Zobrazeno 1 - 10
of 16
pro vyhledávání: '"Kimberly Trabbic-Carlson"'
Autor:
Mohammed F. Shamji, Trine Christensen, Sue Dagher, Kimberly Trabbic-Carlson, Miriam Amiram, Ashutosh Chilkoti, Lori A. Setton
Publikováno v:
Protein Science. 18:1377-1387
We have previously developed a method to purify recombinant proteins, termed inverse transition cycling (ITC) that eliminates the need for column chromatography. ITC exploits the inverse solubility phase transition of an elastin-like polypeptide (ELP
Publikováno v:
Biomacromolecules. 8:1417-1424
This paper reports an improvement in the purification of thioredoxin (Trx) expressed from E. coli by inverse transition cycling (ITC) using cationic elastin-like polypeptides (ELPs). Two ELP libraries having 2% and 5% lysine residues and molecular we
Autor:
Fernando Albertorio, Paul S. Cremer, Kimberly Trabbic-Carlson, Yanjie Zhang, and Ashutosh Chilkoti
Publikováno v:
Biomacromolecules. 7:2192-2199
The kinetics of aqueous two-phase system (ATPS) formation for elastin-like polypeptides (ELP) with defined chemical composition and chain length was investigated by dark field microscopy in an on-chip format with a linear temperature gradient. Scatte
Publikováno v:
Biotechnology Progress. 22:638-646
Elastin-like polypeptides (ELPs) are recombinant peptide-based biopolymers that contain repetitive sequences enriched in glycine, valine, proline, and alanine. Because of the unusually large fraction of these amino acids in ELPs as compared to other
Autor:
Shin R. Ong, Dana L. Nettles, Ashutosh Chilkoti, Kimberly Trabbic-Carlson, Dong W. Lim, Lori A. Setton
Publikováno v:
Biomaterials. 27:1930-1935
Elastin-like polypeptides (ELPs) are a class of biocompatible, non-immunogenic and crosslinkable biomaterials that offer promise for use as an injectable scaffold for cartilage repair. In this study, an oligohistidine (His(6)) epitope tag was incorpo
Autor:
Kimberly Trabbic-Carlson, Ashutosh Chilkoti, Dan E. Meyer, Nidhi Nath, Thomas H. LaBean, Ronald T. Piervincenzi, L. Liu
Publikováno v:
Protein Engineering Design and Selection. 17:57-66
The limited throughput, scalability and high cost of protein purification by chromatography provide motivation for the development of non-chromatographic protein purification technologies that are cheaper and easier to implement in a high-throughput
Publikováno v:
Analytical Biochemistry. 360:166-168
A crucial and challenging problem in proteomics is purification, identification, and characterization of proteins, some of which are expressed at very low levels. The preferred method for purification of low abundance proteins exploits multiple affin
Publikováno v:
Biointerphases. 3(3)
The conformational changes in elastinlike polypeptides (ELPs) grafted to a solid/solution interface via different architectures were studied using surface plasmon resonance spectroscopy and surface plasmon field-enhanced fluorescence spectroscopy (SP
Autor:
Trine, Christensen, Miriam, Amiram, Sue, Dagher, Kimberly, Trabbic-Carlson, Mohammed F, Shamji, Lori A, Setton, Ashutosh, Chilkoti
Publikováno v:
Protein science : a publication of the Protein Society. 18(7)
We have previously developed a method to purify recombinant proteins, termed inverse transition cycling (ITC) that eliminates the need for column chromatography. ITC exploits the inverse solubility phase transition of an elastin-like polypeptide (ELP
Publikováno v:
Biotechnology and bioengineering. 95(3)
This article describes a simple and potentially scalable microfiltration method for purification of recombinant proteins. This method is based on the fact that when an elastin-like polypeptide (ELP) is fused to a target protein, the inverse phase tra