:: Posted by American Biotechnologist on 02-25-2010
Want to learn how to purify and refold biologically active proteins in under 90 minutes? If so, read on…
The expression and purification of recombinant proteins using e. coli as a bacterial host is quite common. One of the challenges facing recombinant protein scientists is the formation of insoluble protein aggregates known as inclusion bodies. While it is often undesirable to have insoluble protein aggregates in your lysate, inclusion bodies can offer the advantage of increased recombinant protein expression levels, easy isolation, low degradation of the expressed protein and high homogeneity of the protein of interest. Nonetheless, recovering the desired proteins from inclusion bodies can often be time consuming and difficult.
In this Bio-Rad tech note you will learn how to purify and refold bioactive proteins expressed in inclusion bodies in a single automated step.
:: Posted by American Biotechnologist on 02-17-2010
With the completion of the human genome project and the subsequent sequencing of the genomes of most model organisms, a wealth of transcriptional data has emerged to broaden our understanding of cellular mechanisms. Technologies including DNA microarrays, real-time PCR, ultra-high throughput DNA sequencing, and intergenic chip-on-chip arrays have allowed researchers to hone in on specific genes implicated in a number of diseases and signaling events. In the post-genomic phase, the focus is shifting toward proteomics studies and the characterization of the proteins encoded by the identified genes. Chromatographic purification is an important tool in proteomic studies and it is the first step of any functional characterization of proteins.
See Sean Taylor’s article for more…