Refolding Record:
Protein | |
---|---|
Protein Name | Outer membrane protein A |
Abbreviated Name | OmpA |
SCOP Family | Outer membrane protein |
Structure Notes | |
Organism | Escherichia coli |
UniProt Accession | P0A911 |
SCOP Unique ID | n/a |
Structure Solved | |
Class | Membrane and cell surface proteins and peptides |
Molecularity | Unknown |
Construct | |
---|---|
Full Length | y |
Domain | n/a |
Chimera | n/a |
Variants | n/a |
Chain Length | 325 |
Molecular Weight | 35172.3 |
Pi | 5.59 |
Molecular Weight | 35172.3 |
Disulphides | 1 |
Full Sequence |
APKDNTWYTGAKLGWSQYHDTGFINNNGPTHENQLGAGAFGGYQVNPYVGFEMGYDWLGRMPYKGSVENGAYKAQGVQLTAKLGYPITDDLDIYTRLGGMVWRADTKSNVYGKNHDTGVSPVFAGGVEYAITPEIATRLEYQWTNNIGDAHTIGTRPDNGMLSLGVSYRFGQGEAAPVVAPAPAPAPEVQTKHFTLKSDVLFNFNKATLKPEGQAALDQLYSQLSNLDPKDGSVVVLGYTDRIGSDAYNQGLSERRAQSVVDYLISKGIPADKISARGMGESNPVTGNTCDNVKQRAALIDCLAPDRRVEIEVKGIKDVVTQPQA
|
Notes | n/a |
Expression | |
---|---|
Report | Dornmair K, Kiefer H, Jähnig F. (1990) Biologycal Chemistry, 265, 18907-18911 |
Project Aim | Protein refolding |
Fusion | None |
Protein Expression and Production | Protein expressed and purified in native conformation prior to denaturation and refolding. |
Expression Host | None |
Expression Strain | None |
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 | not specified |
Solubility |
Refolding | |
---|---|
Refolding Method | Chaperone-assisted refolding |
Wash Buffer | n/a |
Solubilization Buffer | O.O5% SDS, 75 mM Tris/HCl buffer, pH = 7.5. |
Refolding Buffer | Octylglucoside (OG) to a final concentration of 20 mg/ml, |
Pre-Refolding Purification | not specified |
Tag Cleaved | no tag |
Refolding pH | 7.5 |
Refolding Temperature | 25.0 |
Protein Concentration | n/a |
Refolding Time | n/a |
Redox Agent | None |
Redox Agent Concentration | n/a |
Refolding Protocol | OmpA was dissolved at a concentration of 100 ug/ml in O.O5% SDS, 75 mM Tris/HCl buffer, pH = 7.5. This yielded a molar SDS to OmpA ratio of 500. Denaturation was achieved by boiling the sample for 10 min. Thereafter, the sample was put on ice for 2 min. Refolding was induced at room temperature by adding solid OG to a final concentration of 20 mg/ml, corresponding to a molar OG/SDS ratio of 40. |
Refolding Assay | SDS-PAGE,Protease digestion |
Refolding Chaperones | None |
Refolding Additives | Octylglucoside (OG) |
Additives Concentration | 20 mg/ml |
Refolding Yield | n/a |
Purity | n/a |
Notes | n/a |