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Lysis buffer cell extraction buffer

Manufactured by Thermo Fisher Scientific
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Lysis buffer cell extraction buffer is a solution used to facilitate the extraction and isolation of cellular components, such as proteins, from biological samples. It is designed to disrupt the cell membrane and release the contents of the cells, allowing for further analysis or purification of the desired cellular components.

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Lab products found in correlation

Imagequant tl, by GE Healthcare (2 mentions) Pvdf membrane, by Bio-Rad (2 mentions) Ecl prime, by GE Healthcare (2 mentions) Novex tris glycine sds page, by Thermo Fisher Scientific (2 mentions) Anti fabp3, by LifeSpan BioSciences (2 mentions) Anti cpt1b, by Abcam (2 mentions) Anti actin, by Santa Cruz Biotechnology (2 mentions) Bca protein assay, by Thermo Fisher Scientific (2 mentions)

Close spelling variants of this product

Lysis buffer (523 citations) Cell extraction buffer (222 citations) Cell lysis buffer (171 citations) Extraction buffer (35 citations) Cell direct lysis extraction buffer (2 citations) RIPA cell lysis and extraction buffer (2 citations)

2 protocols using lysis buffer cell extraction buffer

1

Protein Expression Analysis in Muscle Tissue

Check if the same lab product or an alternative is used in the 5 most similar protocols
Muscle homogenates were prepared by grinding tissue with ice-cold lysis buffer cell extraction buffer (Invitrogen) as previously described (13 (link)). Protein concentrations were measured using a BCA protein assay (Thermo Scientific). Proteins were separated by 4–20% Novex Tris-Glycine SDS-PAGE (Invitrogen) and transferred to a PVDF membrane (Biorad). Membranes were incubated overnight with anti-FABP3 (Lifespan Biosciences, Seattle, WA; LS-C138955), anti-CPT1B (Abcam, Cambridge, MA; ab15703) or anti-actin (Santa Cruz, Dallas, TX; sc-1616), followed by incubation with appropriate secondary horseradish peroxidase-conjugated antibodies, anti-rabbit (GE Healthcare, Piscataway, NJ; NA931) and anti-goat (Santa Cruz, sc-2020). Immunoreactive proteins were visualized by chemiluminescence reagent (ECL Prime; GE Healthcare) and quantified by densitometric analysis using ImageQuantTL (GE Healthcare).
Mulya A., Haus J.M., Solomon T.P., Kelly K.R., Malin S.K., Rocco M., Barkoukis H, & Kirwan J.P. (2017). Exercise Training Induced Improvement in Skeletal Muscle PGC-1α Mediated Fat Metabolism is Independent of Dietary Glycemic Index. Obesity (Silver Spring, Md.), 25(4), 721-729.
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2

Protein Expression Analysis in Muscle Tissue

Check if the same lab product or an alternative is used in the 5 most similar protocols
Muscle homogenates were prepared by grinding tissue with ice-cold lysis buffer cell extraction buffer (Invitrogen) as previously described (13 (link)). Protein concentrations were measured using a BCA protein assay (Thermo Scientific). Proteins were separated by 4–20% Novex Tris-Glycine SDS-PAGE (Invitrogen) and transferred to a PVDF membrane (Biorad). Membranes were incubated overnight with anti-FABP3 (Lifespan Biosciences, Seattle, WA; LS-C138955), anti-CPT1B (Abcam, Cambridge, MA; ab15703) or anti-actin (Santa Cruz, Dallas, TX; sc-1616), followed by incubation with appropriate secondary horseradish peroxidase-conjugated antibodies, anti-rabbit (GE Healthcare, Piscataway, NJ; NA931) and anti-goat (Santa Cruz, sc-2020). Immunoreactive proteins were visualized by chemiluminescence reagent (ECL Prime; GE Healthcare) and quantified by densitometric analysis using ImageQuantTL (GE Healthcare).
Mulya A., Haus J.M., Solomon T.P., Kelly K.R., Malin S.K., Rocco M., Barkoukis H, & Kirwan J.P. (2017). Exercise Training Induced Improvement in Skeletal Muscle PGC-1α Mediated Fat Metabolism is Independent of Dietary Glycemic Index. Obesity (Silver Spring, Md.), 25(4), 721-729.
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