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Manufactured by BioVendor

Paraoxonase 1 Human E. coli

  • Regulatory status:RUO
  • Type:Recombinant protein
  • Source:E. coli
  • Other names:Arylesterase 1, PON 1, Aromatic Esterase 1, A-Esterase 1, K-45, Serum Aryldialkylphosphatase 1
  • Species:Human
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Cat. No. Size Price


RD172279100 0.1 mg
PubMed Product Details
Technical Data

Type

Recombinant protein

Description

Total 362 AA. MW: 40.68 kDa (calculated). UniProtKB acc.no. P27169 (Met1-Leu355). C-terminal His-tag (7 extra AA). Protein identity confirmed by LC-MS/MS.

Amino Acid Sequence

MAKLIALTLLGMGLALFRNHQSSYQTRLNALREVQPVELPNCNLVKGIETGSEDLEILPNGLAFISSGLKYPGIKSFNPNSPGKILLMDLNEEDPTVLELGITGSKFDVSSFNPHGISTFTDEDNAMYLLVVNHPDAKSTVELFKFQEEEKSLLHLKTIRHKLLPNLNDIVAVGPEHFYGTNDHYFLDPYLQSWEMYLGLAWSYVVYYSPSEVRVVAEGFDFANGINISPDGKYVYIAELLAHKIHVYEKHANWTLTPLKSLDFNTLVDNISVDPETGDLWVGCHPNGMKIFFYDSENPPASEVLRIQNILTEEPKVTQVYAENGTVLQGSTVASVYKGKLLIGTVFHKALYCELEHHHHHH

Source

E. coli

Purity

Purity as determined by densitometric image analysis: >90%

SDS-PAGE Gel

12% SDS-PAGE separation of Human PON-1
1. M.W. marker – 14, 21, 31, 45, 66, 97 kDa
2. reduced and boiled sample, 2.5μg/lane
3. non-reduced and non-boiled sample, 2.5μg/lane

Endotoxin

< 1.0 EU/ug

Formulation

Filtered (0.4 μm) and lyophilized from 0.5 mg/mL in 20mM Tris buffer, 50 mM NaCl, pH 7.5

Reconstitution

Add 200µl of deionized water to prepare a working stock solution of approximately 0.5 mg/ml and let the lyophilized pellet dissolve completely. Product is not sterile! Please filter the product by an appropriate sterile filter before using it in the cell culture.

Applications

Western blotting, ELISA

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the lyophilized protein at –80 °C. Lyophilized protein remains stable until the expiry date when stored at –80 °C. Aliquot reconstituted protein to avoid repeated freezing/thawing cycles and store at –80 °C for long term storage. Reconstituted protein can be stored at 4 °C for a week.

Quality Control Test

BCA to determine quantity of the protein.

SDS PAGE to determine purity of the protein.

LAL to determine quantity of endotoxin.

Note

This product is intended for research use only.

Summary

Research topic

Cardiovascular disease, Energy metabolism and body weight regulation, Lipoprotein metabolism, Others

Summary

PON 1 Hydrolyzes organophosphate substrates and lactones, and a number of aromatic carboxylic acid esters. It is found in plasma associated with HDL. It mediates an enzymatic protection of lipoproteins against oxidative modification and thus against atheroma formation. Genetic variation in PON1 is associated with susceptibility to microvascular complications in diabetic patients.

Summary References (11)

References to Paraoxonase 1

  • Costa LG, Vitalone A, Cole TB, Furlong CE. Modulation of paraoxonase (PON1) activity. Biochem Pharmacol. 2005 Feb 15;69 (4):541-50
  • Deakin SP, James RW. Genetic and environmental factors modulating serum concentrations and activities of the antioxidant enzyme paraoxonase-1. Clin Sci (Lond). 2004 Nov;107 (5):435-47
  • Ferre N, Feliu A, Garcia-Heredia A, Marsillach J, Paris N, Zaragoza-Jordana M, Mackness B, Mackness M, Escribano J, Closa-Monasterolo R, Joven J, Camps J. Impaired paraoxonase-1 status in obese children. Relationships with insulin resistance and metabolic syndrome. Clin Biochem. 2013 Dec;46 (18):1830-6
  • Fuhrman B. Regulation of hepatic paraoxonase-1 expression. J Lipids. 2012;2012:684010
  • Gaidukov L, Tawfik DS. High affinity, stability, and lactonase activity of serum paraoxonase PON1 anchored on HDL with ApoA-I. Biochemistry. 2005 Sep 6;44 (35):11843-54
  • Graner M, James RW, Kahri J, Nieminen MS, Syvanne M, Taskinen MR. Association of paraoxonase-1 activity and concentration with angiographic severity and extent of coronary artery disease. J Am Coll Cardiol. 2006 Jun 20;47 (12):2429-35
  • Huang Y, Wu Z, Riwanto M, Gao S, Levison BS, Gu X, Fu X, Wagner MA, Besler C, Gerstenecker G, Zhang R, Li XM, DiDonato AJ, Gogonea V, Tang WH, Smith JD, Plow EF, Fox PL, Shih DM, Lusis AJ, Fisher EA, DiDonato JA, Landmesser U, Hazen SL. Myeloperoxidase, paraoxonase-1, and HDL form a functional ternary complex. J Clin Invest. 2013 Sep 3;123 (9):3815-28
  • Liang KW, Lee WJ, Lee IT, Lee WL, Lin SY, Hsu SL, Wan CJ, Yu CY, Tsai IC, Fu CP, Ting CT, Sheu WH. Persistent elevation of paraoxonase-1 specific enzyme activity after weight reduction in obese non-diabetic men with metabolic syndrome. Clin Chim Acta. 2011 Sep 18;412 (19-20):1835-41
  • Rice NE, Bandinelli S, Corsi AM, Ferrucci L, Guralnik JM, Miller MA, Kumari M, Murray A, Frayling TM, Melzer D. The paraoxonase (PON1) Q192R polymorphism is not associated with poor health status or depression in the ELSA or INCHIANTI studies. Int J Epidemiol. 2009 Oct;38 (5):1374-9
  • Sorenson RC, Bisgaier CL, Aviram M, Hsu C, Billecke S, La Du BN. Human serum Paraoxonase/Arylesterase's retained hydrophobic N-terminal leader sequence associates with HDLs by binding phospholipids : apolipoprotein A-I stabilizes activity. Arterioscler Thromb Vasc Biol. 1999 Sep;19 (9):2214-25
  • Suehiro T, Nakamura T, Inoue M, Shiinoki T, Ikeda Y, Kumon Y, Shindo M, Tanaka H, Hashimoto K. A polymorphism upstream from the human paraoxonase (PON1) gene and its association with PON1 expression. Atherosclerosis. 2000 Jun;150 (2):295-8
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