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Biotinylated serum albumins

Biotinylated proteins such as immunoglobulins and serum albumins or biotinylated oligonucleotides can bind through affinity interactions streptavidin-functiona-lized Au NPs [156, 157]. [Pg.164]

Table 3.7.1 Colorimetric assay of plasma biotinidase activity pipetting schedule and typical absorbance values obtained with normal plasma. B-PABA biotinyl-p-aminobenzoic acid, BSA bovine serum albumin, DTT dithiothreitol, PABA p-aminobenzoic acid, S substrate stock solution... Table 3.7.1 Colorimetric assay of plasma biotinidase activity pipetting schedule and typical absorbance values obtained with normal plasma. B-PABA biotinyl-p-aminobenzoic acid, BSA bovine serum albumin, DTT dithiothreitol, PABA p-aminobenzoic acid, S substrate stock solution...
Bovine serum albumin (BSA) 1992 A Factor 100,000 (IPCR 9.6 x 10 22 mol ELISA 96 amol) Sano et al. [10], initial publication of the IPCR STV-protein A chimera for coupling biotinylated DNA with an antibody (see Fig. 2A and Section 2.1.1)... [Pg.246]

Fig. 8. Determination of coefficients of variation for protein microarrays. Replica spotting of Cy3 -labeled, biotinylated bovine serum albumin allows the intra- and interarray spot-to-spot reproducibility to be determined. Fig. 8. Determination of coefficients of variation for protein microarrays. Replica spotting of Cy3 -labeled, biotinylated bovine serum albumin allows the intra- and interarray spot-to-spot reproducibility to be determined.
In 2001, Van Orden et al. reported the first biologically relevant FRET investigation using QDs as energy donors.83 They conjugated biotinylated bovine serum albumin (bBSA) to water-soluble CdSe-ZnS-TA QDs via a thiol linkage with 2-iminothiolane. The acceptor was streptavidin covalently labeled with tetra-methylrhodamine (TMR). Once the avidin-biotin interaction took place, a decrease in the QD luminescence and an increase in the TMR luminescence were observed, which was attributed to FRET between QD and TMR. Although no time-resolved fluorescence experiments were carried out and no estimates for the separation distance... [Pg.390]

Figure 12.7 Protein-protein interaction assays performed on filled-squared ZnO NR arrays. (A) Interaction between biotinylated bovine serum albumin (BBSA) and dichlorotriazinylaminofluorescein (DTAF) conjugated streptavidin leads to strong fluorescence emission shown in panels 4 and 5. As-grown ZnO NR arrays do not show any autofluorescence. SEM micrograph of as-synthesized NR arrays is displayed in panel 1 and the corresponding fluorescence emission of as-grown NR arrays is shown in panel 2. (B) Strong fluorescence signal is visible when an alternative fluorophore, exhibiting different absorption and emission profiles than... Figure 12.7 Protein-protein interaction assays performed on filled-squared ZnO NR arrays. (A) Interaction between biotinylated bovine serum albumin (BBSA) and dichlorotriazinylaminofluorescein (DTAF) conjugated streptavidin leads to strong fluorescence emission shown in panels 4 and 5. As-grown ZnO NR arrays do not show any autofluorescence. SEM micrograph of as-synthesized NR arrays is displayed in panel 1 and the corresponding fluorescence emission of as-grown NR arrays is shown in panel 2. (B) Strong fluorescence signal is visible when an alternative fluorophore, exhibiting different absorption and emission profiles than...
Figure 12.8 Protein protein interaction reactions carried out in parallel on the same, striped ZnO NR platform using a microfluidic chamber. Panel 1 displays SEM micrograph of the striped ZnO NR arrays. Fluorescence signal is observed only from the diambers containing interacting pairs of proteins, chambers 2 and 3. No fluorescence is detected from ZnO NRs in chambers 1 and 4. Hie model protein pairs used in the control experiments include fibronectin (Fn), immunoglobulin G (IgG), biotinylated bovine serum albumin (BBSA), DTAF-streptavidin. Figure 12.8 Protein protein interaction reactions carried out in parallel on the same, striped ZnO NR platform using a microfluidic chamber. Panel 1 displays SEM micrograph of the striped ZnO NR arrays. Fluorescence signal is observed only from the diambers containing interacting pairs of proteins, chambers 2 and 3. No fluorescence is detected from ZnO NRs in chambers 1 and 4. Hie model protein pairs used in the control experiments include fibronectin (Fn), immunoglobulin G (IgG), biotinylated bovine serum albumin (BBSA), DTAF-streptavidin.
For every 10 mL of complex required, dilute 50 ilL of the streptavidin stock to 5 mL with bovine serum albumin solution. Similarly, dilute 50 iL of the stock solution of the biotinylated enzyme. [Pg.147]

Blocking solution and diluent Bovine serum albumin (2%), in PBS. Biotinylated primary antibody 0.5 mg/mL in diluent Ferritin-conjugated avidin 1 mg/mL protein in diluent... [Pg.152]

Carrier protein solution Biotinylated bovine serum albumin (0.1 mg/ mL) diluted in 2% underivatized bovine serum albumin (in PBS). Radioactive antigen I-labeled (about 2 x 10 cpm/mL) in PBS. [Pg.153]

Nitro substituted carboxylic acids, N,N-dicyclohexylcarbodiimide (DCC) and N-hydroxysuccinimide were obtained from the Aldrich Chemical Co. (Milwaukee, WI). Avidin-labeled horseradish peroxidase, biotinylated anti-rabbit IgG, ovalbumin ( M.W. 45,000), bovine serum albumin (M.W. 66,000) Freund s complete adjuvant, Freund s incomplete adjuvant, and o-phenylenediamine were purchased from Sigma Chemical Co.(St. Louis, MO). All solvents were reagent grade. DME (1,2-dimethoxyethane) was dried by distillation from sodium-potassium amalgam/benzophenone ketyl. [Pg.82]

Dimyristoylphosphatidylethanolamine (DMPE), biotinyl-N-hydroxysuccinimide ester (BNHS), triethylamine, myoglobin, bovine serum albumin (BSA), lysozyme, guanidinium chloride, dimethylamino-cinnamaldehyde, acrylamide, ammonium persulfate, sodium dodecyl sulfate (SDS), and molybdenum blue reagent were all obtained from Sigma Chemicals and used without further purification as received. The compounds N, N, N, N -tetramethylethylenediamine (TEMED), N, N -methylene-bis-acrylamide, and Coomassie Brilliant Blue R-250 were from BioRad Laboratories. Avidin was obtained from Vector Laboratories with a quoted activity of 14 units/mg. All solvents were from Fisher Scientific. Water was passed through a Barnstead Nanopure system. [Pg.217]

The choice of blocking buffer is sometimes critical for sensitive detection. Milk based blocking solutions are not recommended for use avidin-biotin system because milk contains biotin, which may directly cause competition with biotinylated antibody." Bovine Serum Albumin was not selected in this system in order to avoid the cross-reactivity. Therefore, gelatin was chosen as the blocking agent. [Pg.496]


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See also in sourсe #XX -- [ Pg.164 ]




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Albumin, serum

Biotinylated

Biotinylated bovine serum albumin

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