The final result was approximately 50 μl of nucleic acid in elution buffer.

Elute immunoprecipitate from resin with elution buffer.

Proteins were eluted using reduced glutathione elution buffer (50 mM Tris.

Gentle elution buffer systems that employ high salt concentrations are also available to avoid exposing sensitive antibodies to low pH.

Using an acidic elution buffer, the adherent phage are removed and neutralised with Tris base.

The selection of the elution buffer is co-determined by the contemplated use of the isolated NA.

An elution with a low pH buffer or a more gentle, high salt elution buffer is then used to recover purified antibody from the support.

An elution buffer removes the DNA from channel walls, and the DNA is collected at the end of the channel.

The eluate is collected into a neutral tris or phosphate buffer, to neutralize the low pH elution buffer and halt any degradation of the antibody's activity.

The mRNA was then suspended in 20 μl of elution buffer and the concentration was determined by measuring the attenuance at a wavelength of 260 nm.

The DNA is then washed to remove any excess waste particles from the sample and then eluted from the channel using an elution buffer for further downstream processing.

NA presented in the washed (and preferably dried) silica-nucleic acid complexes is eluted into elution buffer such as TE buffer, aqua bidest, ... , and so on.

EGTA is used as a compound in elution buffer in the protein purification technique known as tandem affinity purification, in which recombinant fusion proteins are bound to calmodulin beads and eluted out by adding EGTA.

Alternatively binding may be achieved using a batch treatment, by adding the initial mixture to the solid phase in a vessel, mixing, separating the solid phase (for example), removing the liquid phase, washing, re-centrifuging, adding the elution buffer, re-centrifuging and removing the eluate.

Batch adsorption recovers the product in a larger volume of elution buffer than does column chromatography or frontal chromatography, and the resulting more dilute product requires concentration, typically on a membrane system, which can lead to loss of product by irreversible adsorption to the membrane.

Binding to the solid phase may be achieved by column chromatography whereby the solid medium is packed onto a column, the initial mixture run through the column to allow setting, a wash buffer run through the column and the elution buffer subsequently applied to the column and collected.

In the most common FPLC strategy, ion exchange, a resin is chosen so that the protein of interest will bind to the resin by a charge interaction while in buffer A (the running buffer) but become dissociated and return to solution in buffer B (the elution buffer).