Refolding Record:
Protein | |
---|---|
Protein Name | Apolipoprotein C-II |
Abbreviated Name | Apo-CII |
SCOP Family | Fragments of apolipoproteins |
Structure Notes | |
Organism | Human |
UniProt Accession | O95996 |
SCOP Unique ID | n/a |
Structure Solved | |
Class | Membrane and cell surface proteins and peptides |
Molecularity | Monomer |
Construct | |
---|---|
Full Length | y |
Domain | n/a |
Chimera | n/a |
Variants | n/a |
Chain Length | 102 |
Molecular Weight | 11283.9 |
Pi | 4.72187 |
Molecular Weight | 11283.9 |
Disulphides | 0 |
Full Sequence |
MGTRLLPALFLVLLVLGFEVQGTQQPQQDEMPSPTFLTQVKESLSSYWESAKTAAQNLYE
KTYLPAVDEKLRDLYSKSTAAMSTYTGIFTDQVLSVLKGEE
|
Notes | n/a |
Expression | |
---|---|
Report | Hatters DM, MacPhee CE, Lawrence LJ, Sawyer WH, Howlett GJ. (2000) Biochemistry, 39, 8276-8283 |
Project Aim | Folding |
Fusion | None |
Protein Expression and Production | Protein recombinantly expressed as and refolded from inclusion bodies. |
Expression Host | Escherichia coli |
Expression Strain | BL21 |
Expression Temp | 37.0 |
Expression Time | unknown |
Expression Vector | pET11a |
Expression Protocol | unknown |
Method of Induction | Not Stated |
Cell Density at Induction | OD = |
Cell Disruption Method | Sonication |
Lytic Agent | None |
Pre-Refolding Purification | Ion-exchange + size exclusion chromatography |
Solubility | insoluble |
Refolding | |
---|---|
Refolding Method | Dilution/Dialysis combination |
Wash Buffer | 6 mM urea, 10 mM TrisHCl, pH 8.0 |
Solubilization Buffer | 5 mM GdnHCl, 100 mM arginine, pH 12.0 |
Refolding Buffer | 100mM urea and 10mM sodium phosphate |
Pre-Refolding Purification | Ion-exchange + size exclusion chromatography |
Tag Cleaved | no tag |
Refolding pH | 7.4 |
Refolding Temperature | 4.0 |
Protein Concentration | 50 micrograms/mL |
Refolding Time | |
Redox Agent | None |
Redox Agent Concentration | n/a |
Refolding Protocol | As misfolding induces aggregation of recombinant proteins , apoC-II was refolded at a relatively low concentration and add 100 mM urea to the buffers after the protein was refolded to inhibit intermolecular hydrophobic interactions. A stock of apoC-II at 9.5 mg/mL in 5 M guanidine HCl was diluted directly into 100 mL of 100 mM sodium phosphate, pH 7.4, to a final protein concentration of 50 microg/mL. The protein was incubated at room temperature for 3 h and then dialyzed into 100 mM urea and 10 mM sodium phosphate, pH 7.4, at 4 C with two buffer changes. The protein solution was applied to a HR5-10 column (Pharmacia-Biotech) packed with Source 15Q anion-exchange resin (Pharmacia-Biotech) preequilibrated in 100 mM urea, 10 mM sodium phosphate, pH 7.4. The protein was eluted with the above buffer and 500 mM NaCl at a flow rate of 1 mL/min. The eluted protein was desalted by application to a 1 ?9 cm column of Sephadex G-25 resin preequilibrated with 100 mM sodium phosphate, pH 7.4, and eluted at a flow rate of 1 mL/min. ApoC-II prepared by this method and used directly is referred to as freshly prepared. |
Refolding Assay | Near-UV Circular Dichroism |
Refolding Chaperones | None |
Refolding Additives | None |
Additives Concentration | NULL |
Refolding Yield | |
Purity | |
Notes |