High-yield purification of functional, full-length steroid receptor coactivator 1 expressed in insect cells

BioTechniques

Volumn 32, Issue 2, 2002, Pages 260-263

  Thackray, Varykina G ^a   Nordeen, Steven K ^a  

^a UNIVERSITY OF COLORADO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; RECOMBINANT PROTEIN; STEROID RECEPTOR COACTIVATOR 1;

ANIMAL CELL; ARTICLE; BACULOVIRUS; CONTROLLED STUDY; GENETIC TRANSCRIPTION; LIGAND BINDING; NONHUMAN; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN SYNTHESIS;

ANIMALIA; INSECTA; UNIDENTIFIED BACULOVIRUS;

EID: 0036161294     PISSN: 07366205     EISSN: None     Source Type: Journal    
DOI: 10.2144/02322bm05     Document Type: Article

References (9)

1. Recombinant baculoviruses as expression vectors for insect and mammalian cells
2. p300 and estrogen receptor cooperatively activate transcription via differential enhancement of initiation and reinitiation
3. Ligand- and cofactor-regulated transcription by nuclear hormone receptors with chromatin templates
4. Steroid receptor coactivator-1 (SRC-1) enhances ligand-dependent and receptor-dependent cell-free transcription of chromatin
5. Specific inhibitors prevent proteolytic degradation of recombinant proteins expressed in High Five™ cells
6. Distinct steady-state nuclear receptor coregulator complexes exist in vivo
7. Baculoviruses: High-level expression in insect cells
8. The steroid receptor coactivator-1 contains multiple receptor interacting and activation domains that cooperatively enhance the activation function 1 (AF1) and AF2 domains of steroid receptors
9. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily