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protein a8  (R&D Systems)


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    Structured Review

    R&D Systems protein a8
    Protein A8, supplied by R&D Systems, used in various techniques. Bioz Stars score: 95/100, based on 46 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/protein+a8/Human+S100A8%2FS100A9+Heterodimer+Quantikine+ELISA+Kit/pm40268791-55-11-16
    Average 95 stars, based on 46 article reviews
    protein a8 - by Bioz Stars, 2026-10
    95/100 stars

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    Related Articles

    Immunohistochemistry:

    Article Title: Nrf2 Deficiency Exacerbates the Decline in Swallowing and Respiratory Muscle Mass and Function in Mice with Aspiration Pneumonia
    Article Snippet: .. The dilution and antibodies used primarily for immunohistochemistry were as follows ( ): neutrophils: S100 calcium-binding protein A8 (S100A8; 1:500; goat; AF3059, R&D Systems, Minneapolis, MN, USA); macrophages: F4/80 (1:100; Rat; MCA497G, Bio-Rad, UK); T cells: CD3e (1:500; hamster; eBio500A2, eBioscience, San Diego, CA, USA); B cells: B220/CD45R (1:500; rat; RA3-6B2, eBioscience). .. Cy3- (Jackson ImmunoResearch Laboratories Inc., West Grove, PA, USA) or FITC-labeled species-specific secondary antibodies were applied.

    Biomarker Discovery:

    Article Title: Increased IL- 36γ in visceral adipose tissue as a key mediator of obesity-driven inflammation in colon cancer.
    Article Snippet: Serum glucose, triglycerides and C-reactive protein (CRP) concentrations were analysed by enzymatic spectrophotometric reactions using an automated analyser (Hitachi Modular P800, Roche, Basel, Switzerland), and insulin was measured with an enzymeamplified chemiluminescence assay (IMMULITE®, Diagnostic Products Corp., Los Angeles, CA, USA) as previously described [29]. .. Circulating levels of the intestinal damage biomarker calprotectin subunit S100 calcium-binding protein A8 (S100 A8) (DS8900, R&D Systems, Abingdon, UK), IL36γ (DY2320 - 05, R&D Systems) lactoferrin (EH309RB, Invitrogen, Carlsbad, CA, USA) and C–C motif chemokine ligand 5 (CCL5) (DRN00B, R&D Systems) concentrations were determined by commercially available ELISA kits following manufacturers’ instructions [29]. .. HT‐ 29 and adipocyte cultures The HT-29 colorectal adenocarcinoma cell line (HTBTM) (ATCC®, Middlesex, UK) was cultured according to the manufacturer’s instructions.

    Article Title: Increased IL- 36γ in visceral adipose tissue as a key mediator of obesity-driven inflammation in colon cancer
    Article Snippet: Serum glucose, triglycerides and C-reactive protein (CRP) concentrations were analysed by enzymatic spectrophotometric reactions using an automated analyser (Hitachi Modular P800, Roche, Basel, Switzerland), and insulin was measured with an enzyme-amplified chemiluminescence assay (IMMULITE®, Diagnostic Products Corp., Los Angeles, CA, USA) as previously described [ ]. .. Circulating levels of the intestinal damage biomarker calprotectin subunit S100 calcium-binding protein A8 (S100 A8) (DS8900, R&D Systems, Abingdon, UK), IL- 36γ (DY2320 - 05, R&D Systems) lactoferrin (EH309RB, Invitrogen, Carlsbad, CA, USA) and C–C motif chemokine ligand 5 (CCL5) (DRN00B, R&D Systems) concentrations were determined by commercially available ELISA kits following manufacturers’ instructions [ ]. .. The HT-29 colorectal adenocarcinoma cell line (HTBTM) (ATCC®, Middlesex, UK) was cultured according to the manufacturer’s instructions.

    Enzyme-linked Immunosorbent Assay:

    Article Title: Increased IL- 36γ in visceral adipose tissue as a key mediator of obesity-driven inflammation in colon cancer.
    Article Snippet: Serum glucose, triglycerides and C-reactive protein (CRP) concentrations were analysed by enzymatic spectrophotometric reactions using an automated analyser (Hitachi Modular P800, Roche, Basel, Switzerland), and insulin was measured with an enzymeamplified chemiluminescence assay (IMMULITE®, Diagnostic Products Corp., Los Angeles, CA, USA) as previously described [29]. .. Circulating levels of the intestinal damage biomarker calprotectin subunit S100 calcium-binding protein A8 (S100 A8) (DS8900, R&D Systems, Abingdon, UK), IL36γ (DY2320 - 05, R&D Systems) lactoferrin (EH309RB, Invitrogen, Carlsbad, CA, USA) and C–C motif chemokine ligand 5 (CCL5) (DRN00B, R&D Systems) concentrations were determined by commercially available ELISA kits following manufacturers’ instructions [29]. .. HT‐ 29 and adipocyte cultures The HT-29 colorectal adenocarcinoma cell line (HTBTM) (ATCC®, Middlesex, UK) was cultured according to the manufacturer’s instructions.

    Article Title: Increased IL- 36γ in visceral adipose tissue as a key mediator of obesity-driven inflammation in colon cancer
    Article Snippet: Serum glucose, triglycerides and C-reactive protein (CRP) concentrations were analysed by enzymatic spectrophotometric reactions using an automated analyser (Hitachi Modular P800, Roche, Basel, Switzerland), and insulin was measured with an enzyme-amplified chemiluminescence assay (IMMULITE®, Diagnostic Products Corp., Los Angeles, CA, USA) as previously described [ ]. .. Circulating levels of the intestinal damage biomarker calprotectin subunit S100 calcium-binding protein A8 (S100 A8) (DS8900, R&D Systems, Abingdon, UK), IL- 36γ (DY2320 - 05, R&D Systems) lactoferrin (EH309RB, Invitrogen, Carlsbad, CA, USA) and C–C motif chemokine ligand 5 (CCL5) (DRN00B, R&D Systems) concentrations were determined by commercially available ELISA kits following manufacturers’ instructions [ ]. .. The HT-29 colorectal adenocarcinoma cell line (HTBTM) (ATCC®, Middlesex, UK) was cultured according to the manufacturer’s instructions.



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    R&D Systems protein a8
    A Kinase prediction tools (KinasePhos 2.0, GPS 3.0, and iGPS 1.0) were used to identify potential kinases targeting TRIM24 at Ser1042. “+” indicates a positive prediction by the respective tool; “−” indicates no prediction. B DLD1 and SW620 cells were transferred with si-NC, si-AURKA, si-AURKB, si-CK2α, and si-AKT. After 72 h, whole cell lysates were derived and immunoblotted for indicated proteins, with Tubulin as a loading control. Experiments were conducted independently three times, consistently producing similar results. C DLD1 and SW620 cells were treated with hesperadin (AURK inhibitor, which has a particularly significant inhibitory effect on AURKB, 20 μM), CX-4945 (CK2 inhibitor, 20 μM), and AKT Inhibitor VIII <t>(AKT1/AKT2</t> inhibitor, 20 μM) for 4 h and 8 h, respectively. Whole cell lysates were derived and immunoblotted for indicated proteins. Experiments were conducted independently three times, consistently producing similar results. D In vitro phosphorylation assays utilized the purified GST-fusion proteins and AURKB, incubated with hesperadin or DMSO vehicle control. The reaction products were immunoblotted using indicated antibodies. AKT was employed as a positive control. Data are representative of three independent experiments. E SW620 cells were treated with hesperadin for 72 h, whole cell lysates were derived and immunoblotted for indicated proteins. Data are representative of three independent experiments. F Cytosolic (Cyto) and nuclear (Nuc) fractions derived from DLD1 and SW620 cells stimulated with 20 μM of hesperadin for 8 h were immunoblotted for indicated proteins. PARP1 and Caspase-3 served as loading controls and nuclear/cytosolic markers, respectively. Shown are the representative results from three independent experiments. G DLD1-WT/DLD1-KO-1 and SW620-WT/SW620-KO-1 cells were co-transfected with Renilla luciferase and TOPFlash plasmids. The cells were harvested 48 h after transfection, and firefly and Renilla luciferase substrates were added successively. The ratio of the detection value of firefly luciferase to the detection value of Renilla luciferase is taken to compare the difference in the results between the two groups of cells. Data were expressed as means ± SEM, two-tailed Student’s t -test. n = 3 biological replicates per group.
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    Image Search Results


    A Kinase prediction tools (KinasePhos 2.0, GPS 3.0, and iGPS 1.0) were used to identify potential kinases targeting TRIM24 at Ser1042. “+” indicates a positive prediction by the respective tool; “−” indicates no prediction. B DLD1 and SW620 cells were transferred with si-NC, si-AURKA, si-AURKB, si-CK2α, and si-AKT. After 72 h, whole cell lysates were derived and immunoblotted for indicated proteins, with Tubulin as a loading control. Experiments were conducted independently three times, consistently producing similar results. C DLD1 and SW620 cells were treated with hesperadin (AURK inhibitor, which has a particularly significant inhibitory effect on AURKB, 20 μM), CX-4945 (CK2 inhibitor, 20 μM), and AKT Inhibitor VIII (AKT1/AKT2 inhibitor, 20 μM) for 4 h and 8 h, respectively. Whole cell lysates were derived and immunoblotted for indicated proteins. Experiments were conducted independently three times, consistently producing similar results. D In vitro phosphorylation assays utilized the purified GST-fusion proteins and AURKB, incubated with hesperadin or DMSO vehicle control. The reaction products were immunoblotted using indicated antibodies. AKT was employed as a positive control. Data are representative of three independent experiments. E SW620 cells were treated with hesperadin for 72 h, whole cell lysates were derived and immunoblotted for indicated proteins. Data are representative of three independent experiments. F Cytosolic (Cyto) and nuclear (Nuc) fractions derived from DLD1 and SW620 cells stimulated with 20 μM of hesperadin for 8 h were immunoblotted for indicated proteins. PARP1 and Caspase-3 served as loading controls and nuclear/cytosolic markers, respectively. Shown are the representative results from three independent experiments. G DLD1-WT/DLD1-KO-1 and SW620-WT/SW620-KO-1 cells were co-transfected with Renilla luciferase and TOPFlash plasmids. The cells were harvested 48 h after transfection, and firefly and Renilla luciferase substrates were added successively. The ratio of the detection value of firefly luciferase to the detection value of Renilla luciferase is taken to compare the difference in the results between the two groups of cells. Data were expressed as means ± SEM, two-tailed Student’s t -test. n = 3 biological replicates per group.

    Journal: Nature Communications

    Article Title: Cytoplasmic TRIM24 promotes colorectal cancer cell proliferation by activating Wnt/β-catenin signaling

    doi: 10.1038/s41467-025-63685-8

    Figure Lengend Snippet: A Kinase prediction tools (KinasePhos 2.0, GPS 3.0, and iGPS 1.0) were used to identify potential kinases targeting TRIM24 at Ser1042. “+” indicates a positive prediction by the respective tool; “−” indicates no prediction. B DLD1 and SW620 cells were transferred with si-NC, si-AURKA, si-AURKB, si-CK2α, and si-AKT. After 72 h, whole cell lysates were derived and immunoblotted for indicated proteins, with Tubulin as a loading control. Experiments were conducted independently three times, consistently producing similar results. C DLD1 and SW620 cells were treated with hesperadin (AURK inhibitor, which has a particularly significant inhibitory effect on AURKB, 20 μM), CX-4945 (CK2 inhibitor, 20 μM), and AKT Inhibitor VIII (AKT1/AKT2 inhibitor, 20 μM) for 4 h and 8 h, respectively. Whole cell lysates were derived and immunoblotted for indicated proteins. Experiments were conducted independently three times, consistently producing similar results. D In vitro phosphorylation assays utilized the purified GST-fusion proteins and AURKB, incubated with hesperadin or DMSO vehicle control. The reaction products were immunoblotted using indicated antibodies. AKT was employed as a positive control. Data are representative of three independent experiments. E SW620 cells were treated with hesperadin for 72 h, whole cell lysates were derived and immunoblotted for indicated proteins. Data are representative of three independent experiments. F Cytosolic (Cyto) and nuclear (Nuc) fractions derived from DLD1 and SW620 cells stimulated with 20 μM of hesperadin for 8 h were immunoblotted for indicated proteins. PARP1 and Caspase-3 served as loading controls and nuclear/cytosolic markers, respectively. Shown are the representative results from three independent experiments. G DLD1-WT/DLD1-KO-1 and SW620-WT/SW620-KO-1 cells were co-transfected with Renilla luciferase and TOPFlash plasmids. The cells were harvested 48 h after transfection, and firefly and Renilla luciferase substrates were added successively. The ratio of the detection value of firefly luciferase to the detection value of Renilla luciferase is taken to compare the difference in the results between the two groups of cells. Data were expressed as means ± SEM, two-tailed Student’s t -test. n = 3 biological replicates per group.

    Article Snippet: Recombinant human AURKB, recombinant human AKT1 protein and crystal violet were purchased from Solarbio (China).

    Techniques: Derivative Assay, Control, In Vitro, Phospho-proteomics, Purification, Incubation, Positive Control, Transfection, Luciferase, Two Tailed Test