Refolding Record:
Protein | |
---|---|
Protein Name | Fel d 1 |
Abbreviated Name | Fel d 1 |
SCOP Family | Uteroglobin like |
Structure Notes | |
Organism | Felis domesticus (cat) |
UniProt Accession | P30438 |
SCOP Unique ID | n/a |
Structure Solved | |
Class | Alpha |
Molecularity | Heterodimer |
Construct | |
---|---|
Full Length | n |
Domain | n/a |
Chimera | Chain 1 and Chain 2 joined by linker |
Variants | n/a |
Chain Length | 168 |
Molecular Weight | 18795.6 |
Pi | 5.08418 |
Molecular Weight | 18795.6 |
Disulphides | 3 |
Full Sequence |
VKM AETCPIFYDV FFAVANGNEL LLDLSLTKVN ATEPERTAMK KIQDCYVENG LISRVLDGLV MTTISSSKDC MGEAVQNTVE
DLKLNTLGR EICPAVKR DVDLFLTGTP DEYVEQVAQY KALPVVLENA RILKNCVDAK MTEEDKENAL SVLDKIYTSP LC HHHHHH
|
Notes | UniProt ID of Chain 2: FEL1B_FELCA |
Expression | |
---|---|
Report | Kaiser L, Gronlund H, Sandalover T, Ljunggren H, Schneider G, van Hag-Hamsten M, Achour A (2003) Acta Crystallographica Section D, 559, 1103-1105 |
Project Aim | Crystallography |
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)pLysS |
Expression Temp | 37.0 |
Expression Time | not stated |
Expression Vector | pET20b |
Expression Protocol | Protein expression was induced with IPTG (no further details provided). |
Method of Induction | IPTG |
Cell Density at Induction | OD = |
Cell Disruption Method | None |
Lytic Agent | None |
Pre-Refolding Purification | None |
Solubility | insoluble |
Refolding | |
---|---|
Refolding Method | Column refolding: Nickel-chelating chromatography |
Wash Buffer | 20mM TrisHCl, 6M Urea, 0.5M NaCl, 20mM imidazole pH 8.0 |
Solubilization Buffer | 20mM TrisHCl, 6M GdnHCl, 0.5M NaCl, 5mM imidazole pH 8.0 |
Refolding Buffer | 20mM TrisHCl, 0.5M NaCl, 20mM imidazole pH 8.0 |
Pre-Refolding Purification | None |
Tag Cleaved | no |
Refolding pH | 8.0 |
Refolding Temperature | 25.0 |
Protein Concentration | |
Refolding Time | |
Redox Agent | None |
Redox Agent Concentration | n/a,n/a,n/a |
Refolding Protocol | The isolated inclusion bodies were dissolved in solubilization buffer and bound to a Hi-Trap Ni-NTA column. The column buffer was changed to wash buffer, and then a linear 12 column volume gradient was used with wash buffer and refolding buffer. The refolded protein was further purified by size exclusion and MonoQ ion-exchange chromatography. |
Refolding Assay | Gel filtration chromatography |
Refolding Chaperones | None |
Refolding Additives | None |
Additives Concentration | |
Refolding Yield | 10mg/L |
Purity | |
Notes |