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Mouse α c myc

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Mouse α-c-myc is a monoclonal antibody that recognizes the c-myc protein, a transcription factor that plays a role in cell proliferation, differentiation, and apoptosis. It is commonly used in research applications for the detection and analysis of c-myc expression in various cell and tissue types.

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Lab products found in correlation

Enhanced chemiluminescence kit, by Cytiva (3 mentions) Nupage, by Thermo Fisher Scientific (3 mentions) Clone cbp kk1, by Merck Group (2 mentions) Rabbit α gfp, by Abcam (1 mentions)

Spelling variants of this product

C-Myc (65 citations) α-myc (19 citations) α-c-Myc (4 citations) Mouse α-Myc (3 citations)

3 protocols using mouse α c myc

1

Optimized Western Blotting for Trypanosome Proteins

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Protein samples were run according to standard protein separation procedures, using SDS-PAGE. However, for VEX2 detection, the use of Bis-Tris gels with a neutral pH environment and a bis–tris/bicine based transfer buffer (containing a reducing agent and 10% methanol) were critical for protein separation and transfer, respectively (NuPAGE, Invitrogen). Otherwise, western blotting was carried out according to standard protocols. The following primary antibodies were used: rabbit α-VEX2 (1:1000), rabbit α-pol-I largest subunit17 (link) (1:500), rabbit α-VSG-2 (1:20,000), rabbit α-VSG-6 (1:20,000), mouse α-c-myc (Millipore, clone 4A6, 1:7,000), rabbit α-GFP (Abcam, 1:1,000) and mouse α-EF1α (Millipore, clone CBP-KK1, 1:20,000). We used horseradish peroxidase coupled secondary antibodies (α-mouse and α-rabbit, Biorad, 1:2000). Blots were developed using an enhanced chemiluminescence kit (Amersham) according to the manufacturer’s instructions. Densitometry was performed using Fiji v. 2.0.0.
Faria J., Glover L., Hutchinson S., Boehm C., Field M.C, & Horn D. (2019). Monoallelic expression and epigenetic inheritance sustained by a Trypanosoma brucei variant surface glycoprotein exclusion complex. Nature Communications, 10, 3023.
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2

Optimized Western Blot Protocol for VEX2 Detection

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Protein samples were run according to standard protein separation procedures, using SDS-PAGE. However, for VEX2 detection, the use of Bis-Tris gels with a neutral pH environment and a Bis-Tris/Bicine based transfer buffer (containing a reducing agent and 10% methanol) were critical for protein separation and transfer, respectively (NuPAGE, Invitrogen). Otherwise, western blotting was carried out according to standard protocols. The following primary antibodies were used: rabbit α-VEX2 (1:1,000), rabbit α-pol-I largest subunit 17 (link) (1:500), rabbit α-VSG-2 (1:20,000), rabbit α-VSG-6 (1:20,000), mouse α-c-myc (Millipore, clone 4A6, 1:7,000), rabbit α-GFP (Abcam Ab290, 1:1,000) and mouse α-EF1α (Millipore, clone CBP-KK1, 1:20,000). We used horseradish peroxidase coupled secondary antibodies (α-mouse and α-rabbit, Biorad, 1:2,000). Blots were developed using an enhanced chemiluminescence kit (Amersham) according to the manufacturer’s instructions. Densitometry was performed using Fiji v. 2.0.0. Uncropped blots are provided as Source Data Extended Data Figs 5 and 6.
Faria J., Luzak V., Müller L.S., Brink B.G., Hutchinson S., Glover L., Horn D, & Siegel T.N. (2021). Spatial integration of transcription and splicing in a dedicated compartment sustains monogenic antigen expression in African trypanosomes. Nature microbiology, 6(3), 289-300.
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3

Optimized Western Blot Protocol for VEX2 Detection

Check if the same lab product or an alternative is used in the 5 most similar protocols
Protein samples were run according to standard protein separation procedures, using SDS-PAGE. However, for VEX2 detection, the use of Bis-Tris gels with a neutral pH environment and a Bis-Tris/Bicine based transfer buffer (containing a reducing agent and 10% methanol) were critical for protein separation and transfer, respectively (NuPAGE, Invitrogen). Otherwise, western blotting was carried out according to standard protocols. The following primary antibodies were used: rabbit α-VEX2 (1:1,000), rabbit α-pol-I largest subunit 17 (link) (1:500), rabbit α-VSG-2 (1:20,000), rabbit α-VSG-6 (1:20,000), mouse α-c-myc (Millipore, clone 4A6, 1:7,000), rabbit α-GFP (Abcam Ab290, 1:1,000) and mouse α-EF1α (Millipore, clone CBP-KK1, 1:20,000). We used horseradish peroxidase coupled secondary antibodies (α-mouse and α-rabbit, Biorad, 1:2,000). Blots were developed using an enhanced chemiluminescence kit (Amersham) according to the manufacturer’s instructions. Densitometry was performed using Fiji v. 2.0.0. Uncropped blots are provided as Source Data Extended Data Figs 5 and 6.
Faria J., Luzak V., Müller L.S., Brink B.G., Hutchinson S., Glover L., Horn D, & Siegel T.N. (2021). Spatial integration of transcription and splicing in a dedicated compartment sustains monogenic antigen expression in African trypanosomes. Nature microbiology, 6(3), 289-300.
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