His tagged Protein PURIFICATION GEL

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. The hexa Histidine-tag (6xHis tag) is one of the most common tags used to facilitate the purification of recombinant proteins. Metal chelate affinity chromatography is widely used for purification of His tagged proteins. Unfortunately, some serum components are absorbed by the metal chelate affinity columns, making these columns impractical for the purification of proteins secreted into the culture supernatant. Indeed many proteins have intrinsic histidine residues or other untagged host proteins that can bind to the metal chelate affinity columns and elute with His tagged protein. These untagged contaminants may be removed using an additional purification or laborious optimizing the imidazole concentration. MBLI?s His tagged Protein PURIFICATION GEL is designed for the isolation of His 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. Therefore, MBLI has developed the Anti-His tag Gel to purify His tagged proteins quickly and efficiently at neutral pH to maintain the activity and conformation of purified proteins. The elution of His tagged proteins from the Gel is achieved by the addition of the 6xHis tag peptide. As the 6xHis tag peptide competes with His tagged proteins on the Gel, the purified proteins do not lose the protein activity.

Human: 57016 Mouse: 15109

1 year

His