Antibody buffer

Fig. 38.3. Silver-oxidation voltammograms, obtained by using the sensor incubated in the solution (1) with the forest-spring encephalitis virus-directed antibodies (2) free of the forest-spring encephalitis virus-directed antibodies. Buffer solution pH = 7.2.

Other organic compounds 3,3, 4,4, 5-Pentachloro- Biacore 2000 2.5 ngmL 15 Antibody, Buffer [32]... 

Buffer (no -DES) coating Anti-DES antibody anti-rcd>bit-lgG antibody PNP DES (3 ug/ml) coating buffer (no anti-DES antibody) anti-red)bit IgG antibody PNP DES Anti-DES antibody buffer (no euiti-rabbit IgG antibody) PNP... 

DES anti-DES antibody anti-rabbit IgG antibody buffer (no PNP)... 

Blot buffer antibody buffer containing NaCl at a final concentration of 400 mM Procedure... 

Wash the cover slip with antibody buffer 3x5 min. 

Incubate the cover slip at 37°C in a damp chamber for 30 min with antibody diluted in antibody buffer. 

Antibody buffer PBS with 5 % goat serum and 0.2 % Triton X-100. 

Standard immunohistochemistry was carried out on sections prepared as described (Sect. 3.1). They were rinsed in PBS (2x10 min) and then placed in antibody birffer for 30 min at 18-20 °C. Sections were then incubated in the same solution containing the primary antibody (250 pL/well in a 24-well plate, three sections/well) for 70 h at 4 °C (control sections incubated in antibody buffer only). Sections were then washed three times for 10 min each in PBS at room temperature before incubation with secondary antibody diluted in the antibody buffer (including controls) for 3 h at 18-20 °C. Sections were washed twice for 10 min in PBS (three times for 10 min for CTIP2 detection). The sections used for CTIP2 detection were then incubated with streptavidin-Alexa 568 for 2 h at 18-20 °C diluted in antibody buffer, followed by two rinses in PBS. All sections were mounted on glass slides and coverslips applied with VECTASHIELD antifade solution. 

The working conditions of the immunosensor (enzyme and antigen concentrations, dilutions of the antibodies, pH of the buffer solution) were found. The cholinesterase immobilized demonstrated the maximum catalytic activity in phosphate buffer solution with pH 8.0. The analytical chai acteristics of the sensor - the interval of the working concentrations and detection limit - have been obtained. The proposed approach of immunoassay made possible to detect 5T0 mg/ml of the bacterial antigen. 

The antibody solution (1.6x10 M) and substrate solutions with various concentration from 10 M to 10 M were mixed on a BSA-coated plate. The mixed solution of antibodies and substrates was allowed to stand for 1 day at room temperature, and then transported to the ELISA plates pre-coated with BSA-hapten and BSA blocking buffer. Absorbance at 405 nm for the resulting enzymatic hydrolysis product (p-nitrophenolate) by alkalinephosphatase of the second antibody was recorded on an Immuno-Mini NJ-2300 to determine the amount of antibody bound to BSA-hapten. 

Fig.Sa-f. The sensorgram of the repeated injection of the aqueous viologen dimer 2 (a, c, e) and the antibody (b, d, f) solutions. [Viologen dimer 2]=2.0 pM and [antibody]=2.0 pM in phosphate borate buffer. Injection period 60 s for a-c and 120 s for d-f. A solution of viologen dimer 2 or the antibody passes over the surface of the sensor chip for 60 or 120 s at a constant flow rate of 20 pL min. The surface of the sensor chip was subsequently washed with buffer...

Fig. 12a,b. The sensorgrams for the binding of the antibody dendrimer (a) or IgG (b) to the anionic porphyrin immobilized onto the surface of the sensor chip. Phosphate borate buffer (0.1 M, pH 9.0) was used. TCPP was immobilized via hexamethylenediamine spacer onto the sensor chip and then a solution of IgG or the dendrimer was injected to the flow cell. After 60 s from the injection of the antibody solutions, flow ceU was filled with buffer... 

Alkaline phosphatase assays based on 3-glycerophosphate now appears to be obsolete, and methods buffered by either glycine or barbital are also obsolete as these buffers inhibit ALP or are poor buffers. Serum alkaline phosphatase is known to be composed of several isoenzymes which presumably arise from bone, liver, intestine, and placenta. The placental alkaline phosphatase is known to be much more resistant to heat denaturation than the other isoenzymes, and this resistance provides a simple test for it (5). The other enzymes can be separated through the differential inhibition by phenylalanine, by electrophoresis and by specific antibodies. However, the clinical usefulness of the results obtained is in doubt (23). 

We therefore developed an ELISA for the detection of soybean protein in processed foods using polyclonal antibodies raised against p34 as a soybean marker protein and using a specific extraction buffer (Morishita et ah, 2008). The p34 protein, originally characterized as an oil... 

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