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. The method of purification is one of the important keys for maintaining protein structure and function. The c-Myc tagged Protein MILD PURIFICATION KIT is designed for the isolation of c-Myc tagged protein from cell lysates and culture supernatant. Severe conditions such as acidic or alkaline elution can denature protein structure while maintaining a neutral pH can preserve protein activity and conformation. MBL has developed the Anti-c-Myc tag Gel to quickly and efficiently purify c-Myc-tagged proteins at neutral pH to maintain protein activity and native conformation. The c-Myc tag peptide competitively elutes the c-Myc tagged protein from Anti-c-Myc tag Beads while minimally interfering with protein function. The affinity of the anti-c-Myc tag antibody is also very important. Very high affinity antibody cannot be dissociated from the c-Myc tagged protein, and low affinity antibody is not sufficient for binding. MBL has optimized the affinity of the anti-c-Myc tag antibody to permit high yields and efficient purification of functional c-Myc-tagged proteins for biochemical studies. This kit is simple and fast, because all procedures of this kit have been optimized by using a Spin Column. In ver.2, MBL improved the purification capacity of the Anti-c-Myc tag Beads by using the new monoclonal antibody (Clone 1G4). It is easily possible for scale-up by using a c-Myc tagged Protein MILD PURIFICATION GEL (code 3306, 3307).