α hsp60 mitochondrial

Manufactured by BD

α-HSP60 (mitochondrial) is a laboratory equipment product. It functions as a molecular chaperone involved in the folding and assembly of proteins within the mitochondria.

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Lab products found in correlation

α myc tag, by Cell Signaling Technology (2 mentions) Protease inhibitor cocktail, by Roche (2 mentions) α cytochrome oxidase subunit 1, by BD (1 mentions) Protease inhibitor cocktail, by Merck Group (1 mentions) Bca assay, by Thermo Fisher Scientific (1 mentions) Supersignal west pico, by Thermo Fisher Scientific (1 mentions)

3 protocols using α hsp60 mitochondrial

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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Western Blot Analysis of Cellular Proteins

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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 (Sigma-Aldrich cat# 11873580001). Protein concentrations were measured using the BCA assay (Thermo Scientific Pierce cat# 23227). Proteins were separated by polyacrylamide gel electrophoresis and transferred to PVDF membranes, blocked and incubated with primary and secondary antibodies using standard techniques [26 ]. Blots were developed with SuperSignal West Pico and exposed to CL-Xposure film (Thermo Scientific Pierce cat# 34080 and #34088, respectively). Primary antibodies were α-myc tag (Cell Signaling Tehnology cat# 2276), α-HSP60 (mitochondrial, BD Biosciences cat# 611562), and α-cytochrome oxidase subunit 2 (AbCam cat#ab91317).

Spadafora D., Kozhukhar N., Chouljenko V.N., Kousoulas K.G, & Alexeyev M.F. (2016). Methods for Efficient Elimination of Mitochondrial DNA from Cultured Cells. PLoS ONE, 11(5), e0154684.

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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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