Protein Capture Science
 | |
| Biotechnology | |
| ISIN | 🆔 |
| Founded 📆 | 2018 |
| Founders 👔 | Dr. Izabela Gierach and Dr. David W. Wood |
| Headquarters 🏙️ | 1275 Kinnear Road, Columbus, OH 43212 |
Area served 🗺️ | |
| Products 📟 | iCapTag™ |
| Members | |
Number of employees | |
| 🌐 Website | https://www.proteincapturescience.com/ |
| 📇 Address | |
| 📞 telephone | |
Protein Capture Science is a biotech company that has developed and commercialized a self-removing affinity tag for the purification of recombinant proteins for research and therapeutic applications. The technologies are based on a split intein, where one segment of the intein acts as an affinity tag in fusion to the target protein, while the other segment is covalently immobilized onto a conventional chromatography bead. Capture of the iCapTag intein tag by the resin-bound segment produces a pH-sensitive self-cleaving module, allowing affinity purification of the target protein followed by pH-induced self-cleaving of the tag. The result is a highly effective affinity platform with applications in high-throughput purification of proteins for research, but with the additional advantage of providing tagless native proteins that can be safely used in clinical applications.
The company
Protein Capture Science was co-founded in 2018 by Dr. David W. Wood and Dr. Izabela Gierach, and is currently located in Columbus, Ohio as a privately held LLC. The protein purification platform was developed by Dr. Wood and his team at the Ohio State University, and is currently covered by five issued patents. The first commercial iCapTag™ product was launched in August of 2021, and includes prepacked columns and bulk iCapTag resin for evaluation and small-scale production of research proteins.[1]
Applications and Tools
Protein Capture Science product
The iCapTag™ resin consists of a modified N-terminal segment of the Nostoc punctiforme (Npu) DnaE intein, covalently bound to a crosslinked agarose chromatography bead. This resin is designed to capture recombinant proteins tagged with the iCapTag™, which is a modified version of the 36-amino acid C-terminal Npu intein segment fused to the N-terminus of the target protein. When the tagged protein is passed over the iCapTag™ resin, the intein segments strongly associate and assemble into an active intein complex, which has been modified for pH-controlled self-cleavage of the iCapTag™ from the tagged target protein. In practice, binding of the tagged target protein at pH 8.5 allows purification of the target protein via a conventional affinity purification approach. Once purified, the iCapTag™ is induced to release the highly purified target protein from the bound tag via a change in buffer pH from 8.5 to 6.2. Cleavage to 90% released target typically takes place over 5 hours at room temperature, where prescribed modifications of the first two amino acids of the target can be used to optimize cleavage. A major advantage of this technology is that it provides a simple and general method for purifying proteins by virtue of the affinity tag, but with the ability to provide a tagless and scarless target protein without the use of protease enzymes or complex buffer components. Once the cleaved target protein is eluted and recovered, the iCapTag™ resin can be regenerated for reuse via a low pH wash. The iCapTag™ resin has been used successfully for simple and complex glycoproteins expressed in E.coli, CHO, and HEK cell lines.[2][3]
Cloning target proteins & more
To use the iCapTag™ technology, the researcher must append the iCapTag™ to the N-terminus of the target protein. In cases where a secretion signal peptide is required for proper expression, the signal is appended to the N-terminus of the iCapTag™.
References
- ↑ "Protein Capture Science". www.proteincapturescience.com. Retrieved 2022-06-28.
- ↑ Cooper, Merideth A.; Taris, Joseph E.; Shi, Changhua; Wood, David W. (2018). "A Convenient Split‐Intein Tag Method for the Purification of Tagless Target Proteins". Current Protocols in Protein Science. 91 (1): 5.29.1–5.29.23. doi:10.1002/cpps.46. ISSN 1934-3655. PMID 29516483. Unknown parameter
|s2cid=ignored (help) - ↑ Prabhala, Sai Vivek; Gierach, Izabela; Wood, David W. (2022). "The Evolution of Intein-Based Affinity Methods as Reflected in 30 years of Patent History". Frontiers in Molecular Biosciences. 9: 857566. doi:10.3389/fmolb.2022.857566 (inactive 31 July 2022). ISSN 2296-889X. PMC 9033041 Check
|pmc=value (help). PMID 35463948 Check|pmid=value (help).
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