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Arginase 1

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Arginase-1 is a protein enzyme found in various tissues. It plays a key role in the urea cycle by catalyzing the hydrolysis of L-arginine to L-ornithine and urea. This enzymatic activity is essential for the regulation of arginine levels and nitrogen metabolism within cells.

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Lab products found in correlation

β actin, by Abcam (2 mentions) Pstat3, by BD (2 mentions) Bis tris gel, by Thermo Fisher Scientific (2 mentions) In situ apoptosis detection kit, by Merck Group (1 mentions) F4 80, by Thermo Fisher Scientific (1 mentions) Cy3 conjugated smooth muscle actin, by Merck Group (1 mentions) Cd11b af700, by Thermo Fisher Scientific (1 mentions) Cd45 30 f11, by Thermo Fisher Scientific (1 mentions) Gapdh, by Cell Signaling Technology (1 mentions) Hybond p, by GE Healthcare (1 mentions) Horseradish peroxidase labeled secondary antibody, by Merck Group (1 mentions) Tgf β1, by BD (1 mentions) Ac 74, by Merck Group (1 mentions) Immobilon fl, by Merck Group (1 mentions) Sc 47778, by Santa Cruz Biotechnology (1 mentions) P stat3 y705, by Cell Signaling Technology (1 mentions) Stat3, by Cell Signaling Technology (1 mentions) Isotype control, by Thermo Fisher Scientific (1 mentions) P stat3, by Thermo Fisher Scientific (1 mentions) C myc, by Santa Cruz Biotechnology (1 mentions)

Close spelling variants of this product

Anti-Arginase 1 antibody Anti-Arginase-1 (BD610708) antibody Mouse monoclonal anti-human Arginase I antibody Mouse anti-arginase-1 Mouse monoclonal Arginase-1 Anti-arginase-1 Mouse anti-arginase 1 (N-20)

15 protocols using arginase 1

1

Histological Analysis of Mammary Tissues

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Tissues were processed as described previously [4 (link)]. Briefly, mammary glands, lungs, and liver samples were fixed, paraffin embedded, and cut into in 4 μm sections. Sections were stained with hematoxylin and eosin for routine histological examination. Whole mount analysis was completed as previously described [4 (link)].
For BrdU analysis, mice were injected with 5-bromo-2′-deoxyuridine (BrdU) 2 hours prior to euthanasia and immunohistochemistry was performed as previously described [54 (link)]. In Situ Apoptosis Detection Kit (EMD Millipore, Billerica, MA) was used according to the manufacturer's instructions for TUNEL staining. For both proliferation and apoptosis, quantification of positive epithelial cells at 400X magnification was completed by counting at least three independent fields per slide from at least three different tumors from each group.
Standard procedures were used for staining of F4/80 (eBiosciences, San Diego, CA), Arginase I (BD), iNOS (BD Biosciences) and CD8a (BD Biosciences), with the number of positive cells counted in at least three independent fields per slide from at least three different tumors per group. CD31 (Dako, Carpinteria, CA) was stained using standard procedures and quantified using image J software to calculate area stained in at least three independent fields per slide from at least three different tumors from each group.
Benight N.M., Wagh P.K., Zinser G.M., Peace B.E., Stuart W.D., Vasiliauskas J., Pathrose P., Starnes S.L, & Waltz S.E. (2015). HGFL supports mammary tumorigenesis by enhancing tumor cell intrinsic survival and influencing macrophage and T-cell responses. Oncotarget, 6(19), 17445-17461.
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2

Modulating Immune Responses with Antibodies

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Depleting anti-CD8 antibody (YTS 169.4 – BioXCell, West Lebanon, NH) was given i.p. 250µg one day before treatment and again 1 week later. Blocking anti-TNFα antibody (XT3.11 – BioXCell) was given i.p. 500µg 6hrs before treatment and again 48hrs later. Fluorescently-conjugated antibodies CD11b-AF700, Gr1-PE-Cy7, IA (MHC class II)-APC-Cy7, CD4-FITC (HlS51), CD8-PerCP-Cy5.5(53.6.7), IFNγ-APC(XMG1.2) were purchased from Ebioscience (San Diego, CA). Western blotting antibodies used include Arginase I (BD biosciences, San Jose, CA), iNOS (Cayman Chemical Corporation, Ann Arbor, MI), GAPdH, anti-mouse-HRP, and anti-rabbit-HRP (all Cell Signaling Technology, Danvers, MA). Immunohistology antibody to F4/80 was purchased from AdB Serotec (Raleigh NC); CD3, CD31 from Spring Bio (Pleasanton, CA); Cy3 conjugated Smooth Muscle Actin from Sigma (St. Louis MO); CD45 (30-F11) from Ebioscience; and unconjugated anti-STING from Cell Signaling.
Baird J.R., Friedman D., Cottam B., Dubensky TW J.r., Kanne D.B., Bambina S., Bahjat K., Crittenden M.R, & Gough M.J. (2015). Radiation therapy combined with novel STING-targeting oligonucleotides results in regression of established tumors. Cancer research, 76(1), 50-61.
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3

Western Blot Protein Detection

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Total protein extracts were eletrophoretically separated in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and blotted onto polyvinylidene difluoride (Hybond-P; GE Healthcare, Little Chalfont, U.K.), membrane according to standard procedures as described by others 24 (link)–26 (link). The antibodies used were: anti-galectin-3 (M3/38 Hybridoma), anti-VEGF (1:500; Santa Cruz Biotechnology, Santa Cruz, CA), anti-VEGFR2, and its anti-phosphorylated form, pY1214-VEGFR2 (1:500; Invitrogen, Life Technologies, Carlsbad, CA), TGFβ1 (1:3000; BD Biosciences—Pharmingen in San Diego, CA) or Arginase I (1:1000; BD Biosciences—Pharmingen); followed by specific HRP (horseradish peroxidase)-labeled secondary antibody (Sigma-Aldrich, 1:4000). The procedures are detailed in the supporting information section.
Machado C.M., Andrade L.N., Teixeira V.R., Costa F.F., Melo C.M., dos Santos S.N., Nonogaki S., Liu F.T., Bernardes E.S., Camargo A.A, & Chammas R. (2014). Galectin-3 disruption impaired tumoral angiogenesis by reducing VEGF secretion from TGFβ1-induced macrophages. Cancer Medicine, 3(2), 201-214.
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4

Immunoblotting Arginase I and β-Actin

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Western blot analysis was performed using standard protocols. Proteins were electrophoresed in 8% TrisGlycine gels, transferred to polyvinylidene difluoride membranes, and immunoblotted with antibodies against arginase I (19; BD Biosciences) and β-actin (AC-74; Sigma).
Hossain F., Al-Khami A.A., Wyczechowska D., Hernandez C., Zheng L., Reiss K., Del Valle L., Trillo-Tinoco J., Maj T., Zou W., Rodriguez P.C, & Ochoa A.C. (2015). Inhibition of Fatty Acid Oxidation Modulates Immunosuppressive Functions of Myeloid-Derived Suppressor Cells and Enhances Cancer Therapies. Cancer immunology research, 3(11), 1236-1247.
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5

Immunoblot Analysis of Cellular Proteins

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Cells were sonicated or lysed in lysis buffer containing 150 mM sodium chloride, 50 mM Tris-HCl and 5 mM EDTA supplemented with 1% Triton X-100, and protease inhibitor cocktail. Samples were subjected to SDS-PAGE. After transfer of the proteins to PVDF (Immobilon-FL, Millipore) and blocking with 50% Odyssey blocking buffer in PBS the membranes were incubated overnight at 4 °C with primary antibodies against iNOS (1:250; BD Biosciences), arginase-1 (1:500; BD Biosciences) and actin (1:1000; Sigma). Appropriate secondary IRDye-conjugated antibodies were applied for 1 h followed by detection on the Odyssey Infrared Imaging system (Li-Cor Biosciences). Quantification was performed with Scion Image software.
Sikkema A.H., Stoffels J.M., Wang P., Basedow F.J., Bulsink R., Bajramovic J.J, & Baron W. (2018). Fibronectin aggregates promote features of a classically and alternatively activated phenotype in macrophages. Journal of Neuroinflammation, 15, 218.
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6

Protein Expression Analysis Protocol

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Cells were homogenized in RIPA buffer as previously described (30 (link)). Antibodies for analyses included: RON (1:200, sc-322, Santa Cruz Biotechnology), Arginase-1 (1:1000, 610708, BD Transduction Labs), p-STAT3 (Y705) (1:800, 9145S, Cell Signaling Technology), STAT3 (1:500, 9139S, Cell Signaling Technology), and C4-actin (ACTIN) (1:40,000, Cincinnati Children’s Hospital Medical Center; 1:5000, sc-47778, Santa Cruz Biotechnology).
Sullivan C., Brown N.E., Vasiliauskas J., Pathrose P., Starnes S.L, & Waltz S.E. (2020). Prostate Epithelial RON Signaling Promotes M2 Macrophage Activation to Drive Prostate Tumor Growth and Progression. Molecular cancer research : MCR, 18(8), 1244-1254.
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7

Multiparametric Flow Cytometry Analysis

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Fluorescent antibodies against Gr1 (Miltenyi Biotech), CD11b (BD), iNOS (BD), Arginase-1 (BD), c-Myc (SantaCruz Biotech), MUC1 (BD), pSTAT3 (eBioscience), CD4, CD8, CD25, FoxP3, CD3, TCR, CD69, IL-2R (BD) and isotype control (eBioscience) were used at a concentration of 1 µg/sample.
Sahraei M., Bose M., Sanders J.A., De C., DasRoy L., Nath S., Brouwer C.R, & Mukherjee P. (2021). Repression of MUC1 Promotes Expansion and Suppressive Function of Myeloid-Derived Suppressor Cells in Pancreatic and Breast Cancer Murine Models. International Journal of Molecular Sciences, 22(11), 5587.
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8

Macrophage Polarization Protein Analysis

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Peritoneal macrophages were cultured in DMEM media containing 10% FBS only (control) or with recombinant mouse IFNγ (50 ng/ml, EMD Millipore, Billerica, MA) or with recombinant mouse IL-4 (20 ng/ml, Thermo Scientific, Rockford, IL) for 24 or 48 h. Proteins were resolved by electrophoresis (50 μg/well) and analyzed by Western blot using antibodies to CCR2 (Epitomics, Burlingame, CA), Ym1 (StemCell Technologies, Vancouver, Canada), or arginase 1 (Arg1; BD Bioscience, San Jose, CA) and β-actin (Abcam).
Babaev V.R., Hebron K.E., Wiese C.B., Toth C.L., Ding L., Zhang Y., May J.M., Fazio S., Vickers K.C, & Linton M.F. (2014). Macrophage deficiency of Akt2 reduces atherosclerosis in Ldlr null mice. Journal of Lipid Research, 55(11), 2296-2308.
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9

Western Blot Analysis of Arg1 and CD3ζ

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Protein extract was obtained by lysing PBMC or purified CD3 cells using Mammalian Protein Extraction Reagent (Thermo Scientific) supplemented with 0.1% SDS and Halt Protease and Phosphatase Inhibitor. Twenty μg (20μg) of protein was loaded into an 8% Bis-tris gel (Life Technologies) for detection of Arg1, or a 4-12% Bis-tris gel for detection of CD3ζ. After transfer to a PVDF membrane it was blocked with 5% milk for 1h and incubated overnight with appropriate primary antibodies. Primary anti-human antibodies included arginase-1 (BD Biosciences), phospho CD3ζ (Abcam), CD3ζ (Abcam), and β-actin. Following incubation HRP was detected using ECL Western Blotting Substrate (Thermo Scientific).
Dean M.J., Ochoa J.B., Sanchez-Pino M.D., Zabaleta J., Garai J., Del Valle L., Wyczechowska D., Baiamonte L.B., Philbrook P., Majumder R., Vander Heide R.S., Dunkenberger L., Thylur R.P., Nossaman B., Roberts W.M., Chapple A.G., Wu J., Hicks C., Collins J., Luke B., Johnson R., Koul H.K., Rees C.A., Morris C.R., Garcia-Diaz J, & Ochoa A.C. (2021). Severe COVID-19 Is Characterized by an Impaired Type I Interferon Response and Elevated Levels of Arginase Producing Granulocytic Myeloid Derived Suppressor Cells. Frontiers in Immunology, 12, 695972.
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10

Immunofluorescence Staining of Wound Macrophages

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Cytospin smears from wound mϕ suspension were fixed in cell fixation buffer (BD Cytofix, BD Biosciences, CA) for 10 min. Following fixation, wound mϕ were washed, blocked in 10% NGS for 30 min and were incubated in primary antibodies for Arginase-1 (1:100; BD Biosciences) and iNOS (1:100; Abcam,). Fluorescence tagged secondary antibody detection was performed with Alexa Fluor 568 secondary antibody (1:200, Life Technologies) as described previously25 (link).
Das A., Datta S., Roche E., Chaffee S., Jose E., Shi L., Grover K., Khanna S., Sen C.K, & Roy S. (2018). Novel mechanisms of Collagenase Santyl Ointment (CSO) in wound macrophage polarization and resolution of wound inflammation. Scientific Reports, 8, 1696.
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