Refolding Record:
Protein | |
---|---|
Protein Name | General odorant-binding protein 2 |
Abbreviated Name | GOBP2 |
SCOP Family | Unknown |
Structure Notes | |
Organism | Manduca sexta (Tobacco hawkmoth) (Tobacco hornworm |
UniProt Accession | P31419 |
SCOP Unique ID | n/a |
Structure Solved | |
Class | Unknown |
Molecularity | Dimer |
Construct | |
---|---|
Full Length | y |
Domain | n/a |
Chimera | n/a |
Variants | n/a |
Chain Length | 141 |
Molecular Weight | 16285.7 |
Pi | 5.21 |
Molecular Weight | 16285.7 |
Disulphides | 3 |
Full Sequence |
TAEVMSHVTAHFGKALEECREESGLPVEVMDEFKHFWREDFEVVHRELGCAIICMSNKFELLQDDTRIHHVKMHDYIKSFPNGQVLSEKMVQLIHNCEKQYDDIADDCDRVVKVAACFKKDAKKEGIAPEVAMIEAVIEKY
|
Notes | n/a |
Expression | |
---|---|
Report | Feng L, Prestwich GD. (1997) Insect Biochem Mol Biol., 27, 405-12 |
Project Aim | Purification & characterization |
Fusion | None |
Protein Expression and Production | Protein recombinantly expressed as and refolded from inclusion bodies. |
Expression Host | Escherichia coli |
Expression Strain | XLBlue |
Expression Temp | 37.0 |
Expression Time | 5-6 h |
Expression Vector | n/a |
Expression Protocol | For large-scale protein production, 1 1 of LB-ampicillin was inoculated with a 5 ml overnight culture and induced by 1 mm IPTG when OD6oo was approximately 0.4~).6. After 5-6 h, cells were isolated by centrifugation |
Method of Induction | IPTG |
Cell Density at Induction | OD 0.4-0.6 = 600 |
Cell Disruption Method | Sonication/French Press |
Lytic Agent | None |
Pre-Refolding Purification | None |
Solubility | partial |
Refolding | |
---|---|
Refolding Method | Dilution |
Wash Buffer | 0.2% Triton X-100 in 50 mm Tris buffer (pH 6.8) |
Solubilization Buffer | 5 ml of 6 N guanidinium hydrochloride |
Refolding Buffer | 5 mM cysteine in 100 mM Tris-HCI, pH 8.0 |
Pre-Refolding Purification | None |
Tag Cleaved | no tag |
Refolding pH | 8.0 |
Refolding Temperature | 25.0 |
Protein Concentration | n/a |
Refolding Time | n/a |
Redox Agent | Cysteine |
Redox Agent Concentration | 5 mM |
Refolding Protocol | Protein refolding Insoluble protein from a 1 1 culture was washed with 0.2% Triton X-100 in 50 mm Tris buffer (pH 6.8) and then dissolved in 5 ml of 6 N guanidinium hydrochloride. A redox protocol (De Bernardez-Clark and Georgiou, 1991) as modified for refolding PBPs (Prestwich, 1993a) was employed. |
Refolding Assay | photoaffinity labeling |
Refolding Chaperones | None |
Refolding Additives | None |
Additives Concentration | n/a |
Refolding Yield | n/a |
Purity | n/a |
Notes | n/a |