Disease relevance of Eriosin Brilliant Cyanine G

• Threshold of pathological proteinuria measured with Coomassie Brilliant Blue [1].
• The identification of TCE visualized proteins is compared to the identification of Coomassie brilliant blue (CBB) stained proteins from two-dimensional gel electrophoresis of E. coli proteins [2].
• After Coomassie Brilliant Blue (CBB) staining, 1200 spots were detected and 140 major spots were excised from the gel and subjected to in-gel digestion with Achromobacter protease I (lysyl endopeptidase) [3].
• Moreover, a single local application, at the time of surgery, of Apyrase (which degrades ATP) or Coomassie Brilliant Blue (an antagonist of purinoreceptors) significantly reduced alveolar bone loss [4].
• Specific autolysis rates were calculated from the difference between initial and actual absorbances at different incubation times of Coomassie brilliant blue-stained protein [5].

High impact information on Eriosin Brilliant Cyanine G

• PAGE in the presence of 0.1% SDS demonstrates that striated flagellar roots are composed of a number of polypeptides, the most predominant one being a protein of 20,000 Mr. The 20,000 Mr protein band represents approximately 63% of the Coomassie Brilliant Blue staining of gels of isolated flagellar roots [6].
• A silver/Coomassie brilliant blue R-250 staining technique that permits a color-coded differentiation of erythrocyte membrane proteins, sialoglycoproteins, and lipids in a single one-dimensional NaDodSO4/polyacrylamide gel has been described [7].
• Polypeptides unique to the olfactory cilia preparation, compared to a control preparation of palate respiratory cilia, are identified by Coomassie brilliant blue staining, silver staining, and radiolabeled lectin overlays, as well as by biosynthetic labeling with 35S-methionine in epithelial explants and protein phosphorylation in isolated cilia [8].
• The activator protein, exhaustively purified and designated as activator II in this study, showed a single protein band on sodium dodecyl sulfate-, native-, and isoelectrofocussing-polyacrylamide slab gel electrophoresis after being stained with Coomassie Brilliant Blue. Its molecular weight and pI were 69,200 and 4.0, respectively [9].
• The strong staining of the TLX antigens with Coomassie Brilliant Blue and Amido Black indicates they are largely proteins [10].

Chemical compound and disease context of Eriosin Brilliant Cyanine G

• We compared the major polypeptides of epimastigotes and trypomastigotes of T. cruzi, by submitting total parasite lysates to electrophoresis in polyacrylamide gels (SDS-PAGE), protein staining with Coomassie brilliant blue, laser densitometry, or immunoblotting with sera derived from infected individuals (Chagas' disease) [11].
• A technique for isolation of rubella virus-like particles by sucrose gradient ultracentrifugation using Coomassie brilliant blue G crystals [12].
• After electrophoresis of total membrane preparations of Escherichia coli B on sodium dodecyl sulfate polyacrylamide gels, and subsequent staining with Coomassie Brilliant blue, a band corresponding to the Braun lipoprotein fails to appear [13].

Biological context of Eriosin Brilliant Cyanine G

• Induction of the lambda OLPL promoter caused the appearance of L-fucose-H+ symport activity and of a Coomassie brilliant blue-stained 32 kDa membrane protein expressed at high levels sufficient for identification as FucP by N-terminal protein sequencing [14].
• Reverse sister chromatid differential staining by Coomassie Brilliant blue R-250 [15].
• After the protein spots had been electroblotted onto a polyvinylidene difluoride membrane and stained with Coomassie Brilliant Blue, the N-terminal amino acid sequences were determined for about twenty protein spots [16].
• The comparison between such maps showed up- and downregulation of 45 polypeptide chains, of which 32 were downregulated and 13 upregulated, out of a total of 700 spots detected by a medium-sensitivity stain, micellar Coomassie Brilliant Blue. Fingerprinting by mass spectrometry analysis enabled the identification of 36 of these spots [17].
• Enzymic deglycosylation of several chromatographic fractions of ribonuclease, which have different degrees of glycosylation, results in increased staining by Coomassie Brilliant Blue R-250 [18].

Anatomical context of Eriosin Brilliant Cyanine G

• The most prominent membrane protein of these endosomes is one of 68 kDa, as revealed by silver and Coomassie Brilliant Blue staining of SDS-gel electrophoretograms [19].
• Combined immunostaining and Coomassie Brilliant Blue staining of polyvinylidene difluoride membranes without organic solvent [20].
• A continuous-flow technique with Coomassie Brilliant Blue for cerebrospinal fluid protein assay [21].
• Total protein determined in human breast milk by use of coomassie brilliant blue and centrifugal analysis [22].
• In addition, these studies suggest that a modified staining method that combines both silver stain and CBB stain provides improved detection of cell wall proteins compared to either method alone [23].

Associations of Eriosin Brilliant Cyanine G with other chemical compounds

• Fluoride affects Coomassie Brilliant Blue measurement of protein in cerebrospinal fluid [24].
• One method depends upon the reduction by living cells of the tetrazolium salt MTT to form a blue formazan product, whereas the other relies on rapid binding of the dye Coomassie brilliant blue to protein at acidic pH [25].
• Using Amido Black, Coomassie Brilliant Blue R-250 and Ponceau S, we have obtained, in comparison with the non-dried membranes, an enormous increase in the number of detectable proteins [26].
• Several new staining methods for polyvinylidene difluoride membranes, including mercurochrome, silver and dimethylaminoazobenzene isothiocyanate staining were compared with Coomassie Brilliant Blue and gold staining [27].
• These were adduced in both sodium dodecyl sulphate (SDS) and native polyacrylamide gel electrophoresis and consisted of ethanol-acetic acid-formaldehyde fixation, Coomassie Brilliant Blue prestaining, Rapidfix pretreatment, formaldehyde enhancement and finally ammoniacal silver staining [28].

Gene context of Eriosin Brilliant Cyanine G

• The slower moving band, which probably corresponded to the higher polymeric form of the G6PD with high specific activity, was not seen on native PAGE due to insufficient protein for Coomassie brilliant blue staining [29].
• When normal human serum and properdin were allowed to diffuse toward each other in agar gel for 16 hr, a line of precipitation could be seen when stained with Coomassie brilliant blue [30].
• In the SDS-PAGE, one major band with a molecular weight of 56,000 and one minor band with 15,000 were stained with Coomassie Brilliant Blue and both showed DIF activity after extraction from gels [31].
• KN-62 inhibited an increase in calcium entry induced by 4AP, while brilliant blue G (BBG) prevented it, supporting the hypothesis that purinergic P2X7 receptors are involved in this action [32].
• The matrix metalloproteinase MMP13, a secretory protein, was expressed in MDCK cells at a level high enough to be detectable in crude supernatants without concentration on sodium dodecyl sulfate-polyacrylamide gel electrophoresis stained with Coomassie brilliant blue R-250 [33].

Analytical, diagnostic and therapeutic context of Eriosin Brilliant Cyanine G

• Following endofacial labeling of ghosts with [35S]glutathione-maleimide, autoradiography reveals radioactivity in all of the major Coomassie brilliant blue bands [34].
• Protein bands were visualized by staining with Coomassie Brilliant Blue, excised, and counted in a liquid scintillation counter [35].
• After electrofocusing, these fractions yielded 15, 12, and 11 Coomassie brilliant blue-staining bands, respectively [36].
• By measuring antipeanut-specific IgE in the ELISA and in IgE-specific immunoblotting, we identified an allergenic component with two Coomassie brilliant blue staining bands by sodium dodecyl sulfate-polyacrylamide gel electrophoresis with a mean molecular weight of 63.5 kd [37].
• In the present study we evaluated the performance of a software/scanner system that employed the Hewlett Packard (HP) ScanJet Plus and Scanplot Software for densitometric quantification of protein loads stained with Coomassie Brilliant Blue following sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) [38].

References