ATP Separopore® 4B-CL

Adenosine 5'-triphosphate (ATP)-Separopore® 4B-CL is used in the purification of ATP binding proteins. Any protein with an accessible ATP-binding domain will bind to ATP- Separopore® 4B-CL, regardless of activation state. The activated proteins will bind to ATP-Separopore® 4B-CL with higher affinity than the corresponding inactivated protein. This is important when purifying proteins from crude fractions where protein concentration is low, as this prevents non-specific binding. Better recovery and yields may be obtained when the ATP-Separopore® 4B-CL purification is followed by ion exchange chromatography.
The production method involves alkylation of the nucleotide, ATP followed by alkaline rearrangement to yield the corresponding N6-carboxymethyl derivative with subsequent condensation using 1,6-diaminohexane to give N6-[(6-aminohexyl)carbamoylmethyl)].
Note: Separopore® is a cost-effective equivalent to Sepharose® in all of its physical properties and binding characteristics.