| Species : |
Human |
| Source : |
E.coli |
| Tag : |
His&SUMO |
| Protein Length : |
1-142 aa |
| Description : |
Functions as chaperone and catalyzes the formation of disulfide bonds in substrate proteins, such as COX17. Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermbrane space (IMS). Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria. The oxidized form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS. Reduced CHCHD4/MIA40 is then reoxidized by GFER/ERV1 via a disulfide relay syst. |
| Form : |
Tris-based buffer, 50% glycerol |
| Molecular Mass : |
32.0 kDa |
| AA Sequence : |
MSYCRQEGKDRIIFVTKEDHETPSSAELVADDPNDPYEEHGLILPNGNINWNCPCLGGMASGPCGEQFKSAFSCFHYSTEEIKGSDCVDQFRAMQECMQKYPDLYPQEDEDEEEEREKKPAEQAEETAPIEATATKEEEGSS |
| Purity : |
> 90% as determined by SDS-PAGE. |
| Notes : |
Repeated freezing and thawing is not recommended. Store working aliquots at 4 centigrade for up to one week. |
| Storage : |
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 centigrade/-80 centigrade. The shelf life of lyophilized form is 12 months at -20 centigrade/-80 centigrade. |
| Concentration : |
A hardcopy of COA with concentration instruction is sent along with the products. |
