DDDDK-tagged Protein PURIFICATION GEL with Elution Peptide

Isolation of DDDDK tagged protein with protein activity and native conformation from cell culture supernatants and cell lysate under neutral pH condition.

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 DDDDK epitope tag (DYKDDDDK) has been widely used as a multi-purpose tag, and anti-DDDDK-tag antibodies are optimally suited for identifying, detecting, purifying, and monitoring the expression levels of recombinant DDDDK-tagged proteins. MBLI?s DDDDK-tagged Protein PURIFICATION GEL with Elution Peptide is designed for the isolation of DDDDK-tagged protein from cell culture supernatants 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. Therefore, MBLI has developed the Anti-DDDDK-tag Gel to purify DDDDK-tagged proteins quickly and efficiently at neutral pH to maintain the activity and conformation of purified proteins. The elution of DDDDK-tagged proteins from the Gel is achieved by the addition of the DDDDK-tag peptide (DYKDDDDK). As the DDDDK-tag peptide competes with DDDDK-tagged proteins on the Gel, the purified proteins do not lose the protein activity.

Anti-DDDK tag beads, elution peptide, spin column sets, wash concentrate

1 year

DDDDK