Refolding Record:
Protein | |
---|---|
Protein Name | Tax |
Abbreviated Name | Tax |
SCOP Family | Unknown |
Structure Notes | |
Organism | Bovine Leukemia Virus |
UniProt Accession | Q5MNW3 |
SCOP Unique ID | n/a |
Structure Solved | |
Class | Unknown |
Molecularity | Monomer |
Construct | |
---|---|
Full Length | y |
Domain | n/a |
Chimera | n/a |
Variants | n/a |
Chain Length | 315 |
Molecular Weight | 35043.3 |
Pi | 6.13 |
Molecular Weight | 35043.3 |
Disulphides | 0 |
Full Sequence |
ASVVGWGPHSLHACPALVLSNDDTIDAWCPLCGPHERLQFERIDTTLTCETHHITWTADG
RPFGLNGALFPRLHVSETRPQGPRRLWINCPLPAVRAQPGPVSLPPLEQSPFQPYQCQLP
SASSDGSPIIGHGLLPWNNLVTHPVLGKVLILNQMANFSLLPSFDTLIVDPLRLSVFAPD
TRGTIRYLSTLLTLCPATCILPLDEPFSPNVPICRFPRDSNEPPLSEFELPLIQTPGLSW
SVPAIDLFLTGPPSPNDRLHVWSSPQALQRFLHDPTLTWSELVASRKLKLDSPLKLQLLE
NEWLSPALFHHHHHH
|
Notes | n/a |
Expression | |
---|---|
Report | Boros, I. M., Tie, F., Giam, C. Z. (1995) Virology, 214, 207-214 |
Project Aim | Protein-Protein Interaction Identification |
Fusion | C-terminal hexahistidine tag |
Protein Expression and Production | Protein recombinantly expressed as and refolded from inclusion bodies. |
Expression Host | Escherichia coli |
Expression Strain | BL21(DE3) |
Expression Temp | 37.0 |
Expression Time | 2-3h |
Expression Vector | pET-BLV-His6 |
Expression Protocol | Cells grown in LB medium containing 100microg/ml ampicillin. After induction, cells were harvested via centrifugation(10,000g, 10min, 4degC). The pellet was resuspended in 20ml of Buffer A (50mM Tris, pH 8.0, 1 mM EDTA, 100mM NaCl) containing 0.5mM PMSF. Cells were then lyzed and inclusion bodies collected by centrifugation(17,000g, 20min, 4degC). |
Method of Induction | IPTG |
Cell Density at Induction | OD 600 = 0.6-0.8 |
Cell Disruption Method | Sonication |
Lytic Agent | None |
Pre-Refolding Purification | Metal affinity chromatography |
Solubility | insoluble |
Refolding | |
---|---|
Refolding Method | Dialysis |
Wash Buffer | PBS, pH 7.4, 1% Triton X-100, 1M GuHCl |
Solubilization Buffer | PBS, pH 7.4, 6M GuHCl |
Refolding Buffer | 20mM HEPES, pH 7.9, 400mM KCl, 0.2 mM EDTA, 0.5mM PMSF, 0.5mM DTT and 20% glycerol |
Pre-Refolding Purification | Metal affinity chromatography |
Tag Cleaved | no |
Refolding pH | 7.9 |
Refolding Temperature | 25.0 |
Protein Concentration | n/a |
Refolding Time | n/a |
Redox Agent | None |
Redox Agent Concentration | n/a |
Refolding Protocol | Inclusion bodies were washed 2x 20ml with washing buffer prior to solubilization and centrifugation. The solubilized supernatant was then mixed with 5ml Ni2+ chelating Sepharose Fast flow which had been preequilibrated with solubilization buffer. The column was washed with 20ml solubilization buffer containing 0.02 M imidazole and 15 ml of washing buffer. The protein was then eluted in PBS containing 0.3 M NaCl, 5% glycerol, and 0.25 M imidazole. Fractions containing protein were then dialyzed against refolding buffer. |
Refolding Assay | Ligand Binding,Gel filtration chromatography |
Refolding Chaperones | None |
Refolding Additives | None |
Additives Concentration | n/a |
Refolding Yield | n/a |
Purity | n/a |
Notes | n/a |