c-Myc tagged Protein MILD 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.

The method of purification is one of the important keys for maintaining protein structure and function. The c-Myc tagged Protein MILD PURIFICATION GEL 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 Gel 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. Anti-c-Myc tag monoclonal antibody (clone 1G4) used by this gel shows the best affinity to refine the c-Myc tag fusion protein under a mild condition.