Anti cxcl10

Manufactured by Abcam

Sourced in United Kingdom, United States

Anti-CXCL10 is a laboratory reagent used for the detection and quantification of CXCL10 protein in various biological samples. CXCL10 is a chemokine involved in inflammatory processes.

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Lab products found in correlation

Anti cxcr3, by Abcam (2 mentions) Polyvinylidene fluoride membrane, by Merck Group (2 mentions) Cd8 magnetic beads, by Miltenyi Biotec (1 mentions) Stattic, by Selleck Chemicals (1 mentions) S7024, by Selleck Chemicals (1 mentions) Anti cd8, by Abcam (1 mentions) Anti cd4, by Abcam (1 mentions) Anti il 17a, by Abcam (1 mentions) Anti cd31, by BD (1 mentions) Rat anti mouse igg2a hrp, by Bio-Rad (1 mentions) Anti tubulin, by Merck Group (1 mentions) Sheep anti mouse hrp and donkey anti rabbit hrp, by Cytiva (1 mentions) Anti glut1, by Cell Signaling Technology (1 mentions) Anti stat1, by Proteintech (1 mentions) Anti gapdh, by Yeasen (1 mentions) Anti jak1, by Proteintech (1 mentions) Anti p stat1, by Abcam (1 mentions) Anti tublin, by Yeasen (1 mentions) Rabbit peroxidase conjugated secondary antibody, by ABclonal (1 mentions) Anti pd l1, by Proteintech (1 mentions)

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CXCL10 (9 citations)

7 protocols using anti cxcl10

CD8+ T Cell Migration Assay

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Isolation of CD8⁺ T cells from HD samples was performed with CD8 magnetic beads (Miltenyi Biotech, Bergisch Gladbach, Germany) according to manufacturer’s instructions. Freshly isolated CD8⁺ T cells, anti-CXCR3 (10 ng/mL, Abcam), or Stattic (10 nM; S7024; Selleck Chem, Houston, TX)-treated CD8⁺ T cells as well as peripheral blood mononuclear cells (PBMCs) from HDs were seeded on the upper chambers of a 5.0-μm pore Transwell. Supernatants of tumor tissue, anti-CXCL10 (100 ng/mL, Abcam), or recombinant human (rh) CXCL10 (Peprotech, Rocky Hill, NJ) were added to the lower chambers. CD8⁺ T cells in the upper chambers were pretreated with rhIL-17A (20 ng/mL), Stattic (10 nM), and/or the supernatants of enriched Th17 cells (5 × 10⁶) with or without anti-IL-17A (10 ng/mL) for 48 h in vitro. Migrated cells in the lower chambers were then counted and analyzed by flow cytometry after 12 h.

Wang D., Yu W., Lian J., Wu Q., Liu S., Yang L., Li F., Huang L., Chen X., Zhang Z., Li A., Liu J., Sun Z., Wang J., Yuan W, & Zhang Y. (2020). Th17 cells inhibit CD8+ T cell migration by systematically downregulating CXCR3 expression via IL-17A/STAT3 in advanced-stage colorectal cancer patients. Journal of Hematology & Oncology, 13, 68.

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Immunohistochemical and Immunofluorescence Analysis of Colorectal Cancer

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Specimens from CRC patients and mice were formalin fixed, sectioned, and embedded into paraffin for immunohistochemistry. Immunofluorescence was performed with frozen samples and freshly fixed cells. The following antibodies were used: anti-CD8 (1:500), anti-CXCL10 (1:300), anti-CD4 (1:300), anti-IL-17A (1:300), and anti-CXCR3 (1:300; all Abcam, Cambridge, UK). Immunohistochemistry and immunofluorescence were performed as described elsewhere [33 (link), 34 (link)]. For immunohistochemistry, three fields of view per sample were imaged. The intensity of immunostaining was considered when analyzing the data. The percentage scoring of immunoreactive cells was as follows: 0 (< 10%), 1 (10–40%), 2 (40–70%), and 3 (> 70%). Staining intensity was visually scored and stratified as follows: 0 (negative), 1 (yellowish), 2 (light brown), and 3 (dark brown). Immunoreactivity scores (IRS) were obtained by multiplying the two items to a total score and ranged from 0 to 9. Protein expression levels were further analyzed by classifying IRS values as low (based on an IRS value ≤ 5) and as high (based on an IRS value > 5).

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Antibody Sources for Cell Experiments

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Antibodies were obtained from the following commercial sources: anti-tubulin (Sigma, St. Louis, MO), anti-GLUT1 (Cell Signaling, Beverly, MA), anti-HIF-1ɑ and anti-HIF-2ɑ (Novus Biologicals, Littleton, CO), anti-CXCL10 (Abcam, Cambridge, MA for IHC; R&D Systems, Minneapolis, MN for neutralization studies), anti-CD31 (BD Biosciences, San Jose, CA), rat anti-mouse IgG2a-HRP (Serotec, Raleigh, NC), and sheep anti-mouse-HRP and donkey anti-rabbit-HRP (Amersham, Pittsburgh, PA). Anti-reovirus antibody and Reolysin were kindly provided by Oncolytics Biotech, Inc. (Calgary, AB, Canada). Alexa Fluor 488 rabbit anti-goat was obtained from Molecular Probes (Eugene, OR). Sunitinib, bevacizumab, and temsirolimus were purchased from the hospital pharmacy.

Carew J.S., Espitia C.M., Zhao W., Mita M.M., Mita A.C, & Nawrocki S.T. (2017). Oncolytic reovirus inhibits angiogenesis through induction of CXCL10/IP-10 and abrogation of HIF activity in soft tissue sarcomas. Oncotarget, 8(49), 86769-86783.

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Western Blot Profiling of HPV Biomarkers

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Cultured cells were lysed with lysis buffer. Equal amounts of protein were run on 10% SDS-PAGE and electrotransferred to polyvinylidene fluoride membranes (Millipore). After blocking with 5% milk in TBST, membranes were incubated with primary antibodies overnight. The following antibodies were used: anti-HPVE6 (1:1000, Arigo), anti-HPVE7(1:1000, Bioss), (anti-CXCL10 (1:1,000, Abcam), anti-CXCR3 (1:1,000, Boster), anti-PDL1 (1:2,000, proteintech), anti-STAT1 (1:1,000, proteintech), anti-pSTAT1 (1:1,000, Abcam), anti-JAK1 (1:2,000, proteintech), anti-GAPDH (1:6,000, Yeasen) and anti-tublin (1:3,000, Yeasen). Membranes were then incubated with the rabbit peroxidase-conjugated secondary antibody (1:10,000, Abclonal). The blots were detected by sensitive chemiluminescence liquid analysis (Yeasen) and Biorad software was used to capture the images.

Chen X., He H., Xiao Y., Hasim A., Yuan J., Ye M., Li X., Hao Y, & Guo X. (2021). CXCL10 Produced by HPV-Positive Cervical Cancer Cells Stimulates Exosomal PDL1 Expression by Fibroblasts via CXCR3 and JAK-STAT Pathways. Frontiers in Oncology, 11, 629350.

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Immunohistochemical analysis of mouse brain

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Sixteen-months-old mice were sacrificed by cervical dislocation. Brains were recovered and the right hemisphere was fixed in 4% paraformaldehyde in phosphate buffer saline (PBS) for 24 hours at 4°C. After three washes with PBS, the samples were dehydrated and embedded in paraffin and sectioned at 4 μm using a microtome HM-340E (Microm, Madrid, Spain). Sections were deparaffined, rehydrated and microwave antigen retrieval was performed for 10 min in 10 mM citrate buffer pH 6.0. Sections were immersed in blocking buffer (1% BSA, 10% FBS, 0.2% Triton X100, in PBS) and incubated O/N at 4°C with primary antibody diluted in blocking buffer: anti-Lcn2 (1/25, Novus Biologicals NBP1-05183), anti-Cxcl10 (1/25, Abcam ab8098), anti-Gfap (1/300, Synaptic Sytems 173 004), anti-Gfap (1/200, Sigma G3893) and anti-Iba1 (1/50, Waco 019-19741). After three washes of 10 min in PBS, sections were incubated for one hour at room temperature with the appropriate secondary antibody diluted at 1/500 in blocking buffer without Triton X100, washed once with PBS, incubated with DAPI (Sigma, Madrid, Spain), washed twice with PBS and mounted in AquaPolymount (Polysciences Inc., USA). Images were acquired in a Confocal Spectral Leica TCS SP8 microscope (Leica, Wetzlar, Germany).

Lahuerta M., Gonzalez D., Aguado C., Fathinajafabadi A., García-Giménez J.L., Moreno-Estellés M., Romá-Mateo C., Knecht E., Pallardó F.V, & Sanz P. (2019). Reactive glia-derived neuroinflammation, a novel hallmark in Lafora progressive myoclonus epilepsy that progresses with age.. Molecular neurobiology, 57(3), 1607-1621.

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Immunoblotting Analysis of Chemokine Signaling

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Cultured cells were lysed on ice with 100 µl lysis buffer, collected by a cell scraper for a violent vortex, and then centrifuged at 4°C at 12,000 rpm for 10 min. Supernatants were collected, and the quantified proteins were boiled for sodium dodecyl sulfate polyacrylamide gel electrophoresis. Samples were run on 6 and 12% Tris-Glycine gels separately. Immunoblotting was performed according to standard protocol, transferred to polyvinylidene fluoride membrane (Merck Millipore, Billerica, MA, USA), blocked with tris buffered saline with tween (TBST) + 5% skim milk for 2 h at room temperature, incubated overnight at 4 °C with the following antibodies: anti-CCL2 (Abcam, #9669, Cambridge, MA, USA), anti-β-actin (Abcam, #8226), and anti-CXCL10 (Abcam, #9807). After incubating with the aforementioned antibodies, samples were washed three times with horseradish peroxidase and incubated with HRP-conjugated IgG antibodies for 2 h at room temperature. Specific bands were detected using the chemiluminescent substrate (Thermo Fisher, Waltham, MA, USA). Immunoblot bands were quantified in relation to β-actin using Image-Pro Plus.

Lu X., Liu Y., Xu L., Liang H., Zhou X., Lei H, & Sha L. (2023). Role of Jumonji domain-containing protein D3 and its inhibitor GSK-J4 in Hashimoto’s thyroiditis. Open Medicine, 18(1), 20230659.

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Western Blot Analysis of Extracellular Vesicles

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Pf-iRBC were saponized using 0.2% saponin in PBS (S7900-Sigma) and then were lysed using RIPA buffer. EVs at a concentration of 1.5–2 × 10¹¹ particles per ml were lysed in 20 µl of 5X RIPA buffer were sonicated in a bath sonicator for 10 s. THP-1 cells were lysed using RIPA buffer. Then, 120 μg of the obtained protein was subjected to gel electrophoresis; CXCL10 WB using 4–20% Bis-Tris gradient gels (GeneScript) and transferred into PVDF membranes (Bio-Rad); the rest of WB using 10% SDS-TRIS gels transferred into nitrocellulose membranes (Bio-Rad). The membrane was blocked for 1 hour with 5% skim milk in PBS-Tween 20 0.05%. The following primary antibodies were used in this work: anti-CXCL10 produced in rabbit (Abcam) for 2 h or anti-HSP90 produced in mouse (Abcam) for 1 hour, both diluted 1:1000; Anti-HUR produced in rabbit (Santa Cruz), anti-GAPDH produced in rabbit (Abcam), and anti-Dematin produced in rabbit (Abcam) for 1 h, all diluted 1:1000. The secondary antibodies used were goat anti-rabbit (Sigma-Aldrich) diluted 1:20,000 and goat anti-mouse (Abcam) diluted 1:2000, both conjugated with HRP and incubated for 40 minutes. The membrane was developed using Western ECL Substrate (Bio-Rad) and captured by Amersham imager 680 v2.0.0.

Ofir-Birin Y., Ben Ami Pilo H., Cruz Camacho A., Rudik A., Rivkin A., Revach O.Y., Nir N., Block Tamin T., Abou Karam P., Kiper E., Peleg Y., Nevo R., Solomon A., Havkin-Solomon T., Rojas A., Rotkopf R., Porat Z., Avni D., Schwartz E., Zillinger T., Hartmann G., Di Pizio A., Quashie N.B., Dikstein R., Gerlic M., Torrecilhas A.C., Levy C., Nolte-‘t Hoen E.N., Bowie A.G, & Regev-Rudzki N. (2021). Malaria parasites both repress host CXCL10 and use it as a cue for growth acceleration. Nature Communications, 12, 4851.

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