Chromosomal rearrangements of BCL6 are commonly associated with diffuse large-cell lymphomas. We set out to determine the DNA-binding site of a glutathione-S-tranderase fusion protein containing the 6CL6 zinc finger region by employing cyclic amplification and selection of targets (CASTing). From ol
Detection and Purification of Sequence-Specific DNA Binding Protein
โ Scribed by Kshitish C. Majumdar; Sreeram Shetty; Renu Wadhwa; Seema Bhaskar; Mala Ganesan; Lalji Singh
- Publisher
- Elsevier Science
- Year
- 1996
- Tongue
- English
- Weight
- 254 KB
- Volume
- 241
- Category
- Article
- ISSN
- 0003-2697
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
Double-stranded DNA can be viewed as a multifunctional, modular receptor that can be read sequenceselectively in a digital way (base pair per base pair) by a complementary, similarly modular ligand. This principle has been exploited in several approaches to design sequence-specific DNA-binding ligan
We describe a rapid and sensitive method to isolate sets of high-affinity binding sites for sequence-specific DNA binding proteins. The DNA binding domain of the protein is expressed in Escherichia coli as a fusion with glutathione S-transferase (GST). Binding reactions are set up with total soluble
An affinity matrix was constructed by synthesis of a DNA oligonucleotide on a Teflon fiber support followed by deblocking and hybridization of the complementary strand. It was used to purify a sequence-specific binding protein at least 100-fold to near homogeneity. This matrix is easily fabricated o