Kinetic Solubility Testing Service

Why Do Kinetic Solubility Testing

Heterologous expression of recombinant proteins often leads to decreased protein solubility and aggregation, and in the same way in the field of biopharmaceuticals, antibodies also aggregate after entering the body, causing reduced activity and additional immune responses.

Protein solubility and stability are affected by a variety of factors, such as pH, temperature, solvents, ionic strength, metal ion cofactors, and surfactants. In addition to this, solubility can be predicted by solvent-accessible surface area and hydrogen bond estimation algorithms. The isoelectric point (pI) of a protein is the pH of a protein with a net charge of 0 when the protein solubility is at its lowest, and the protein solubility can be improved by designing to optimize the protein pI value. Protein pI is the average value of the amino acid functional group pKa, and a lower pKa indicates that the protein is more acidic. In the case of proteins, their net charge is affected by pH and is determined by the content of all ionizable amino acids and pKa.

Fig.1 Hydrophilic amino acids. (Qing, et al., 2022) Fig.1 Schematic diagram of hydrogen bonds formed by hydrophilic amino acids with water at neutral pH.1

Our Services

Creative Biolabs offers antibody protein solubility testing to assess the importance of an antibody or antibody fragment in biotechnology and drug development.

General solubility test

PEG precipitation solubility test

Ultra-high-throughput microfluidic platform

Kinetic Solubility Testing Process

Fig.2 Kinetic solubility testing process.

Why Choose Creative Biolabs

Based on a complete technology platform and experienced scientists, Creative Biolabs has established a complete testing service process in the field of in vitro ADME detection of antibodies and proteins, which can provide you with a one-stop solution to meet your analysis needs.

Fig.3 Our advantages.

If you have any kinetic solubility testing needs, please contact us!

Reference

  1. Qing, Rui et al. "Protein design: from the aspect of water solubility and stability." Chemical reviews. 122,18 (2022): 14085-14179.

For Research Use Only | Not For Clinical Use

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