Arginase I, Human Liver-Type BioAssay(TM) ELISA Kit

This ELISA is a double monoclonal sandwich enzyme immunoassay for the quantitative measurement of human liver-type arginase in serum and cerebrospinal fluid (CSF). It is intended for in vitro and research use.\n\nFeatures\nпїЅ The total assay time is less than three hours.\nпїЅ The kit measures total serum liver-type arginase.\nпїЅ Quality controls are human serum based. No animal sera are used.\nпїЅ Serum samples require very careful preparation.\nThe erythrocytes have to be spun down immediately (within a few seconds) after taking blood to avoid hemolysis and contamination of the sample with erythrocyte arginase.\n\nArginase [EC 3.5.3.1; L-arginine aminohydrolase] is an enzyme that hydrolyzes L-arginine to L-ornithine and urea in the urea cycle. Two forms of arginase exist which are designated arginase I and arginase II. Liver-type arginase I is expressed primarily in the liver and to some extent in the erythrocytes. Arginase II is expressed in many extrahepatic tissues such as the brain, spinal cord, kidney, small intestine, and mammary gland. Although arginase I and arginase II have similar enzyme activities, they have different pI, immunological reactivity and are encoded by different genes. Human arginase I is a 35kD protein circulating in blood probably as a homotrimer.\n\nCirculating liver-type arginase was clinically used as a liver specific marker which may reflect not only early occurrence of liver injury but also early termination of liver injury. The measurement of liver-type arginase is clinically applicable for monitoring conditions of patients with liver disorders or pre- and postoperative conditions of patients who received partial hepatectomy with quicker normalization in comparison with aminotransferases (ALT and AST). Recently, the arginase I gene was found to be one of the most prominent among asthma genes. In situ hybridization demonstrated marked staining of arginase I in submucosal inflammatory lesions and arginase activity increased in allergen-challenged lungs. \n\nFinally, it was found that arginase I was the most significantly up-regulated protein in the murine spinal cord during experimental autoimmune encephalomyelitis. The results indicated that arginase I played important roles in autoimmune inflammation in the central nervous system.\n\nTime: <3 hours.\n\nRange: 5-320ng/ml\n\nSensitivity: 0.5ng/ml.\n\nKit Components:\nA3340-14F Microtiter Plate 1x96 wells Coated with capture Anti-Arginase Antibody,\nA3340-14G Mab (HRP) 1x13ml\n*A3340-14H Calibrator 2x 1 vial\n*A3340-14J Quality Control, High 2x 1 vial\n*A3340-14K Quality Control, Low 2x 1 vial\nA3340-14L Standard Diluent,1x2ml\nA3340-14M Dilution Buffer 1x13ml\nA3340-14N Wash Buffer 10X ,1x100ml\nA3340-14P Substrate (TMB) Solution 1x13ml\nA3340-14Q Stop Solution (0.2M H2SO4) 1x13ml\n\nStorage and Stability:\nStore *A3340-14H, A3340-14J and A3340-14K at -20 degrees C. Store other components at 4 degrees C. Stable for 3 months For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.

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SPECIFICATIONS

Catalog Number

A3340-14

Size

1Kit

References

1. Ikemoto M, et al., A useful ELISA system for human liver-type arginase, and its utility in diagnosis of liver diseases. Clin Biochem. 34, 455-461 (2001). 2. Ikemoto M, et al., Liver-type arginase in serum during and after liver transplantation: a novel index in monitoring conditions of the liver graft and its clinical significance. Clin Chim Acta. 271, 11-23 (1998). 3. Zimmermann N, et al., Dissection of experimental asthma with DNA microarray analysis identifies arginase in asthma pathogenesis. J Clin Invest. 111, 1863-1874 (2003). 4. Vercelli D: Arginase: marker, effector, or candidate gene for asthma? J Clin Invest. 111, 1815-1817 (2003). 5. Xu L, Hilliard B, et al., Arginase and immune inflammation in the central nervous system. Immunology. 110 , 141-148 (2003). 6. Roikhel VM, et al., Alterations of arginase activity in scrapie-infected mice and in amyotrophic lateral sclerosis. Acta Virol. 34, 545-553 (1990). 7. Ikemoto M, et al., Expression of human liver arginase in Escherichia coli. Purification and properties of the product. Biochem J. 270, 697-703 (1990). 8. Lavulo LT, et al., Subunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid. J Biol Chem. 276, 14242-14248. (2001). 9. Dillon BJ, et al., Biochemical characterization of the arginine degrading enzymes arginase and arginine deiminase and their effect on nitric oxide production. Med Sci Monit. 8, :BR248-253 (2002).