Specification
| Organism | Homo sapiens (Human) |
| Expression Host | E.coli |
| Tag Info | N-terminal 6xHis-SUMO-tagged |
| Purity | Greater than 85% by SDS-PAGE |
| Uniprot ID | Q8N4Q1 |
| Gene Names | CHCHD4 |
| Alternative Names | Coiled-coil-helix-coiled-coil-helix domain-containing protein 4 |
| Expression Region | Full Length(1-142aa ) |
| Molecular Weight | 32 kDa |
| Protein Sequence | MSYCRQEGKDRIIFVTKEDHETPSSAELVADDPNDPYEEHGLILPNGNINWNCPCLGGMASGPCGEQFKSAFSCFHYSTEEIKGSDCVDQFRAMQECMQKYPDLYPQEDEDEEEEREKKPAEQAEETAPIEATATKEEEGSS |
| Form | Liquid or Lyophilization |
| Buffer | The default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol if the delivery form is liquid. The lyophilization buffer is Tris/PBS-based buffer, 6% Trehalose, pH 8.0 if the delivery form is lyophilized powder. Please contact us if you have any special requirment. |
| Reconstitution | Please reconstitute protein in deionized sterile water and we recommend that briefly centrifuge thevial prior to opening the vial .We recommend aliquot for long-term storage at -20℃/-80℃. |
Background
| Relevance | 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. |
| Involvement in Disease | |
| Subcellular Location | Mitochondrion intermembrane space |
| Protein Families | |
| Tissue Specificity | CHCHD4 |
QC Data
| Note | Please contact us for QC Data |
| Product Image (Reference Only) |  |