ZA was sourced from Novartis Pharma AG Basel, Switzerland. Monoclonal antibodies against human CD25-PE were purchased from eBioscience (San Diego, CA, USA), CD69-FITC was sourced from BD Biosciences (San Jose, CA, USA); the secondary antibody goat anti-mouse IgG FITC was sourced from Merck Millipore (Billerica, MA); and human CCL2/MCP1, human CCL5/RANTES, anti-CCL2 antibody, and anti-CCL5 antibody were sourced from R & D Systems (Minneapolis MN). The triple negative breast cancer cell lines MDA-MB-231 and MDA-MB-468 were purchased from Food Industry Research and Development Institute (FIRDI) and Culture Collection and Research Center (CCRC, Taiwan, ROC). Both cell line were cultured with DMEM medium (Gibco®, Grand Island, NY, USA) containing 10% fetal bovine serum (FBS; Biological Industries, Kibbutz Beit HaEmek, Israel).
Anti ccl5 antibody
Manufactured by R&D Systems
Sourced in United States
The Anti-CCL5 antibody is a laboratory research tool designed to detect and measure levels of the CCL5 protein in biological samples. CCL5, also known as RANTES, is a chemokine that plays a role in immune cell recruitment and activation. This antibody can be used in various immunoassay techniques to quantify CCL5 expression in different experimental models or clinical samples.
Automatically generated - may contain errors
Lab products found in correlation
Goat anti mouse igg fitc, by Merck Group (1 mentions)
Cd69 fitc, by BD (1 mentions)
Human ccl5 rantes, by R&D Systems (1 mentions)
Dmem medium, by Thermo Fisher Scientific (1 mentions)
Human ccl2 mcp 1, by R&D Systems (1 mentions)
Anti ccl2 antibody, by R&D Systems (1 mentions)
Oxaliplatin, by Merck Group (1 mentions)
Anti pd l1 antibody, by BioXCell (1 mentions)
Anti gr 1 antibody, by BioXCell (1 mentions)
Transwell plate, by Corning (1 mentions)
Horseradish peroxidase linked anti mouse or anti rabbit igg, by Cell Signaling Technology (1 mentions)
Polyvinylidene difluoride membrane, by Merck Group (1 mentions)
Protease inhibitor cocktail, by Nacalai Tesque (1 mentions)
Anti β actin antibody, by Cell Signaling Technology (1 mentions)
Anti hsp70 antibody, by Cell Signaling Technology (1 mentions)
4 protocols using anti ccl5 antibody
1
Detecting Triple Negative Breast Cancer Markers
2
Evaluating Oxaliplatin Resistance in HCC
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For this study, 6- to 8-week-old male C57BL/6 mice were purchased from SLAC Laboratory Animal Co, Ltd (Shanghai, China). For subcutaneous tumor models, a total of 5 × 106 HCC cells were inoculated into the right flank of the mice. The mice were monitored every 3 days and the tumor volumes were measured using the following formula: length × width2 × 0.5 (mm3). For orthotopic tumor xenograft models, tumors from subcutaneous tumor tissues were minced into 2-mm3 cubes and transplanted to the livers of WT C57BL/6 mice. At the study end point, the weight of each tumor was assessed. For drug treatment, the tumor-bearing mice were treated with 10 mg/kg oxaliplatin (Sigma, St. Louis, MO) intraperitoneally (IP) weekly for up to 21 days. To evaluate the efficacy of PD-L1 and MDSC blockade on oxaliplatin-resistant HCC, Hepa 1-6–OXA–control or Hepa 1-6–OXA–shMyc–bearing mice were treated with anti–Gr-1 antibody (200 μg/mouse, IP, every 3 days; Bio X cell, NH), anti-CCL5 antibody (20 ug/mouse, intratumorally, every 3 days; R&D Systems), or anti–PD-L1 antibody (200 μg, IP, every 3 days; Bio X cell). The control mice were treated with an isotype control antibody (Bio X cell) or vehicle (phosphate-buffered saline). The mice were killed humanely after treatments and the blood, spleen, and tumor samples were collected for analysis.
3
Measuring NK-92 Cell Chemotaxis
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To measure NK-92 cell migration by chemotaxis assay, 2 × 105 NK-92 cells were seeded in the upper chamber of a 24-well Transwell plate with 100 μL serum free-medium, and 600 μL of conditioned media collected from the supernatant of AsPC-1 cells with or without cGAMP stimulation was placed in the lower chamber of the 24-well Transwell plate (5 μm pore size, Corning, USA). The cells were cultured in the incubator at 37°C under 5% CO2 for 8 h. Furthermore, NK-92 cells were pre-incubated with 1 μM anti-CCL5 antibody (R&D, USA) to block CCL5-mediated cell migration. Finally, the number of NK-92 cells that migrated to the lower chamber was counted and the data was presented as a percentage of migration based on total cell input.
4
Western Blot Analysis of Protein Expression
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Cells were harvested using a cell extract solution [50 mM Tris-HCl (pH 7.6), 150 mM NaCl, 1 mM EDTA, 1% TritonX-100, 0.1% Protease Inhibitor Cocktail (Nacalai Tesque, Kyoto, Japan)] and then centrifuged at 4°C, 15,000 × g for 10 min. The supernatant was added with 2× sample buffer [0.1 M Tris-HCl (pH 6.8), 4% sodium dodecyl sulfate (SDS), 20% glycerol, 0.01% bromophenol blue] and 1% 2-mercaptoethanol. The cells were resolved by 10% SDS-polyacrylamide gel electrophoresis. Proteins were transferred onto polyvinylidene difluoride membranes (MERCK Millipore, Billerica, MA, USA). The membranes were blocked with 3% bovine serum albumin in TBS-T at room temperature for 30 min and then incubated at 4°C overnight with primary antibodies, including anti-CCL5 antibody (R&D Systems, 1:1000), anti-HSP70 antibody (Cell Signaling Technology, Danvers, MA, USA, 1:1000), and anti-β-actin antibody (Cell Signaling Technology, 1:1000). The membranes were washed three times with TBS-T for 10 min and then incubated with a secondary antibody [horseradish peroxidase-linked anti-mouse or anti-rabbit IgG (Cell Signaling Technology, 1:5000)] at room temperature for 1 h. The signal for each protein was visualized using enhanced chemiluminescence detection (Nacalai Tesque) and ChemiDoc TM XRS+. Each band was quantified using ImageJ software (https://imagej.nih.gov/ij/).
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