Summary:
coiled-coil-helix-coiled-coil-helix domain containing 4
Cat：P06254
| 【Derived From】： E.coli |
| 【Endotoxin】： Not measured |
| 【Amino Acid】： 1-143aa |
| 【Purity】： ≥85% by SDS-PAGE. |
| 【Name】： CHCHD4 |
| 【Full Name】： coiled-coil-helix-coiled-coil-helix domain containing 4 |
| 【Uniprot】： Q8N4Q1 |
| 【Gene ID】： 131474 |
| 【Species Reactivity】： Human Mouse Rat (Bovine Zebrafish) |
| 【Mol Mass】： 16kDa |
| 【Application】： Immunology research |
| 【Purification】： NI-NTA affinity purification |
| 【Bioactive】： No activity experimental data, to be verified. |
| 【Tag】： With a 6×His tag at the N/C-terminus. |
| 【Concentration】： 1mg/ml by SDS-PAGE. |
Store:
| 【Reconstitution】： Reconstituted protein solution can be diluted with distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. (It is not recommended to reconstitute to a concentration less than 10μg/ml. Dissolve the lyophilized protein in distilled water.) |
| 【Storage】： Reconstituted protein solution can be stored at 4-7℃ for 2-7 days， stored at < -20℃ for 1 year. |
| 【Formulation】： Powder: Lyophilized from a 0.2 μm filtered solution of 20mM Tris-HCl, 150mM NaCl, 1mM DTT, PH7.2-8.0. |
Background:
Central component of a redox-sensitive mitochondrial intermembrane space import machinery which is required for the biogenesis of respiratory chain complexes (PubMed:26004228).Functions as chaperone and catalyzes the formation of disulfide bonds in substrate proteins, such as COX17, COX19, MICU1 and COA7 (PubMed:16185709, PubMed:26387864, PubMed:19182799, PubMed:21059946, PubMed:23186364, PubMed:23676665, PubMed:30885959).Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS). Required for the import of COA7 in the IMS (PubMed:30885959).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 (PubMed:16185709, PubMed:19182799
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