St1202

Manufactured by Merck Group

Sourced in United States

The ST1202 is a laboratory equipment product manufactured by Merck Group. It is designed for specific laboratory tasks, but a detailed description cannot be provided while maintaining an unbiased and factual approach. Additional information about the core function or intended use of this product is not available.

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Lab products found in correlation

Ab128568, by Abcam (2 mentions) Ne per nuclear and cytoplasmic extraction reagent, by Thermo Fisher Scientific (2 mentions) Bca protein assay kit, by Thermo Fisher Scientific (2 mentions) Nuclear extraction kit, by Solarbio (1 mentions) Ab77232, by Abcam (1 mentions) Ab124937, by Abcam (1 mentions) Ab11083, by Abcam (1 mentions) Sc 7294, by Santa Cruz Biotechnology (1 mentions) Nbp1 00861, by Novus Biologicals (1 mentions) Ab22555, by Abcam (1 mentions) Ab16048, by Abcam (1 mentions) Ab32358, by Abcam (1 mentions) A5441, by Merck Group (1 mentions) A3854, by Merck Group (1 mentions) Nb300 109, by Novus Biologicals (1 mentions) Ab6673, by Abcam (1 mentions) 3 3 diaminobenzidine (dab), by Merck Group (1 mentions) Clarity ecl, by Bio-Rad (1 mentions)

Spelling variants of this product

Anti-PGC-1α (ST1202) (2 citations)

7 protocols using st1202

Immunohistochemical Quantification of CPT1A and PGC1α

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Immunohistochemical (IHC) staining was performed as previously described.41, 42 The results were separately quantified by 2 pathologists from Xiangya Hospital, Changsha, China. The negative to positive patterns (denoted as – to +++) and IHC scores were determined by their staining intensity and positive rate. Anti–CPT1A (ab128568, Abcam) and anti–PGC1α (ST‐1202, Millipore) were used to detect the respective proteins.

Du Q., Tan Z., Shi F., Tang M., Xie L., Zhao L., Li Y., Hu J., Zhou M., Bode A., Luo X, & Cao Y. (2019). PGC1α/CEBPB/CPT1A axis promotes radiation resistance of nasopharyngeal carcinoma through activating fatty acid oxidation. Cancer Science, 110(6), 2050-2062.

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Protein Extraction and Analysis from C2C12 Cells

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We use RIPA lysis buffer containing 1 mM PMSF to lyse C2C12 cell or muscles. For the nuclear or cytoplasmic protein extraction, proteins were isolated according to the procedure of the nuclear extraction kit (Solarbio, SN0020). Protein concentration was determined using a BCA protein assays kit. After sodium dodecyl sulfate (SDS)–polyacrylamide gel electrophoresis gels, primary antibodies were used, including rabbit anti‐β‐tubulin (bs‐1482M, 1:5,000, Bioss), rabbit anti‐SUNCR1 (NBP1‐00861, 1:1,000, Novus), mouse anti‐MyHC I (ab11083, 1:1,000; Abcam), rabbit anti‐MyHC IIa (ab124937, 1:1,000, Abcam), goat anti‐MyHC IIb (sc‐168672, 1:500; Santa Cruz), mouse anti‐PGC‐1α (ST1202, 1:1,000, Millipore), rabbit anti‐histone (4499S, 1:2,000; CST), mouse anti‐NFAT (sc‐7294, 1:500; Santa Cruz), rabbit anti‐NRF‐1 (#12381s, 1:2,000, CST), rabbit anti‐calcineurin (#2614s, 1:2,000; CST), rabbit anti‐Myoglobin (ab77232, 1:1,000, Abcam), and rabbit anti‐MEF2A (#97365, 1:2,000; CST). Protein expression levels were determined using MetaMorph software (ImageJ, National Institutes of Health, USA).

Wang T., Xu Y., Yuan Y., Xu P., Zhang C., Li F., Wang L., Yin C., Zhang L., Cai X., Zhu C., Xu J., Liang B., Schaul S., Xie P., Yue D., Liao Z., Yu L., Luo L., Zhou G., Yang J., He Z., Du M., Zhou Y., Deng B., Wang S., Gao P., Zhu X., Xi Q., Zhang Y., Shu G, & Jiang Q. (2019). Succinate induces skeletal muscle fiber remodeling via SUNCR1 signaling. EMBO Reports, 20(9), e47892.

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Quantifying Nuclear PGC1α Levels

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U87 cells were harvested after treatment by DMSO or Ki8751, or after transfection by shRNA (shSCR, sh#1, #2, #3). Cell pellets were washed once with PBS, and preparation of cytoplasmic extract and nuclear extract were then conducted by using NE-PER™ Nuclear and Cytoplasmic Extraction Reagents (#78833, Thermo Fisher Scientific) according to the manufacturer’s instructions. The protein levels were quantified and the same amounts of protein (50 μg cytoplasmic proteins and 15 μg nuclear proteins) were loaded on SDS-PAGE gels and run Western blot to compare PGC1α expression (clone 4C1.3; ST1202; Millipore, Hayward, CA, USA), where GAPDH (ab22555; 1:1,000; Abcam, Cambridge, UK) and LaminB1 (ab16048; 1:1,000; Abcam) were used to assess cytoplasmic and nuclear protein input levels, respectively.

Guo M., Zhang J., Han J., Hu Y., Ni H., Yuan J., Sun Y., Liu M., Gao L., Liao W., Ma C., Liu Y., Li S, & Li N. (2024). VEGFR2 blockade inhibits glioblastoma cell proliferation by enhancing mitochondrial biogenesis. Journal of Translational Medicine, 22, 419.

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Western Blot Analysis of Metabolic Regulators

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Western blot analysis was performed as previously described.39 The following antibodies were used for western blotting: anti–CPT1A (ab128568; Abcam), anti–PGC1α (ST‐1202; Millipore), anti–CEBPB (ab32358, Abcam) and β‐actin (A5441; Sigma‐Aldrich).

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Immunoprecipitation of PGC1α from Hepa 1-6 Cells

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Hepa 1-6 cells were infected with indicated adenoviruses or transiently transfected with indicated plasmids. At 48 hours following infection or transfection, cells were lysed with ice-cold RIPA buffer on a shaker at 4°C for 1 hour. The lysate was centrifuged at 14,000g for 15 minutes at 4°C to pellet debris and the supernatant was transferred into a fresh Eppendorf tube. After quantification by DC assay, 1 mg of protein for each group was incubated with anti-PGC1α (Millipore, catalog ST1202) overnight at 4°C with rotation. Five percent of the lysate was saved as input. Thirty microliters of protein G-agarose (Santa Cruz Biotechnology, catalog sc-2002) was washed with RIPA buffer 3 times and then added into protein lysate following rotation at 4°C for 3 hours. The beads were pelleted by quick spin and washed with RIPA buffer 3 times. After removing supernatant, 30 μL of sample buffer was added to elute the immunoprecipitated proteins followed by boiling at 98°C for 5 minutes. The immunoprecipitated protein was subjected to immunoblotting as described above.

Ma Y., Liu S., Jun H., Wang J., Fan X., Li G., Yin L., Rui L., Weinman S.A., Gong J, & Wu J. (2020). A critical role for hepatic protein arginine methyltransferase 1 isoform 2 in glycemic control. FASEB journal : official publication of the Federation of American Societies for Experimental Biology, 34(11), 14863-14877.

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Immunohistochemistry and Immunoblotting Analysis

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For immunohistochemistry, animals were perfused with PBS followed by 4% paraformaldehyde. Brains were postfixed with 4% paraformaldehyde and cryoprotected in 30% sucrose. Coronal sections, including striatum and ventral middle brain, were incubated with rabbit polyclonal anti-tyrosine hydroxylase (TH; catalog #NB300-109, Novus Biologicals; RRID: AB_350437). The image was visualized with 3,3'-diaminobenzidine (Sigma-Aldrich) and analyzed by Stereo Investigator software. The sections were incubated with goat polyclonal anti-green fluorescent protein (GFP) (catalog #ab6673, Abcam; RRID: AB_305643), and secondary antibodies were coagulated with Alexa fluorescent for 1 h at room temperature. Brain cell lysates were immunoblotted with mouse mono anti-PGC-1α (catalog #ST1202, Millipore; RRID: AB_2237237), rabbit polyclonal anti- succinate dehydrogenase complex, subunit A (SDHA; catalog #5839S, Cell Signaling Technology; RRID:AB_10707493), mouse mono anti-Tomm20 (translocase of outer mitochondrial membrane 20; catalog #WH0009804M1, Sigma-Aldrich; RRID:AB_1843992), monoclonal anti-β-actin-peroxidase (Sigma-Aldrich catalog #A3854; RRID:AB_262011).

Jiang H., Kang S.U., Zhang S., Karuppagounder S., Xu J., Lee Y.K., Kang B.G., Lee Y., Zhang J., Pletnikova O., Troncoso J.C., Pirooznia S., Andrabi S.A., Dawson V.L, & Dawson T.M. (2016). Adult Conditional Knockout of PGC-1α Leads to Loss of Dopamine Neurons. eNeuro, 3(4), ENEURO.0183-16.2016.

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Protein Extraction and Western Blot Analysis

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Total proteins from cultured cells were extracted with lysis buffer (50 mM Tris–HCl pH 7.4, 1% Triton X-100, 0.25% sodium deoxycholate, 150 mM NaCl, 1 mM EDTA) supplemented with inhibitors (2 μg/mL pepstatin, 1 μg/mL aprotinin, 1 μg/mL leupeptin, 0.2 mM phenylmethylsulfonyl fluoride and 1 mM sodium orthovanadate) and quantified using a BCA protein assay kit (Thermo Fisher Scientific #PI123225). The blots were incubated according to the manufacturer's instructions with the following primary antibodies: PGC-1α (Calbiochem #ST1202, RRID:AB_2237237), PGC-1β (Millipore #ABC218, RRID:AB_2891214), and Actin (Santa Cruz Biotechnology #sc-1616, RRID:AB_630836) and with horseradish peroxidase-conjugated secondary antibodies (anti-mouse, KPL #KP-074–1806; anti-rabbit, KPL #KP-074–1506; anti-goat, Abcam #ab6881, RRID:AB_955236). The results were visualized using Clarity ECL (Bio-Rad #1705060).

McGuirk S., Audet-Delage Y., Annis M.G., Xue Y., Vernier M., Zhao K., St-Louis C., Minarrieta L., Patten D.A., Morin G., Greenwood C.M., Giguère V., Huang S., Siegel P.M, & St-Pierre J. (2021). Resistance to different anthracycline chemotherapeutics elicits distinct and actionable primary metabolic dependencies in breast cancer. eLife, 10, e65150.

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