Select country change
Shopping cart (0 , 0,00 ) Menu Search
Manufactured by BioVendor

Arginase Liver Type Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, HRP-labelled antibody
  • Other names:EC 3.5.3.1, L-arginine aminohydrolase
  • Species:Human
Please select your region to see available products and prices.
Cat. No. Size Price


RD193028000R 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Sandwich ELISA, HRP-labelled antibody

Applications

Serum, Cerebrospinal fluid

Sample Requirements

25 µl/well

Shipping

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

Storage/Expiration

Place the lyophilized Master Standards and Quality Controls at –20 °C after the kit delivery. Store the other kit components at 2–8°C. Under these conditions the kit is stable till the expiry date is over. (See the expiry date indicated on the kit label).

Calibration Curve

Calibration Range

5–320 ng/ml

Limit of Detection

2.7 ng/ml

Intra-assay (Within-Run)

n = 8; CV = 5.8%

Inter-assay (Run-to-Run)

n = 8; CV = 7.8%

Spiking Recovery

87,00%

Dilution Linearity

91,00%

Crossreactivity

  • bovine Non-detectable
  • cat Yes (recommended dilution 1:4)
  • dog Non-detectable
  • goat Non-detectable
  • hamster Non-detectable
  • horse Non-detectable
  • mouse Non-detectable
  • pig Non-detectable
  • rabbit Non-detectable
  • rat Non-detectable
  • sheep Non-detectable
  • chicken Not tested
  • human Yes
  • monkey Yes (recommended dilution 1:4)
Summary

Features

  • It is intended for research use only
  • The total assay time is less than 3 hours
  • The kit measures total Arginase I (Liver-Type) in serum and cerebrospinal fluid (CSF)
  • Assay format is 96 wells
  • Standard is recombinant protein based
  • Serum samples require very careful preparation. The erythrocytes have to be spinned down immediately (within few seconds) after taking blood to avoid hemolysis and contamination of the sample with erythrocyte arginase
  • Components of the kit are provided ready to use, concentrated or lyophilized

Research topic

Asthma and allergic rhinitis, Blood pressure regulation and NO metabolism, Immunology, Oncology, Pulmonary diseases

Summary

Arginase [EC 3.5.3.1; L-arginine aminohydrolase] is an enzyme that hydrolyzes Larginine to L-ornithine and urea in the urea cycle. Two forms of arginase exists which are designed as arginase I and arginase II. Liver-type arginase I is expressed primarily in the liver and to some extend in the erythrocytes. Arginase II is expressed in many extrahepatic tissues, such as 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 35 kDa protein circulating in blood probably as a homotrimer. Circulating 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, arginase I gene was found to be one of the most prominent among astma genes. In situ hybridization demonstrated marked staining of arginase I in submucosal inflammatory lesions and arginase activity increased in allergen challenged lungs. Finally, it was found that both 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.

Product References (18)

References

  • Bekpinar S, Gurdol F, Unlucerci Y, Develi S, Yilmaz A. Serum levels ofarginase I are associated with left ventricular function after myocardialinfarction. Clin Biochem. 2011 Sep;44(13):1090-1093. doi:10.1016/j.clinbiochem.2011.06.003. Epub 2011 Jun 17. PubMed PMID: 21704615. See more on PubMed
  • Dimitriades V, Rodriguez PC, Zabaleta J, Ochoa AC. Arginase I levels aredecreased in the plasma of pediatric patients with atopic dermatitis. Ann AllergyAsthma Immunol. 2014 Sep;113(3):271-5. doi: 10.1016/j.anai.2014.06.010. Epub 2014Jul 11. PubMed PMID: 25027824; PubMed Central PMCID: PMC4517580. See more on PubMed
  • El-Hady SB, Farahat MH, Atfy M, Elhady MA. Nitric oxide metabolites andarginase I levels in β-thalassemic patients: an Egyptian study. Ann Hematol. 2012Aug;91(8):1193-200. doi: 10.1007/s00277-012-1427-0. Epub 2012 Feb 25. PubMedPMID: 22362120. See more on PubMed
  • Gabitass RF, Annels NE, Stocken DD, Pandha HA, Middleton GW. Elevatedmyeloid-derived suppressor cells in pancreatic, esophageal and gastric cancer arean independent prognostic factor and are associated with significant elevation ofthe Th2 cytokine interleukin-13. Cancer Immunol Immunother. 2011Oct;60(10):1419-30. doi: 10.1007/s00262-011-1028-0. Epub 2011 Jun 5. PubMed PMID:21644036; PubMed Central PMCID: PMC3176406. See more on PubMed
  • Giallongo C, Parrinello N, Tibullo D, La Cava P, Romano A, Chiarenza A,Barbagallo I, Palumbo GA, Stagno F, Vigneri P, Di Raimondo F. Myeloid derivedsuppressor cells (MDSCs) are increased and exert immunosuppressive activitytogether with polymorphonuclear leukocytes (PMNs) in chronic myeloid leukemiapatients. PLoS One. 2014 Jul 11;9(7):e101848. doi: 10.1371/journal.pone.0101848. eCollection 2014. PubMed PMID: 25014230; PubMed Central PMCID: PMC4094386. See more on PubMed
  • Grasemann H, Schwiertz R, Grasemann C, Vester U, Racké K, Ratjen F. Decreased systemic bioavailability of L-arginine in patients with cystic fibrosis. RespirRes. 2006 Jun 9;7:87. PubMed PMID: 16764721; PubMed Central PMCID: PMC1526723. See more on PubMed
  • Morris CR, Suh JH, Hagar W, Larkin S, Bland DA, Steinberg MH, Vichinsky EP,Shigenaga M, Ames B, Kuypers FA, Klings ES. Erythrocyte glutamine depletion,altered redox environment, and pulmonary hypertension in sickle cell disease.Blood. 2008 Jan 1;111(1):402-10. Epub 2007 Sep 11. PubMed PMID: 17848621; PubMed Central PMCID: PMC2200820. See more on PubMed
  • Nzoumbou-Boko R, Dethoua M, Gabriel F, Buguet A, Cespuglio R, Courtois P,Daulouède S, Bouteille B, Ngampo S, Mpandzou G, Semballa S, Vincendeau P. Serumarginase, a biomarker of treatment efficacy in human African trypanosomiasis. JClin Microbiol. 2013 Jul;51(7):2379-81. doi: 10.1128/JCM.03371-12. Epub 2013 Apr 3. PubMed PMID: 23554207; PubMed Central PMCID: PMC3697696. See more on PubMed
  • Rodriguez PC, Ernstoff MS, Hernandez C, Atkins M, Zabaleta J, Sierra R, Ochoa AC. Arginase I-producing myeloid-derived suppressor cells in renal cell carcinomaare a subpopulation of activated granulocytes. Cancer Res. 2009 Feb15;69(4):1553-60. doi: 10.1158/0008-5472.CAN-08-1921. Epub 2009 Feb 5. PubMedPMID: 19201693; PubMed Central PMCID: PMC2900845. See more on PubMed
  • Rotondo R, Barisione G, Mastracci L, Grossi F, Orengo AM, Costa R, Truini M,Fabbi M, Ferrini S, Barbieri O. IL-8 induces exocytosis of arginase 1 byneutrophil polymorphonuclears in nonsmall cell lung cancer. Int J Cancer. 2009Aug 15;125(4):887-93. doi: 10.1002/ijc.24448. PubMed PMID: 19431148. See more on PubMed
  • Rotondo R, Bertolotto M, Barisione G, Astigiano S, Mandruzzato S, Ottonello L,Dallegri F, Bronte V, Ferrini S, Barbieri O. Exocytosis of azurophil and arginase1-containing granules by activated polymorphonuclear neutrophils is required toinhibit T lymphocyte proliferation. J Leukoc Biol. 2011 May;89(5):721-7. doi:10.1189/jlb.1109737. Epub 2011 Feb 17. PubMed PMID: 21330347. See more on PubMed
  • Scrimini S, Pons J, Agustí A, Soriano JB, Cosio BG, Torrecilla JA, Núñez B,Córdova R, Iglesias A, Jahn A, Crespi C, Sauleda J. Differential effects ofsmoking and COPD upon circulating myeloid derived suppressor cells. Respir Med.2013 Dec;107(12):1895-903. doi: 10.1016/j.rmed.2013.08.002. Epub 2013 Aug 28.PubMed PMID: 23993707. See more on PubMed
  • Silva MA, Mirza DF, Buckels JA, Bramhall SR, Mayer D, Wigmore SJ, Murphy N,Richards DA. Arginine and urea metabolism in the liver graft: A study usingmicrodialysis in human orthotopic liver transplantation. Transplantation. 2006Nov 27;82(10):1304-11. PubMed PMID: 17130779. See more on PubMed
  • Steggerda SM, Bennett MK, Chen J, Emberley E, Huang T, Janes JR, Li W,MacKinnon AL, Makkouk A, Marguier G, Murray PJ, Neou S, Pan A, Parlati F,Rodriguez MLM, Van de Velde LA, Wang T, Works M, Zhang J, Zhang W, Gross MI.Inhibition of arginase by CB-1158 blocks myeloid cell-mediated immune suppressionin the tumor microenvironment. J Immunother Cancer. 2017 Dec 19;5(1):101. doi:10.1186/s40425-017-0308-4. PubMed PMID: 29254508; PubMed Central PMCID:PMC5735564. See more on PubMed
  • Stejskal D, Vavrousková J, Mares J, Urbánek K. Applications of new laboratory marker assays in neurological diagnoses - a pilot study. Biomed Pap Med Fac Univ Palacky Olomouc Czech Repub. 2005 Dec;149(2):265-6. PubMed PMID: 16601767. See more on PubMed
  • Wu P, Wu D, Ni C, Ye J, Chen W, Hu G, Wang Z, Wang C, Zhang Z, Xia W, Chen Z, Wang K, Zhang T, Xu J, Han Y, Zhang T, Wu X, Wang J, Gong W, Zheng S, Qiu F, Yan J, Huang J. γδT17 cells promote the accumulation and expansion of myeloid-derivedsuppressor cells in human colorectal cancer. Immunity. 2014 May 15;40(5):785-800.doi: 10.1016/j.immuni.2014.03.013. Epub 2014 May 8. PubMed PMID: 24816404; PubMedCentral PMCID: PMC4716654. See more on PubMed
  • Zahradka P, Wright B, Weighell W, Blewett H, Baldwin A, O K, Guzman RP, TaylorCG. Daily non-soy legume consumption reverses vascular impairment due toperipheral artery disease. Atherosclerosis. 2013 Oct;230(2):310-4. doi:10.1016/j.atherosclerosis.2013.07.048. Epub 2013 Aug 6. PubMed PMID: 24075762. See more on PubMed
  • Pinton L, Solito S, Masetto E, Vettore M, Canè S, Puppa AD, Mandruzzato S.Immunosuppressive activity of tumor-infiltrating myeloid cells in patients withmeningioma. Oncoimmunology. 2018 Mar 15;7(7):e1440931. doi:10.1080/2162402X.2018.1440931. eCollection 2018. PubMed PMID: 29900047; PubMedCentral PMCID: PMC5993508. See more on PubMed
Summary References (9)

References to Arginase I

  • Ikemoto M, Tsunekawa S, Awane M, Fukuda Y, Murayama H, Igarashi M, Ngata A, Kasai Y, Totani M: A useful ELISA system for human liver-type arginase, and its utility in diagnosis of liver diseases. Clin Biochem. 34, 455–461 (2001).
  • Ikemoto M, Tsunekawa S, Tanaka K, Tanaka A, Yamaoka Y, Ozawa K, Fukuda Y, Moriyasu F, Totani M, Kasai Y, Mori T, Ueda K: 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).
  • Zimmermann N, King NE, Laporte J, Yang M, Mishra A, Pope SM, Muntuel EE, Witte DP, Pegg AA, Foster PS, Hamid Q, Rothenberg ME: Dissection of experimental asthma with DNA microarray analysis identifies arginase in asthma pathogenesis. J Clin Invest. 111, 1863–1874 (2003).
  • Vercelli D: Arginase: marker, effector, or candidate gene for asthma? J Clin Invest. 111, 1815–1817 (2003).
  • Xu L, Hilliard B, Carmody RJ, Tsabry G, Shin H, Christianson DW, Chen YH: Arginase and immune inflammation in the central nervous system. Immunology. 110, 141–148 (2003).
  • Roikhel VM, Fokina GI, Khokhlov AI, Sobolev SG, Zavalishin IA, Korolev MB, Pogodina VV: Alterations of arginase activity in scrapie-infected mice and in amyotrophic lateral sclerosis. Acta Virol. 34, 545–553 (1990).
  • Ikemoto M, Tabata M, Miyake T, Kono T, Mori M, Totani M, Murachi T: Expression of human liver arginase in Escherichia coli. Purification and properties of the product. Biochem J. 270, 697–703 (1990).
  • Lavulo LT, Sossong TM Jr, Brigham-Burke MR, Doyle ML, Cox JD, Christianson DW, Ash DE: Subunit-subunit interactions in trimeric arginase. Generation of active monomers by mutation of a single amino acid. J Biol Chem. 276, 14242–14248 (2001).
  • Dillon BJ, Holtsberg FW, Ensor CM, Bomalaski JS, Clark MA: 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)
Related Products Docs