Production of 35S-Labeled Proteins in E. coli and Their Use as Molecular Probes
The ability to obtain essentially unrestricted quantities of a cloned protein via expression in a bacterial, fungal, or eukaryotic cell expression system facilitates the structural and functional characterization of that protein. The rapidly increasing availability of diverse expression vectors and complementary cellular systems will eventually allow for the heterologous expression of any protein (1 -3 ). Heterologous protein expression with concomitant radiolabeling provides an attractive means to produce a readily detectable, biochemically active form of the protein without the potential chemical modifications that may arise when a radioactive or other detectable marker is covalently linked to it.
- The Use of Maternal Plasma for Prenatal RhD Blood Group Genotyping
- SI Mapping Using Single-Stranded DNA Probes
- Systemic Delivery of Antisense Oligomer in Animal Models and Its Implications for Treating DMD
- An Assay for In Vitro Recombination Between Duplex DNA Molecules
- Evolutionary Molecular Engineering by Random Elongation Mutagenesis
- Immunostimulatory CpG Motifs and DNA Vaccines
- Next-Generation Sequencing of the Human Olfactory Receptors
- HandGun-Mediated Inoculation of Plants with Viral Pathogens for Mechanistic Studies
- Solid-Phase Minisequencing as a Tool to Detect DNA Polymorphism
- Isolation of Kinetoplast DNA