Serum paraoxonase/arylesterase 1 Recombinant Protein | PON1 recombinant protein

Recombinant Human Serum paraoxonase/arylesterase 1

Cat. Num. AAA962256

• Gene Names: PON1; ESA; PON; MVCD5
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Serum paraoxonase/arylesterase 1; Recombinant Human Serum paraoxonase/arylesterase 1; Aromatic esterase 1; A-esterase 1K-45; Serum aryldialkylphosphatase 1; PON1 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: 2-355aa; Full Length of Mature Protein
• Sequence: AKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIETGSEDLEILPNGLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTFTDEDNAMYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLDPYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPPASEVLRIQNILTEEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCEL

• 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 technical support team or email to [email protected] 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 PON1 recombinant protein

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.

Product Categories/Family for PON1 recombinant protein

Cardiovascular

References

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)

NCBI and Uniprot Product Information

• NCBI GI #: 19923106
• NCBI GeneID: 5444
• NCBI Accession #: NP_000437.3
• NCBI GenBank Nucleotide #: NM_000446.5
• UniProt Accession #: P27169; Q16052; Q6B0J6; Q9UCB1; B2RA40
• Molecular Weight: 66.6 kDa
• NCBI Official Full Name: serum paraoxonase/arylesterase 1
• NCBI Official Synonym Full Names: paraoxonase 1
• NCBI Official Symbol: PON1
• NCBI Official Synonym Symbols: ESA; PON; MVCD5
• NCBI Protein Information: serum paraoxonase/arylesterase 1
• UniProt Protein Name: Serum paraoxonase/arylesterase 1
• Protein Family: Serum paraoxonase/arylesterase
• UniProt Gene Name: PON1
• UniProt Synonym Gene Names: PON; A-esterase 1
• UniProt Entry Name: PON1_HUMAN

NCBI Description

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]

Uniprot Description

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