Category: Protein purification

Trace metal ions can significantly interfere with downstream protein analysis by promoting aggregation or inhibiting enzymes. Understanding how to remove metal from protein is a critical step in achieving high-purity and functional results.

An ideal 260/280 ratio for common purified proteins, such as Bovine Serum Albumin (BSA), is approximately 0.6. Understanding what is a good 260-280 ratio for protein is crucial in molecular biology and biochemistry for assessing the purity of a protein sample via spectrophotometry. Deviations from this optimal range can signify contamination, which is a common challenge during purification experiments.

Hydrophobic interaction chromatography (HIC) is a powerful protein purification technique known for its ability to separate molecules under mild, non-denaturing conditions, which preserves biological activity. Learning how HIC works is crucial for researchers and biochemists needing high-resolution separation of sensitive biomolecules.

In biopharmaceutical manufacturing, Host Cell Proteins (HCPs) are a critical process-related impurity, with regulatory agencies often requiring levels below 100 parts per million (ppm) in the final drug product. Controlling these impurities is vital, as they can impact product stability, safety, and efficacy. This guide addresses effective strategies on how to reduce host cell proteins throughout the production process.