Bradford protein assay

About: Bradford protein assay is a research topic. Over the lifetime, 635 publications have been published within this topic receiving 239107 citations.

Absolute protein assay for the simultaneous quantification of two epoxide hydrolases in rats by mass spectrometry-based targeted proteomics.

Abstract: Epoxide hydrolases catalyze the hydrolysis of both exogenous and endogenous epoxides to the corresponding vicinal diols by adding water. Microsomal and soluble epoxide hydrolase are two main mammalian enzymes that have been intensely characterized. The purpose of this investigation was to develop and validate a proteomics assay allowing the simultaneous quantification of microsomal and soluble epoxide hydrolase in rats. Protein quantification was realized through targeted proteomics using liquid chromatography with tandem mass spectrometry for the determination of trypsin-specific surrogate peptides after digestion. Stable isotope-labeled peptides were used as the internal standards. The chromatography of the surrogate peptides was performed on an Agilent SB C18 column (100 mm × 4.6 mm, 1.8 µm) with gradient elution. Acetonitrile containing 0.1% formic acid and 0.1% formic acid aqueous solution were used as mobile phases. A multiple reaction monitoring method in a positive ionization mode was used for the simultaneous detection of the peptides. The method was validated concerning the specificity, linearity, within-day and between-day accuracy and precision, matrix effect, stability, and digestion efficiency. The developed assay was successfully used to quantify the protein levels of microsomal and soluble epoxide hydrolase in rat liver, kidney, and heart S9 samples.

Quantitative peptide or protein assay

Abstract: Peptide and/or protein quantitation methods, kits, and compositions, particularly useful for mass spectrometry, are provided herein based on a bathocuproine-based composition complex such as bathocuproinedisulfonic acid disodium salt hydrate complex. The methods are one-step rapid absorbance methods using small sample volumes. They produce a robust signal with high signal to background ratio and accurately quantitate even complex peptide mixtures with low variability and high sensitivity.

Method for detecting angiogenesis promoting capacity of MSC through VCAM-1

Abstract: The invention discloses a method for detecting the angiogenesis promoting capacity of an MSC through VCAM-1. The method is characterized in that a new purpose of known protein VCAM-1 is found, the protein expression of VCAM-1 is detected through an ELISA, the total protein content is measured through a Bradford method, and the angiogenesis promoting capacity of the cell is reflected through the protein content of VCAM-1 in every 1 g of total protein. The angiogenesis promoting capacity of the MSC can be quantified through the method.

Ponceau 4R: A Novel Staining Agent for Resolve Food Proteins on PAGE and Its Impact on Digestibility

Abstract: Ponceaue 4R interaction with protein, Nisin and BSA was concentration dependent and may be used for protein assay. As the dye binds with almost all the proteins and current methodology may be used for the estimation of proteins in various food systems. During the course of present work staining with ponceau 4R of resolved proteins on PAGE (poly acryl amide gel electrophorosis) was comparable with Coommassie Brilliant Blue R250. The Ponceaue 4R was highly sensitive, rapid and produced sharp red bands on the gel on 0.2% concentration. The effects of pH, concentration of proteins and dye were also investigated in various conditions which would help food processors to use a calculated amount of dye. The impact of tryptic digestibility on Ponceaue 4R -Protein Complexes (PPC) has illustrated that dye may safely be used without any adverse effect on the digestion of PPC.