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Manufactured by BioVendor

Arginase Liver Type Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, HRP-labelled antibody
  • Other names:EC, L-arginine aminohydrolase
  • Species:Human
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Cat. No. Size Price

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


Sandwich ELISA, HRP-labelled antibody


Serum, Cerebrospinal fluid

Sample Requirements

25 µl/well


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


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


Dilution Linearity



  • 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)


  • 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


Arginase [EC; 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 (19)


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  • 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
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  • 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
  • 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
  • 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
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Summary References (9)

References to Arginase I

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  • Vercelli D: Arginase: marker, effector, or candidate gene for asthma? J Clin Invest. 111, 1815–1817 (2003).
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