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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).
• Ligand: ATP
• Matrix: Separapore 4B-CL (crosslinked agarose beads, 4 %)
• Particle size range: 52 - 165 m
• Matrix activation: Cyanogen bromide
• Ligand density: 2 - 5 ATP mol / ml drained gel
• Attachment: N6 of the purine ring
• Spacer: 11 atoms
• Supplied as lyophilized powder, 1g powder yields 8 - 10 ml of gel
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