Examples of 'mm imidazole' in a sentence
Meaning of "mm imidazole"
This phrase refers to a chemical compound known as imidazole, which is often used in scientific research, laboratory experiments, or pharmaceutical applications. The 'mm' in 'mm imidazole' could potentially refer to a specific concentration or dosage of the compound, depending on the scientific context in which it is used. Further information is required to provide a more accurate explanation
How to use "mm imidazole" in a sentence
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mm imidazole
About 8 mM imidazole was needed to elute the column.
Column was washed with the same buffer followed by buffer containing 50 mM imidazole.
During the 20 mM imidazole wash loosely attached contaminating proteins were elution of the column.
The column was washed with equilibration buffer and eluted with buffer solution containing 50 mM imidazole.
Bound proteins were eluted with 50 mM imidazole in wash buffer.
The column was washed using a modified Buffer C which additionally contained 10 mM imidazole.
Protein was eluted with 400 mM imidazole and analysed as previously described.
The column was then washed with 25 mM imidazole.
The protein is eluted with 250 mM imidazole following the Qiagen instructions.
The protein was eluted in the same buffer containing 200 mM imidazole.
Nanobodies were eluted from the column with 250 mM imidazole and subsequently desalted towards dPBS.
Bound proteins were eluted using an elution buffer containing 300 mM imidazole.
Nanobodies were eluted from the column with 150 mM imidazole and subsequently dialyzed against PBS.
The scFv was then eluted in wash buffer containing 250 mM imidazole.
SDS-PAGE analysis showed that 350 mM imidazole was the optimal elution condition for these recombinants.
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After renaturation the proteins are eluted by the addition of 250 mM imidazole.
The 200 mM imidazole elution fractions were pooled and desalted.
The product is eluted from the resin with a buffer containing 20 mM imidazole.
Proteins are eluted with 250 mM imidazole in sonication buffer on a gravity column ( BioRad ).
After renaturation the proteins can be eluted by the addition of 250 mM imidazole.
A second wash using same buffer+10 mM imidazole was performed, producing a “ wash fraction 2.
The protein was eluted with the same buffer containing 250 mM imidazole.
The mutants were washed with 40mM imidazole followed by elution at 500 mM Imidazole.
The resin was then eluted with the elution buffer containing 100 mM imidazole.
The native protein was then eluted by 500 mM imidazole in the same buffer.
For purification of the deca-His-tagged proteins, starting materials were supplemented with 1 mM imidazole.
The tagged protein eluted at 100 mM imidazole concentration.
The recombinant proteins were then eluted with the same buffer containing 100 mM imidazole.
The proteins were eluted by a solution containing 100 mM imidazole in the appropriate buffer.
The supernatant was loaded on a Nickel-Sepharose column pre-equilibrated with buffer containing 5 mM Imidazole.
The column was washed with the loading buffer containing 35 mM imidazole followed by 50 mM imidazole.
The BCAT enzyme was then eluted with the same buffer but with 350 mM imidazole.
The AAT was then eluted with 10 mM imidazole solution.
The bound protein was eluted by buffer A containing 250 mM imidazole.
The recombinant HA ectodomain were eluted with 500 mM imidazole in 20 mM Hepes buffer.
The initial elution was carried out using Buffer A + 25 mM imidazole.
Then the lysates were supplemented with 10 % glycerole and 20 mM imidazole and recentrifuged.
The aqueous receptor solution was 15 mM sodium chloride buffered to pH 7 with 10 mM imidazole.
The protein was eluted with 300 mM imidazole in PBS.
Buffer B was the same as buffer A except for the inclusion of 500 mM imidazole.
The packed resin is washed with 15 mM Imidazole.
This washing was followed by 7 column volumes of 20 mM sodium phosphate and 10 mM imidazole.
KDR protein is eluted in 1X KB containing a linear gradient of 200 mM imidazole over 10 column volumes.
The bound E1 * protein was then eluted with equilibration buffer containing 250 mM imidazole.
Fusion protein was eluted with 250 mM imidazole.
The protein is eluted with 6 volumes of lysis buffer containing 250 mM imidazole.
As a result, it was confirmed that a desired protein was contained in 20-30 mM imidazole elution fraction.
The purified protein is eluted with 5 ml lysis buffer containing 200 mM imidazole.
The Alpha-1 antitrypsin is then eluted with 10 mM imidazole solution.
The protein was eluted with buffer containing 250 mM imidazole.
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