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Anti fabp3

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Anti-FABP3 is a laboratory product used to detect and quantify the presence of Fatty Acid Binding Protein 3 (FABP3) in biological samples. FABP3 is a cytoplasmic protein involved in the intracellular transport of fatty acids. The Anti-FABP3 product provides a tool for researchers to study FABP3 expression and regulation in various experimental models and clinical applications.

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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 cpt1b, by Abcam (2 mentions) Lysis buffer cell extraction buffer, by Thermo Fisher Scientific (2 mentions) Anti actin, by Santa Cruz Biotechnology (2 mentions) Bca protein assay, by Thermo Fisher Scientific (2 mentions)

2 protocols using anti fabp3

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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