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Arginase-I (Liver Type) Human, Mouse Monoclonal Antibody, Clone: 6G3

  • Regulatory status:RUO
  • Type:Monoclonal Antibody
  • Other names:EC, L-arginine aminohydrolase
  • Species:Human
Cat. No. Size Price
1 pc / 2 - 5 pcs / 6+ pcs

RD182028100 0.1 mg $300 / $266 / On request
PubMed Product Details
Technical Data


Monoclonal Antibody


Western blotting, ELISA, Immunohistochemistry

Antibodies Applications

Source of Antigen

E. coli








The antibody is a mouse monoclonal antibody against recombinant Human Arginase – liver type arginase.

Species Reactivity

Human. Not yet tested in other species.

Purification Method

Affinity chromatography on a column with immobilized protein A.

Antibody Content

0.1 mg (determined by BCA method, BSA was used as a standard)


The antibody is lyophilized in 0.05 M phosphate buffer, 0.1 M NaCl, pH 7.2.


Add 0.2 ml of deionized water and let the lyophilized pellet dissolve completely. Slight turbidity may occur after reconstitution, which does not affect activity of the antibody. In this case clarify the solution by centrifugation.


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


The lyophilized antibody remains stable and fully active until the expiry date when stored at -20°C. Aliquot the product after reconstitution to avoid repeated freezing/thawing cycles and store frozen at -80°C. Reconstituted antibody can be stored at 4°C for a limited period of time; it does not show decline in activity after one week at 4°C.

Quality Control Test

SDS PAGE - to determine purity of the antibody BCA - to determine quantity of the antibody


This product is for research use only.


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 (1)


  • 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 of smoking 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
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)
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