Anti socs3

Manufactured by Santa Cruz Biotechnology

Sourced in China, United States

Anti-SOCS3 is a laboratory reagent that can be used to detect the presence of SOCS3 (Suppressor of Cytokine Signaling 3) in biological samples. SOCS3 is a protein that plays a role in the regulation of cytokine signaling pathways. The Anti-SOCS3 reagent can be used in various research applications, such as Western blotting, immunoprecipitation, and immunohistochemistry, to study the expression and function of SOCS3 in different cell types and experimental models.

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5 protocols using anti socs3

Western Blot Analysis of SOCS3 and GAPDH

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Western blot analysis was performed as in(5 (link)) using anti-SOCS3 (Santa Cruz Biotechnology, Santa Cruz, CA) or anti-GAPDH (EMD Millipore, Billerica, MA) antibodies.

Zheng S., Hedl M, & Abraham C. (2015). TAM receptor-dependent regulation of SOCS3 and MAPKs contributes to pro-inflammatory cytokine downregulation following chronic NOD2 stimulation of human macrophages. Journal of immunology (Baltimore, Md. : 1950), 194(4), 1928-1937.

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Immunofluorescent Staining of STAT3 Signaling

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Heat-mediated antigen retrieval was performed on brain sections by incubation in sodium citrate buffer (10 mM sodium citrate, 0.05% Tween 20, pH 6.0) at 95 °C for 30 min prior to immunofluorescent staining. The brain sections were blocked in 2.5% horse serum (Vector Lab) plus 0.3% Triton X-100 at room temperature for 1 h and then incubated with primary antibodies in blocking solution overnight in 4 °C, followed by incubation with Alexa Fluor-conjugated secondary antibodies. The primary antibodies were anti-phopho-STAT3 (Tyr 705; Cell Signaling), anti-PTPase 1B (Ab-1, Oncogene), anti-SOCS-3 (Santa Cruz), anti-GFP (Santa Cruz) and anti-G_sα [26] (link). The signals in GFP-expressing neurons in the DMH were captured and visualized with fluorescence microscopy. The average on a minimum of 4 sections from each mouse was quantified using BZ-II Analyzer software version 2.1 (Keyence). UCP1 immunohistochemistry was performed as previously described using an anti-UCP1 primary antibody (Abcam, Ab10983, 1:1000 dilution) [27] (link).

Chen M., Wilson E.A., Cui Z., Sun H., Shrestha Y.B., Podyma B., Le C.H., Naglieri B., Pacak K., Gavrilova O, & Weinstein L.S. (2019). Gsα deficiency in the dorsomedial hypothalamus leads to obesity, hyperphagia, and reduced thermogenesis associated with impaired leptin signaling. Molecular Metabolism, 25, 142-153.

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Western Blot Analysis of PEDV Signaling

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After washing with PBS, the cells were acquired by RIPA lysis buffer with PMSF and phosphatase inhibitor. Then, the cell samples were homogenized and centrifuged at 4 °C. The supernatants were collected. Then, the samples were separated by SDS-PAGE and transferred to PVDF membranes. The membranes were blocked by 5% nonfat milk. After this, the membranes were incubated overnight with the corresponding antibodies: anti-PEDV (Medgene Labs, Brookings, SD, USA); anti-STAT1, anti-p-STAT1, anti-STAT3, anti-p-STAT3, anti-JAK1, anti-JAK2, anti-NF-κB, anti-p-NF-κB, anti-IκBα (Cell Signaling Technology, Shanghai, China); anti-VDR (Abcam, Shanghai, China); anti-SOCS3 and anti-β-actin (Santa Cruz, Shanghai, China). Following washing, the samples were incubated with secondary antibodies for 1 h at room temperature, and then proteins were incubated with ECL reagent (Beyotime Biotechnology, Shanghai, China) for chemiluminescence by the ChemiDoc^TM XRS Imager System (Bio-Rad, Hercules, CA, USA).

Yang J., Chen D., Tian G., Mao X., He J., Zheng P., Yu J., Luo Y., Luo J., Huang Z., Wu A., Yan H, & Yu B. (2022). 1,25-Dihydroxyvitamin D3 Negatively Regulates the Inflammatory Response to Porcine Epidemic Diarrhea Virus Infection by Inhibiting NF-κB and JAK/STAT Signaling Pathway in IPEC-J2 Porcine Epithelial Cells. International Journal of Molecular Sciences, 23(18), 10603.

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Immunoblotting and Signaling Pathway Analysis

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Ultrapure LPS and CpG oligonucleotide (ODN1826) were from InvivoGen. Recombinant murine IL-4, IL-6, and IFN-γ were from PeproTech. Pam3Cys was from EMC Microcollections. PUGNAc, Tm, GlcNAc, SFN, tBHQ, DMF, and AOM were from Sigma-Aldrich. DSS was from TDB Consultancy AB. Antibodies for immunoblotting included Phospho-Stat Antibody Sampler kit containing anti–p-STAT1 (Y701), anti–p-STAT3 (Y705), anti–p-STAT6 (Y641), anti–p-IKKα/β (S176/180), anti-IKKβ, anti–p-IκBα (S32), anti-IκBα, anti–p-p65 (S536), anti-p65, anti–p-ERK1/2 (T202/Y204), anti–p-JNK (T183/Y185), anti–p-p38 (T180/Y182), anti-OGT and anti–O-GlcNAc (Cell Signaling Technology), anti-STAT3, anti-SOCS3, anti-CHOP, HRP-conjugated anti–β-actin (Santa Cruz Biotechnology, Inc.), HRP-conjugated anti-FLAG (Sigma-Aldrich), anti-Xbp1s (BioLegend), and anti-CUL3 (BD). Anti-Nrf2 (Abcam) antibody was used for both immunoblotting and immunoprecipitation.

Li X., Zhang Z., Li L., Gong W., Lazenby A.J., Swanson B.J., Herring L.E., Asara J.M., Singer J.D, & Wen H. (2017). Myeloid-derived cullin 3 promotes STAT3 phosphorylation by inhibiting OGT expression and protects against intestinal inflammation. The Journal of Experimental Medicine, 214(4), 1093-1109.

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Insulin Signaling Pathway Analysis

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Lopinavir and darunavir were purchased from Toronto Research Chemicals Inc. (Toronto, Ontario, Canada) and dissolved in ethyl acetate and methanol, respectively. Since the levels of IRS1 expression and IRS1 phosphorylation by insulin were comparable in preliminary experiments, methanol was used as a vehicle control in the following experiments. Insulin from bovine pancreas was obtained from Sigma-Aldrich (St. Louis, MO, USA). The primary antibodies used were anti-phospho (Ser307)-IRS1 and anti-IRS1 antibodies (Upstate Biotechnology Inc., Lake Placid, NY, USA), and anti-SOCS1, anti-SOCS3 and anti-PTP1B antibodies (Santa Cruz Biotechnology, Santa Cruz, CA, USA). The phospho-tyrosine-specific monoclonal antibody 4G10 (Upstate Biotechnology, Darmstadt, Germany) was used in the immunoprecipitation assay.

KITAZAWA T., YOSHINO Y., SUZUKI S., KOGA I, & OTA Y. (2014). Lopinavir inhibits insulin signaling by promoting protein tyrosine phosphatase 1B expression. Experimental and Therapeutic Medicine, 8(3), 851-855.

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