The ability to isolate and study a purified protein lies at the heart of modern biochemistry. Researchers in many fields require highly purified, active proteins for studies involving signaling pathways, enzymology, receptor binding, DNA binding, post-transcriptional modifications, and much more. Thus, choosing a method of purification is an important aspect in maintaining protein structure and function.
　Recombinant tagged protein purification methods and kits are now widely recognized. The V5 epitope tag, GKPIPNPLLGLDST, is derived from the P/V proteins of paramyxovirus SV5. This V5 tag is also commonly used in such as mammalian and insect cell expression vectors.
MBL’s V5 tagged Protein PURIFICATION KIT is designed for the isolation of V5 tagged protein from cell culture supernatants containing serum and cell lysate under neutral pH condition. Severe conditions such as acidic or alkaline elution denature protein structure. However, a neutral pH elution can preserve protein activity and native conformation. MBL has developed the Anti-V5 tag Beads to purify V5 tagged proteins quickly and efficiently. As the Beads can be used at neutral pH, the purified proteins can maintain the activity and conformation. The elution of V5 tagged proteins from the Beads is achieved by the addition of the V5 peptide. As the V5 peptide competes with V5 tagged proteins on the Beads, the purified proteins do not lose the protein activity. The simple procedures of this kit have been optimized by using a Spin Column resulting in high efficiency.