Bca reagent

Manufactured by Boster Bio

Sourced in China

The BCA reagent is a colorimetric detection kit used for the quantitation of total protein concentration. It works by the combination of the Biuret reaction and the chelation of copper with bicinchoninic acid (BCA), resulting in a purple-colored complex that absorbs light at 562 nm. This reagent provides a simple, reliable, and accurate method for protein determination.

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Lab products found in correlation

Bradford reagent, by Boster Bio (2 mentions) Gapdh, by Cell Signaling Technology (2 mentions) Protease inhibitor cocktail, by Roche (2 mentions) Lamin a c, by Santa Cruz Biotechnology (2 mentions) Gapdh, by Abcam (1 mentions) P glycoprotein, by Abcam (1 mentions) Radioimmunoprecipitation assay (ripa), by Beyotime (1 mentions) Cyp2c9, by Abcam (1 mentions) Flag tag antibody, by Proteintech (1 mentions)

Spelling variants of this product

BCA protein assay reagent (9 citations) BCA protein assay reagent kit (3 citations)

4 protocols using bca reagent

Protein Expression Analysis in Liver and Ileum

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Liver and terminal ileum tissue samples were homogenized in RIPA (Beyotime Biotechnology, China), respectively. The total protein concentrations of the homogenates were measured with BCA reagent (BOSTER, China). An equal amount of protein was subjected to sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and transferred to polyvinylidene difluoride membranes by electroblotting. After blocking, the membranes were incubated with primary antibodies directed against human CYP1A2, CYP3A4, CYP2C9, P-glycoprotein, and GAPDH (Abcam, UK). Software ImageJ was used to analyze the Gray scale of the obtained images:
Gray value of each protein = gray value of target protein/gray value of internal reference protein.

Chen W., Qian J., Fu J., Wu T., Lv M., Jiang S, & Zhang J. (2022). Changes in the Gut Microbiota May Affect the Clinical Efficacy of Oral Anticoagulants. Frontiers in Pharmacology, 13, 860237.

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Subcellular Fractionation and Protein Quantification

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Isolation of cytosolic and nuclear fractions was performed as previously described20 . Heart samples were lysed using tissue homogenizer in buffer-A containing 10 mM HEPES-KOH (pH 7.9), 10 mM KCl, 1.5 mM MgCl₂, 1 mM EDTA, 0.6% NP-40, 0.5 mM DTT, protease inhibitor cocktail (Roche diagnostics GmbH, Mannheim, Germany) and lysates were incubated for 10 min on ice. After brief vortexing the lysates were centrifuged for 10 min at 5,000 rpm at 4°C. Supernatants were collected as cytosolic fractions and the pellets were resuspended in 100 ml of buffer-B containing 10 mM HEPES-KOH (pH 7.9), 25% glycerol, 420 mM NaCl, 1.5 mM MgCl₂, 0.2 mM EDTA, 0.5 mM DTT and protease inhibitors. Lysates were incubated for 20 min on ice followed by centrifugation at 12,000 g at 4°C for 10 min. Supernatants containing the nuclear extracts were collected and stored at - 80°C.
A similar procedure was used for isolation of cytosolic and nuclear fractions of cells where buffer-A contains 10 mM HEPES-KOH (pH 7.9), 10 mM KCl, 1.5 mM MgCl₂, 0.5 mM DTT and protease inhibitors. Protein concentration was measured using Bradford reagent or BCA reagent (Boster, Wuhan, China), and purity of nuclear and cytoplasmic fractions was determined by Lamin A/C (Santa Cruz Biotechnology, Inc) and GAPDH (Cell Signaling Technology, Danvers, MA) western blots, respectively.

Wang T., Wu J., Dong W., Wang M., Zhong X., Zhang W., Dai L., Xie Y., Liu Y., He X., Liu W., Madhusudhan T., Zeng H, & Wang H. (2021). The MEK inhibitor U0126 ameliorates diabetic cardiomyopathy by restricting XBP1's phosphorylation dependent SUMOylation. International Journal of Biological Sciences, 17(12), 2984-2999.

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Flagged Protein Interactome Profiling

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LN229-MAEA-OE cells were lysed in IP buffer (87787, Thermo Fisher Scienti c) containing inhibitor cocktail (4693116001, Roche). The protein concentration was determined by BCA reagent (AR0197, Boster Biological Technology). Subsequently, the cell lysates were incubated overnight with magnetic protein-G beads and Flag-tag antibody (80010-1-RR, Proteintech). The beads were then sent to PTM BIO for analysis by mass spectrometer (TMQ Exactive Plus, Thermo Fisher Scienti c).

Zhou P., Peng X., Tang S., Zhang K., Tan Z., Li D., Shen L., Peng J, & Yang L. (2023). E3 ligase MAEA-mediated ubiquitination and degradation of PHD3 promotes glioblastoma progression. Oncogene, 42(16).

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Isolation of Cytosolic and Nuclear Fractions

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Isolation of cytosolic and nuclear fractions was performed as previously described [20] . Heart samples were lysed using tissue homogenizer in buffer-A containing 10 mM HEPES-KOH (pH 7.9), 10 mM KCL, 1.5 mM MgCl2, 1 mM EDTA, 0.6% NP-40, 0.5 mM DTT, protease inhibitor cocktail (Roche diagnostics GmbH, Mannheim, Germany) and lysates were incubated for 10 min on ice. After brief vortexing the lysates were centrifuged for 10 min at 5,000 rpm at 4°C. Supernatants were collected as cytosolic fractions and the pellets were resuspended in 100 ml of buffer-B containing 10 mM HEPES-KOH (pH 7.9), 25% glycerol, 420 mM NaCl, 1.5 mM MgCl 2 , 0.2 mM EDTA, 0.5 mM DTT and protease inhibitors. Lysates were incubated for 20 min on ice followed by centrifugation at 12,000 g at 4°C for 10 min. Supernatants containing the nuclear extracts were collected and stored at - 80°C.
A similar procedure was used for isolation of cytosolic and nuclear fractions of cells where buffer-A contains 10 mM HEPES-KOH (pH 7.9), 10 mM KCL, 1.5 mM MgCl2, 0.5 mM DTT and protease inhibitors. Protein concentration was measured using Bradford reagent or BCA reagent (Boster, Wuhan, China), and purity of nuclear and cytoplasmic fractions was determined by Lamin A/C (Santa Cruz Biotechnology, Inc) and GAPDH (Cell Signaling Technology, Danvers, MA) western blots, respectively.

Wang T., Wu J., Dong W., Wang M., Zhong X., Zhang W., Dai L., Xie Y., Liu Y., He X., Liu W., Madhusudhan T., Zeng H., & Wang H. (2021). The MEK Inhibitor U0126 Ameliorates Diabetic Cardiomyopathy By Restricting Xbp1’s Phosphorylation Dependent SUMOylation.

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