HaloLink™ Resin: High Capacity, Specificity and Scalable Throughput for Protein Analysis Export

@article{citeulike:3470764, abstract = {HaloLink™ Resin provides a new method for specific, covalent and oriented immobilization of proteins onto surfaces. The strategy is based on the HaloTag™ Protein, which is derived from a catalytically inactive hydrolase engineered to form a covalent bond with a specific ligand. Here we demonstrate the high binding capacity and minimal nonspecific binding of the HaloLink™ Resin. We also show that the covalent HaloTag™ bond provides stability during dilution and stringent washing, minimizing the loss of the HaloTag™ fusion proteins from the surface. By analyzing protein:protein interactions and enzyme activity for several fusion proteins, we also demonstrate that fusion proteins bound to the HaloLink™ Resin maintain functionality. HaloLink™ Resin is not a purification resin; however, in conjunction with protease cleavage, it can be used to isolate a protein of interest.}, author = {Urh, Marjeta and Simpson, Dan and Sankbeil, Jacqui and Hartzell, Danette and Karassina, Natasha and Betz, Natalie and Nassif, Nadine and English, Jami and Zhu, Ji and Meisenheimer, Poncho and Klaubert, Dieter and Bulleit, Bob and Wood, Keith and 1promega}, citeulike-article-id = {3470764}, citeulike-linkout-0 = {http://www.promega.com/pnotes/92/13408_24/13408_24.html}, journal = {Promega Notes}, keywords = {protein\_analysis}, pages = {24--29}, posted-at = {2008-10-31 18:44:43}, priority = {0}, title = {HaloLink™ Resin: High Capacity, Specificity and Scalable Throughput for Protein Analysis}, url = {http://www.promega.com/pnotes/92/13408_24/13408_24.html}, volume = {92}, year = {2006} }

TY - JOUR ID - citeulike:3470764 L3 - citeulike-article-id:3470764 N2 - HaloLink™ Resin provides a new method for specific, covalent and oriented immobilization of proteins onto surfaces. The strategy is based on the HaloTag™ Protein, which is derived from a catalytically inactive hydrolase engineered to form a covalent bond with a specific ligand. Here we demonstrate the high binding capacity and minimal nonspecific binding of the HaloLink™ Resin. We also show that the covalent HaloTag™ bond provides stability during dilution and stringent washing, minimizing the loss of the HaloTag™ fusion proteins from the surface. By analyzing protein:protein interactions and enzyme activity for several fusion proteins, we also demonstrate that fusion proteins bound to the HaloLink™ Resin maintain functionality. HaloLink™ Resin is not a purification resin; however, in conjunction with protease cleavage, it can be used to isolate a protein of interest. JF - Promega Notes EP - 29 TI - HaloLink™ Resin: High Capacity, Specificity and Scalable Throughput for Protein Analysis VL - 92 SP - 24 KW - protein_analysis AU - Urh, Marjeta AU - Simpson, Dan AU - Sankbeil, Jacqui AU - Hartzell, Danette AU - Karassina, Natasha AU - Betz, Natalie AU - Nassif, Nadine AU - English, Jami AU - Zhu, Ji AU - Meisenheimer, Poncho AU - Klaubert, Dieter AU - Bulleit, Bob AU - Wood, Keith AU - 1promega PY - 2006/// UR - http://www.promega.com/pnotes/92/13408_24/13408_24.html ER -