protein

Recombinant Human Serum paraoxonase/arylesterase 1

MBS962256

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Serum paraoxonase/arylesterase 1

Serum paraoxonase/arylesterase 1

Aromatic esterase 1; A-esterase 1K-45; Serum aryldialkylphosphatase 1

serum paraoxonase/arylesterase 1; Serum paraoxonase/arylesterase 1; serum paraoxonase/arylesterase 1; paraoxonase 1; Aromatic esterase 1; A-esterase 1; K-45; Serum aryldialkylphosphatase 1

PON1

PON1; PON1; ESA; PON; MVCD5; PON; A-esterase 1

PON1_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

2-355

355

AKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELP
NCNLVKGIETGSEDLEILPNGLAFISSGLKYPGIKSFNP
NSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGIS
TFTDEDNAMYLLVVNHPDAKSTVELFKFQEEEKSLLHLK
TIRHKLLPNLNDIVAVGPEHFYGTNDHYFLDPYLQSWEM
YLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYV
YIAELLAHKIHVYEKHANWTL

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Cardiovascular

Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation.

Characterization of cDNA clones encoding rabbit and human serum paraoxonase the mature protein retains its signal sequence.Hassett C., Richter R.J., Humbert R., Chapline C., Crabb J.W., Omiecinski C.J., Furlong C.E.Biochemistry 30:10141-10149(1991) Molecular basis for the polymorphic forms of human serum paraoxonase/arylesterase glutamine or arginine at position 191, for the respective A or B allozymes.Adkins S., Gan K.N., Mody M., La Du B.N.Am. J. Hum. Genet. 52:598-608(1993) Studies on human serum paraoxonase/arylesterase.La Du B.N., Adkins S., Kuo C.L., Lipsig D.Chem. Biol. Interact. 87:25-34(1993) Human and rabbit paraoxonases purification, cloning, sequencing, mapping and role of polymorphism in organophosphate detoxification.Furlong C.E., Costa L.G., Hassett C., Richter R.J., Sundstrom J.A., Adler D.A., Disteche C.M., Omiecinski C.J., Chapline C., Crabb J.W.Chem. Biol. Interact. 87:35-48(1993) Structural organization of the human PON1 gene.Clendenning J.B., Humbert R., Green E.D., Wood C., Traver D., Furlong C.E.Genomics 35:586-589(1996) Differential expression of a cDNA clone in human liver versus hepatic cancer -- highly homologous to aryl-dialkyl-phosphatase.Wang K.K., Wan D.F., Qiu X.K., Lu P.X., Gu J.R.Cell Res. 7:79-90(1997) Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) SeattleSNPs variation discovery resourceThe DNA sequence of human chromosome 7.Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.Nature 424:157-164(2003) Human chromosome 7 DNA sequence and biology.Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.Science 300:767-772(2003)

19923106

NP_000437.3

NM_000446.5

P27169

67kD

Metabolic Pathways (132956); Phase I, Non P450 Pathway (198854)

The enzyme encoded by this gene is an arylesterase that mainly hydrolyzes paroxon to produce p-nitrophenol. Paroxon is an organophosphorus anticholinesterase compound that is produced in vivo by oxidation of the insecticide parathion. Polymorphisms in this gene are a risk factor in coronary artery disease. The gene is found in a cluster of three related paraoxonase genes at 7q21.3. [provided by RefSeq, Oct 2008]

PON1: Hydrolyzes the toxic metabolites of a variety of organophosphorus insecticides. Capable of hydrolyzing a broad spectrum of organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. Mediates an enzymatic protection of low density lipoproteins against oxidative modification and the consequent series of events leading to atheroma formation. Genetic variation in PON1 is associated with susceptibility to microvascular complications of diabetes type 5 (MVCD5). These are pathological conditions that develop in numerous tissues and organs as a consequence of diabetes mellitus. They include diabetic retinopathy, diabetic nephropathy leading to end-stage renal disease, and diabetic neuropathy. Diabetic retinopathy remains the major cause of new- onset blindness among diabetic adults. It is characterized by vascular permeability and increased tissue ischemia and angiogenesis. Homozygosity for the Leu-54 allele is strongly associated with the development of retinal disease in diabetic patients. Belongs to the paraoxonase family. Protein type: Lipid-binding; Motility/polarity/chemotaxis; EC 3.1.1.81; EC 3.1.1.2; Hydrolase; Secreted, signal peptide; EC 3.1.8.1; Secreted; Phosphatase (non-protein). Chromosomal Location of Human Ortholog: 7q21.3. Cellular Component: extracellular region; extracellular space; intracellular membrane-bound organelle. Molecular Function: aryldialkylphosphatase activity; arylesterase activity; calcium ion binding; phospholipid binding; protein homodimerization activity. Biological Process: aromatic compound catabolic process; carboxylic acid catabolic process; dephosphorylation; organophosphate catabolic process; phosphatidylcholine metabolic process; positive regulation of binding; positive regulation of transporter activity; response to external stimulus; response to nutrient levels; response to toxin. Disease: Microvascular Complications Of Diabetes, Susceptibility To, 5

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

0.05 mg (Baculovirus)

1120

1 mg (E-Coli)

1180