H2 db 28 14 8

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H2-Db (28–14–8) is a laboratory equipment product designed for specific biological and scientific applications. It serves as a tool to facilitate precise measurements and analysis. The core function of this product is to provide accurate and reliable data collection for research purposes. No further details or interpretations about its intended use are provided.

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3 protocols using h2 db 28 14 8

Multiparametric Flow Cytometry Analysis

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The following antibodies were used: CD45 (clone 30-F11), CD11b (M1/70), KLRG1 (2F1), CD103 (M290), NKg2a (20d5), Ly6C (AL-21), Ly6G (1A8), PD-L1 (MIH5), I-A/I-E (M5/114), CD11c (HL3), PDCA1 (927), CD64 (X54-5/7.1), B220 (RA3-6B2), CD24 (M1/69), CD4 (GK1.5), CD25 (3C7), CD3 (500A2), NKp46 (29A1.4), TNF-α (MP6-XT22), IFN-γ (XMG1.2), H2-Kb (AF6-88.5), and H2-Db (28–14–8) were from BD Biosciences; Tim3 (RMT3-23), PD-1 (29F.1A12), CD38 (90), Gr-1 (RB6-8C5), CD206 (C068C2), CD68 (FA-11) were from BioLegend; FoxP3 (FJK-16s), T-bet (4B10), GATA-3 (TWAJ), and RORγt (AFKJS-9) were from ThermoFisher Scientific; Granzyme B (REA226) was from Miltenyi; CD8 (KT15) was from MBL. Dead cells were stained with LIVE/DEAD Yellow or Aqua fluorescent reactive dye (Life Technologies) and excluded from analyses. Murine MHC-peptide multimers were from Immudex (Copenhagen, Denmark). Cells were analyzed using an Attune NxT flow cytometer (ThermoFisher Scientific), and results were analyzed with Kaluza (Beckman Coulter) software.

Rossi M., Carboni S., Di Berardino-Besson W., Riva E., Santiago-Raber M.L., Belnoue E, & Derouazi M. (2021). STING Agonist Combined to a Protein-Based Cancer Vaccine Potentiates Peripheral and Intra-Tumoral T Cell Immunity. Frontiers in Immunology, 12, 695056.

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Cytotoxicity Assay for Tumor Cells

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1×10³ target cells (E0771-LG:Fluc_NLR cells), 4×10³ effector cells (splenic NK cells), and/or 3×10³ suppressor cells (macrophages or MDSCs isolated from the lung containing E0771-LG metastatic tumors) were seeded into 96-well plates (Nunc) precoated with basement membrane extract (Geltrex, Gibco). These cells were cocultured in αMEM including 10% FBS, 1% penicillin/streptomycin, 1000 U/mL IL-2 (PeproTech), 20 ng/mL M-CSF (PeproTech), and 2.5 µM fluorogenic caspase-3 substrate (NucView 488, Biotium) at 37°C, 5% CO₂, and imaged by IncuCyte Zoom Live-Cell Analysis System (Sartorius) at 10× magnification for up to 48–72 hours. The numbers of apoptotic tumor cells (nuclei showing large areas of overlapping red/green fluorescence) were counted using the IncuCyte Zoom software (Sartorius) as previously described.13 (link) In some experiments, the following antibodies (25 µg/mL) were added in culture: anti-Ly49A (YE1/48.10.6), anti-H2-Kb (AF6-88.5), anti-TGF-β (19D8) from BioLegend, H2-Db (28-14-8), and Ly49C/I (5E6) from BD Biosciences.

Brownlie D., Doughty-Shenton D., YH Soong D., Nixon C., O Carragher N., M Carlin L, & Kitamura T. (2021). Metastasis-associated macrophages constrain antitumor capability of natural killer cells in the metastatic site at least partially by membrane bound transforming growth factor β. Journal for Immunotherapy of Cancer, 9(1), e001740.

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Insulin-Loaded DC Stimulate NOD CD8+ T Cells

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Splenic DC from NOD mice were cultured overnight (16–20 h) at 37°C with 1 μM porcine insulin, 4 μM peptide mixes from the preproinsulin peptide libraries, or 1 μM individual peptides (except where indicated otherwise) in the presence of LPS. On day 1, 2×10⁴ CD8 T cells from spleens of NOD.AI4αβ Tg or NOD.8.3 mice, isolated using MACS microbeads (Miltenyi Biotec), were cultured with 2×10⁴ peptide-loaded DC for 72 h, following which BrdU labeling solution (Roche) was added. BrdU incorporation was measured by ELISA after 16–20 h following the manufacturer’s protocol.
To determine MHC class I restriction, 50 μg/ml of H-2K^d (SF1-1.1.1; eBioscience) or H-2D^b (28-14-8; BD Biosciences) blocking antibody was added to the peptide-loaded DC prior to introduction of the CD8 T cells. T cell proliferation was assessed by BrdU incorporation.

Lamont D., Mukherjee G., Kumar P.R., Samanta D., McPhee C.G., Kay T.W., Almo S.C., DiLorenzo T.P, & Serreze D.V. (2014). Compensatory Mechanisms Allow Undersized Anchor-deficient Class I MHC Ligands to Mediate Pathogenic Autoreactive T Cell Responses. Journal of immunology (Baltimore, Md. : 1950), 193(5), 2135-2146.

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