Anti c myc

Manufactured by Fortrea

The Anti-c-Myc is a laboratory reagent used to detect and quantify the c-Myc protein, a transcription factor involved in cell growth and proliferation. It provides a reliable and specific method for identifying and analyzing the presence and levels of c-Myc in various biological samples.

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Lab products found in correlation

Anti axin1, by Cell Signaling Technology (2 mentions) Anti lc3b, by Abcam (2 mentions) Anti sqstm1 p62, by Abcam (2 mentions) Nitrocellulose membrane, by Merck Group (2 mentions) Enhanced chemiluminescence reagent, by Merck Group (2 mentions) Anti β catenin, by Cell Signaling Technology (2 mentions) Anti gsk3β, by Cell Signaling Technology (2 mentions) Anti p β catenin, by Cell Signaling Technology (2 mentions) Anti ldha, by Cell Signaling Technology (2 mentions) Anti histone h3, by Cell Signaling Technology (2 mentions) Anti β actin, by Proteintech (2 mentions) Radioimmunoprecipitation assay lysis buffer, by Beyotime (2 mentions) Ne per nuclear cytoplasmic extraction reagent kit, by Thermo Fisher Scientific (1 mentions) Ecl prime, by GE Healthcare (1 mentions) Horseradish peroxidase conjugated secondary antibody, by Bio-Rad (1 mentions) Anti ha, by Fortrea (1 mentions)

3 protocols using anti c myc

Protein Extraction and Western Blot Analysis

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Total protein was extracted using radioimmunoprecipitation assay lysis buffer (Beyotime, China). An NE-PER™ Nuclear Cytoplasmic Extraction Reagent kit (Thermo Fisher Scientific, MA) was used according to the manufacturer’s instructions for extracting nuclear and cytoplasmic proteins from the different groups.
A 12% sodium dodecyl sulfate‐polyacrylamide gel was chosen for total protein separation, and the proteins were then transferred to nitrocellulose membranes (Millipore, USA). The membranes were incubated with primary antibodies, including anti-LC3B (Abcam Cat# ab192890, RRID: AB_2827794), anti-P62/SQSTM1 (Abcam Cat# ab207305, RRID: AB_2885112), anti-β-actin (Proteintech# 20536-1-AP), anti-LDHA (Cell Signaling Technology Cat# 3582, RRID: AB_2066887), anti-β-catenin (Cell Signaling Technology Cat# 8480), anti-p-β-catenin (Cell Signaling Technology Cat# 4176), anti-c-Myc (Covance Cat# MMS-150P-1000, RRID: AB_291322), anti-GSK3-β (Cell Signaling Technology Cat# 121456), anti-Axin1 (Cell Signaling Technology Cat# 2087, RRID: AB_2274550) and anti-Histone H3 (Cell Signaling Technology Cat# 4499, RRID: AB_10544537). Enhanced chemiluminescence reagents (Millipore, USA) were used to assess protein expression.

Li T., Tong H., Yin H., Luo Y., Zhu J., Qin Z., Yin S, & He W. (2021). Starvation induced autophagy promotes the progression of bladder cancer by LDHA mediated metabolic reprogramming. Cancer Cell International, 21, 597.

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Transient Protein Expression and Western Blotting

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Proteins were separated by SDS-PAGE, transferred to nitrocellulose, then detected by ECL prime (GE) using anti-HA (Covance), anti-cMyc (Covance), or anti-6xHis (Qiagen) and horseradish peroxidase-conjugated secondary antibodies (Bio-Rad). Primary and secondary antibodies were typically diluted 1:3000 to 1:5000 and 1:3000, respectively.
Transient protein expression in N. benthamiana.
A. tumefaciens strains grown overnight at 28°C were collected and incubated in induction media (10 mM 2-(N-morpholino) ethanesulfonic acid [pH 5.6], 10 mM MgCl 2 , and 150 µM acetosyringone) for 2 h. Leaves were inoculated with a final suspension (0.8 × 10 9 CFU/ml) of two strains. Plants were incubated at ambient temperature under continuous low light for 48 to 72 h.

Dubrow Z., Sunitha S., Kim J.G., Aakre C.D., Girija A.M., Sobol G., Teper D., Chen Y.C., Ozbaki-Yagan N., Vance H., Sessa G, & Mudgett M.B. (2018). Tomato 14-3-3 Proteins Are Required for Xv3 Disease Resistance and Interact with a Subset of Xanthomonas euvesicatoria Effectors. Molecular plant-microbe interactions : MPMI, 31(12).

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Protein Expression Analysis Protocol

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Total protein was drawn out using radioimmunoprecipitation assay lysis buffer (Beyotime, China). NE-PER TM Nuclear Cytoplasmic Extraction Reagent kit (Thermo Fisher Scienti c, MA) were used according to the manufacturer's instruction for extracting protein of nuclear and cytoplasmic from different groups.
12% sodium dodecyl sulfate-polyacrylamide gel was chosen for total protein separation and transferred to nitrocellulose membranes (Millipore, USA). Membranes were incubated with primary antibodies including: anti-LC3B (Abcam Cat# ab192890, RRID:AB_2827794), anti-P62/SQSTM1 (Abcam Cat# ab207305, RRID:AB_2885112), anti-β-actin (Proteintech# 20536-1-AP), anti-LDHA (Cell Signaling Technology Cat# 3582,RRID:AB_2066887), anti-β-catenin (Cell Signaling Technology Cat# 8480), anti-p-βcatenin (Cell Signaling Technology Cat# 4176), anti-c-Myc (Covance Cat# MMS-150P-1000,RRID:AB_291322), anti-GSK3-β (Cell Signaling Technology Cat# 121456), anti-Axin1 (Cell Signaling Technology Cat# 2087,RRID:AB_2274550) and anti-Histone H3 (Cell Signaling Technology Cat# 4499,RRID:AB_10544537). Enhanced chemiluminescence reagents (Millipore, USA) were used to assess protein expression.

Li T., Tong H., Yin H., Luo Y., Zhu J., Qin Z., Yin S., & He W. (2021). Starvation Induced Autophagy Promotes The Progression of Bladder Cancer By LDHA Mediated Metabolic Reprogramming.

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