α myc tag

Manufactured by Cell Signaling Technology

Sourced in United States

The α-myc tag is a laboratory equipment product manufactured by Cell Signaling Technology. It is designed to detect the presence and location of the c-Myc protein in various biological samples.

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Lab products found in correlation

Protease inhibitor cocktail, by Roche (3 mentions) 710 confocal microscope, by Zeiss (3 mentions) α cytochrome oxidase subunit 1, by BD (2 mentions) α hsp60 mitochondrial, by BD (2 mentions) α myc tag, by Merck Group (1 mentions) α gm130, by BD (1 mentions) α eea1, by Abcam (1 mentions) Fv1000 confocal microscope, by Zeiss (1 mentions) α lc3b, by Cell Signaling Technology (1 mentions)

4 protocols using α myc tag

Protein Extraction and Western Blot Analysis

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Protein extracts from treated and control cells were prepared using lysis solution containing 10 mM Tris-HCl, 1% SDS, 1x EDTA-free protease inhibitor cocktail (Roche, Indianapolis, IN). Protein concentrations were measured using the BCA assay (Pierce, Rockford, IL, USA). Proteins were separated by PAAG electrophoresis and transferred to PVDF membranes, blocked and incubated with primary and secondary antibodies using standard techniques [20 ]. Blots were developed with SuperSignal West Pico and exposed to CL-Xposure film (both Pierce). Primary antibodies were α-HSP60 (mitochondrial, BD Biosciences), α-cytochrome oxidase subunit 1 (AbCam), α-Lig3 and α-MnSOD (BD Biosciences), α-myc Tag (Cell Signaling Technology) and α-TOM-70 (Proteintech).

Spadafora D., Kozhukhar N, & Alexeyev M.F. (2016). Presequence-Independent Mitochondrial Import of DNA Ligase Facilitates Establishment of Cell Lines with Reduced mtDNA Copy Number. PLoS ONE, 11(3), e0152705.

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Western Blot Analysis of Protein Expression

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Protein extracts from treated and control cells were prepared using lysis solution containing 10 mM Tris-HCl, 1% SDS, 1× EDTA-free protease inhibitor cocktail (Roche, Indianapolis, IN). Protein concentrations were measured using the BCA assay (Pierce, Rockford, IL). Proteins were separated by PAGE and transferred to PVDF membranes, blocked, and incubated with primary and secondary antibodies using standard techniques (Sambrook & Russel, 2001 ). Blots were developed with SuperSignal West Pico and exposed to CL-Xposure film (both Pierce, Rockford, IL). Primary antibodies were α-myc tag (Cell Signaling), α-HSP60 (mitochondrial, BD Biosciences, San Jose, CA), α-cytochrome oxidase subunit 1 (AbCam, Cambridge, UK).

Kozhukhar N., Spadafora D., Fayzulin R., Shokolenko I.N, & Alexeyev M. (2015). The efficiency of the translesion synthesis across abasic sites by mitochondrial DNA polymerase is low in mitochondria of 3T3 cells. Mitochondrial DNA. Part A, DNA mapping, sequencing, and analysis, 27(6), 4390-4396.

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Immunofluorescence Staining and Live-Cell Imaging

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For Immunofluorescence studies, cells were grown on glass coverslips for 2 days, then the coverslips were washed once in PBS and then fixed with 4% p-formaldehyde for 30 min at room temperature. Immunofluorescence staining of cells was carried out as previously described.^{39 (link)} An Olympus FV1000 confocal microscope with a 60 × objective and a Zeiss 710 confocal microscope with × 63 objective were used for taking images.
Antibodies used were as follows: α-Myc-Tag (Millipore; 4A6), α-Myc-Tag (Cell Signaling; #2272), α-LC3B (Cell Signaling; #2775), α-LAMP2 (BD Pharmingen, San Jose, CA, USA; CD107b), α-EEA1 (Abcam, ab2900), α-Calnexin (Cell Signaling; #2679), α-WIPI2 (Bio-rad; MCA578OGA) and α-GM130 (BD Bioscience, #610822).
For live-cell imaging, cells were transfected with GFP-tagged DRAM-3 and RFP-tagged Rab5 or Rab7 at least 2 days before confocal analysis. An Andor spinning disc confocal system with Cairn Optsplit (for simultaneous GFP/RFP imaging) was used for imaging. Videos of endosomes were taken for 1 min, with pictures in 1-s intervals.

Mrschtik M., O'Prey J., Lao L.Y., Long J.S., Beaumatin F., Strachan D., O'Prey M., Skommer J, & Ryan K.M. (2015). DRAM-3 modulates autophagy and promotes cell survival in the absence of glucose. Cell Death and Differentiation, 22(10), 1714-1726.

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Western Blot Analysis of Protein Extracts

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Protein extracts from treated and control cells were prepared using lysis solution containing 10 mM Tris-HCl, 1% SDS, 1 × EDTA-free protease inhibitor cocktail (Roche, Indianapolis, IN). Protein concentrations were measured using the BCA assay (Pierce, Rockford, IL). Proteins were separated by PAAG electrophoresis and transferred to PVDF membranes, blocked and incubated with primary and secondary antibodies using standard techniques (Sambrook & Russel, 2001 ). Blots were developed with SuperSignal West Pico and exposed to CL-Xposure film (both Pierce). Primary antibodies were α-myc tag (Cell Signaling), α-HSP60 (mitochondrial, BD Biosciences).

Shokolenko I.N., Wilson G.L, & Alexeyev M.F. (2014). The “fast” and the “slow” modes of mitochondrial DNA degradation. Mitochondrial DNA. Part A. DNA mapping, sequencing, and analysis, 27(1), 490-498.

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