Dt 1bon1000 96

Manufactured by Immunodiagnostic Systems

The DT-1BON1000-96 is a laboratory equipment product manufactured by Immunodiagnostic Systems. The core function of this product is to perform diagnostic tests and analyses. No further details are available while maintaining an unbiased and factual approach.

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Lab products found in correlation

D4418, by Merck Group (1 mentions) Wga lectin, by Merck Group (1 mentions) Crosslaps for culture ctx 1 elisa kit, by Immunodiagnostic Systems (1 mentions) Sc 32790l, by Santa Cruz Biotechnology (1 mentions) Ma1 27198, by Thermo Fisher Scientific (1 mentions) Rankl, by R&D Systems (1 mentions) Antibodies directed against cd14, by Miltenyi Biotec (1 mentions) Rankl, by Miltenyi Biotec (1 mentions) Rpmi 1640, by Thermo Fisher Scientific (1 mentions) M csf, by Thermo Fisher Scientific (1 mentions) Accutase solution, by Merck Group (1 mentions) Magnetic microbead, by Miltenyi Biotec (1 mentions)

4 protocols using dt 1bon1000 96

Coculture of Osteoclasts and Precursors on Bone Slices

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OCLs (2 × 10³/well) and OCy-like cells (5 × 10³/well) were cocultured on bovine bone slices (Immunodiagnostic Systems, DT-1BON1000-96) in 96-well plates with αMEM plus 10% FCS with and without anti-IGF1R (0.5 μg/mL) for 72 hours. The cells were then removed, the bone slices stained with acid hematoxylin, and the areas of bone resorbed determined as previously described (30 (link)).

Miyagawa K., Tenshin H., Mulcrone P.L., Delgado-Calle J., Subler M.A., Windle J.J., Chirgwin J.M., Roodman G.D, & Kurihara N. (2023). Osteoclast-derived IGF1 induces RANKL production in osteocytes and contributes to pagetic lesion formation. JCI Insight, 8(14), e159838.

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Quantifying Bone Resorption Using Osteoclasts

Cited 5 times

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For bone resorption assays, BMDMs or pre-osteoclasts were seeded and cultured on bovine cortical bone slices (DT-1BON1000-96; Immunodiagnostic Systems) with 20 ng/ml M-CSF and 30 ng/ml RANKL (R&D Systems; Wu et al., 2017 (link); Zhang et al., 2018 (link); Zhu et al., 2020 (link)), in the presence or absence of galectin-3 (8259-GA; R&D Systems), galectin-3C (10110-GA; R&D Systems), GCS-100 (La Jolla Pharmaceutical), RAP (4480-LR; R&D Systems), an anti–galectin-3 blocking antibody (sc-32790L; Santa Cruz), or an anti-Lrp1 blocking antibody (MA1-27198; Thermo Fisher Scientific; Chen et al., 2015 (link); Demotte et al., 2010 (link); John et al., 2003 (link); Moxon et al., 2015 (link); Seguin et al., 2017 (link)). After the indicated culture period, bone samples were sonicated in PBS, stained with 20 μg/ml WGA-lectin (L3892; Sigma-Aldrich) for 45 min and then incubated with DAB tablets (D4418; Sigma-Aldrich) for 15 min. Image J software was used to quantify the resorbed area. The concentration of the CTX-I was measured using the CrossLaps for Culture CTX-I ELISA kit (AC-07F1; Immunodiagnostic Systems) according to the manufacturer’s instructions.

Zhu L., Tang Y., Li X.Y., Kerk S.A., Lyssiotis C.A., Sun X., Wang Z., Cho J.S., Ma J, & Weiss S.J. (2023). Proteolytic regulation of a galectin-3/Lrp1 axis controls osteoclast-mediated bone resorption. The Journal of Cell Biology, 222(4), e202206121.

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Osteoclast TRAP Activity Quantification

Cited 1 time

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TRAP activity was determined in condition media derived from osteoclasts grown upon cortical bone slices (Immunodiagnostic Systems, IDS, DT-1BON1000–96) and serum. Briefly, bone chips were placed in 96-well plates and seeded with WT and dnMAML osteoclast precursors and later treated with MCSF alone; MCSF + LPS; MCSF + RANKL and MCSF + LPS (after RANKL stimulation) respectively. Condition media was collected at 2^nd and 5^th day. Serum samples were obtained from WT PBS, dnMAML PBS, WT LPS and dnMAML LPS groups. Here, mice were injected with LPS above calvaria at a dose of 20 mg/kg and sacrificed after 3 days [27 (link), 28 (link)]. TRAP enzymatic activity was later estimated as per the procedure described previously [29 (link)]. Briefly TRAP solution buffer consisting of L- Ascorbic acid, di-Sodium tartrate, 4-Nitrophenylphosphate and Reaction buffer (1 M Acetate, 0.5% Triton X-100, 1 M NaCl, 10 mM EDTA pH=5.5) was added to 10 μl of Condition media in a 96-well plate system. Plates were incubated in dark and the reaction was stopped using NaOH. Absorbance was later recorded at 405 nm using a Biotek spectrophotometer.

Goel P.N., Egol A.J., Moharrer Y., Harvey B.B., Ahn J, & Ashley J.W. (2019). Notch signaling inhibition protects against LPS mediated Osteolysis. Biochemical and biophysical research communications, 515(4), 538-543.

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Isolation and Differentiation of Human Monocytes

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Human monocytes were isolated from blood of healthy donors as previously described (Van Goethem et al., 2010 (link)). Cells were re-suspended in cold PBS supplemented with 2 mM EDTA, 0.5% heat-inactivated fetal calf serum (FCS) at pH 7.4 and magnetically sorted with using magnetic microbeads coated with antibodies directed against CD14 (Miltenyi Biotec). Monocytes were then seeded on plastic at 2 × 10⁶ cells/well in six-well plates in RPMI 1640 (Invitrogen) without FCS. After 2 h at 37 °C in humidified 5% CO₂ atmosphere, the medium was replaced by RPMI containing 10% FCS, 100 ng/mL of macrophage colony-stimulating factor (M-CSF, Peprotech) and 60 ng/mL of human receptor activator of NF-κB-ligand (RANK-L, Miltenyi Biotec). The medium was then changed every third day by RPMI containing 10% FCS, 100 ng/mL of RANK-L and 25 ng/mL of M-CSF. For experiments, cells were harvested at day 10 using Accutase solution (Sigma-Aldrich) and centrifugation (1100 rpm, 10 min), and were then plated either on clean 1.5 H precision glass coverslips (Marienfeld 0117640) or on bovine bone slices (Immuno Diagnostic Systems DT-1BON1000-96). Cells were left to adhere in cytokine-supplemented medium for 3 days before fixation.

Portes M., Mangeat T., Escallier N., Dufrancais O., Raynaud-Messina B., Thibault C., Maridonneau-Parini I., Vérollet C, & Poincloux R. (2022). Nanoscale architecture and coordination of actin cores within the sealing zone of human osteoclasts. eLife, 11, e75610.

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