Expression and Purification of Recombinant Proteins Using the Baculovirus System
Open Access
- 1 January 2004
- journal article
- unit
- Published by Wiley in Current Protocols in Molecular Biology
- Vol. 65 (1) , 16.11.1-16.11.14
- https://doi.org/10.1002/0471142727.mb1611s65
Abstract
This unit describes how to analyze protein expression in cells infected with recombinant baculovirus on a small scale for optimizing protein production , how to maximize and scale up recombinant protein production, and how to purify recombinant proteins.Keywords
This publication has 5 references indexed in Scilit:
- Analysis of the NuRD subunits reveals a histone deacetylase core complex and a connection with DNA methylationGenes & Development, 1999
- Reconstitution of a Core Chromatin Remodeling Complex from SWI/SNF SubunitsMolecular Cell, 1999
- Affinity chromatography of platelets on immobilised thrombin: Retention of catalytic activity by platelet-bound thrombinThrombosis Research, 1992
- Ligation-independent cloning of glutathione fusion genes for expression in Escherichia coliGene, 1992
- Eukaryotic proteins expressed in Escherichia coli: An improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferaseAnalytical Biochemistry, 1991