Protein Family: Carbonic anhydrase
• UniProt Gene Name: CA1
• UniProt Synonym Gene Names: CAB; CA-I
• UniProt Entry Name: CAH1_HUMAN

NCBI Description

Carbonic anhydrases (CAs) are a large family of zinc metalloenzymes that catalyze the reversible hydration of carbon dioxide. They participate in a variety of biological processes, including respiration, calcification, acid-base balance, bone resorption, and the formation of aqueous humor, cerebrospinal fluid, saliva and gastric acid. They show extensive diversity in tissue distribution and in their subcellular localization. This CA1 gene is closely linked to the CA2 and CA3 genes on chromosome 8. It encodes a cytosolic protein that is found at the highest level in erythrocytes. Allelic variants of this gene have been described in some populations. Alternative splicing results in multiple transcript variants. [provided by RefSeq, May 2014]

Uniprot Description

CA1: Reversible hydration of carbon dioxide. Can hydrates cyanamide to urea. Belongs to the alpha-carbonic anhydrase family.

Protein type: Lyase; Energy Metabolism - nitrogen; EC 4.2.1.1

Chromosomal Location of Human Ortholog: 8q21.2

Cellular Component: cytosol

Molecular Function: arylesterase activity; carbonate dehydratase activity; hydro-lyase activity; protein binding; zinc ion binding

Biological Process: bicarbonate transport; one-carbon compound metabolic process