Refolding Record:
| Construct | |
|---|---|
| Full Length | n |
| Domain | 163 |
| Chimera | n/a |
| Variants | n/a |
| Chain Length | 3 |
| Molecular Weight | 204.2 |
| Pi | 5.24001 |
| Molecular Weight | 204.2 |
| Disulphides | 0 |
| Full Sequence |
S V
|
| Notes | n/a |
| Expression | |
|---|---|
| Report | Unpublished (0) J Virol Methods, 0, 0 |
| Project Aim | Structure-Function |
| Fusion | None |
| Protein Expression and Production | Protein expressed and purified in native conformation prior to denaturation and refolding. |
| Expression Host | |
| Expression Strain | |
| Expression Temp | 0.0 |
| Expression Time | 0 |
| Expression Vector | |
| Expression Protocol | |
| Method of Induction | Not Stated |
| Cell Density at Induction | OD = |
| Cell Disruption Method | None |
| Lytic Agent | None |
| Pre-Refolding Purification | DEAE-Sepharose Fast Flow column |
| Solubility | |
| Refolding | |
|---|---|
| Refolding Method | Dialysis |
| Wash Buffer | Tris-HCl 50mM pH 8.0 |
| Solubilization Buffer | Tris-HCl 50mM pH 8.0 |
| Refolding Buffer | (Guanidine hidrochloride 8-2M); (Ureia 2M, L-Arg 0.5M); (Guanidine hidrochloride 3M, L-Cys 0.5 mM, 1mM EDTA, 20mM CaCl2) |
| Pre-Refolding Purification | DEAE-Sepharose Fast Flow column |
| Tag Cleaved | no |
| Refolding pH | 8.5 |
| Refolding Temperature | 25.0 |
| Protein Concentration | 140 mM |
| Refolding Time | 24 h |
| Redox Agent | None |
| Redox Agent Concentration | n/a |
| Refolding Protocol | n/a |
| Refolding Assay | enzyme activity |
| Refolding Chaperones | None |
| Refolding Additives | None |
| Additives Concentration | n/a |
| Refolding Yield | 10 |
| Purity | n/a |
| Notes | n/a |