Recombinant Human Mitochondrial Intermembrane Space Import And Assembly Protein 40 (CHCHD4) Protein (His-SUMO)

Name: Recombinant Human Mitochondrial Intermembrane Space Import And Assembly Protein 40 (CHCHD4) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-09881P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Mitochondrial Intermembrane Space Import And Assembly Protein 40 (CHCHD4) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q8N4Q1
Target Symbol	CHCHD4
Synonyms	CHCHD4; MIA40Mitochondrial intermembrane space import and assembly protein 40; Coiled-coil-helix-coiled-coil-helix domain-containing protein 4
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MSYCRQEGKDRIIFVTKEDHETPSSAELVADDPNDPYEEHGLILPNGNINWNCPCLGGMASGPCGEQFKSAFSCFHYSTEEIKGSDCVDQFRAMQECMQKYPDLYPQEDEDEEEEREKKPAEQAEETAPIEATATKEEEGSS
Expression Range	1-142aa
Protein Length	Full Length
Mol. Weight	32.0kDa
Research Area	Transport
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Central component of a redox-sensitive mitochondrial intermembrane space import machinery which is required for the biogenesis of respiratory chain complexes. Functions as chaperone and catalyzes the formation of disulfide bonds in substrate proteins, such as COX17, COX19, MICU1 and COA7. 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. 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 system. Mediates formation of disulfide bond in MICU1 in the IMS, promoting formation of the MICU1-MICU2 heterodimer that regulates mitochondrial calcium uptake.
Subcellular Location	Mitochondrion intermembrane space.
Database References	HGNC: 26467 OMIM: 611077 KEGG: hsa:131474 STRING: 9606.ENSP00000295767 UniGene: Hs.517815
Tissue Specificity	Expressed in all tissues tested, suggesting an ubiquitous expression.

Gene Functions References

First group to discover the expression of the human CHCHD4 isoforms and first to call the human gene CHCHD4, and to clone and show the expression of its alternatively expressed CHCHD4 isoforms (CHCHD4.1 and CHCHD4.2). PMID: 22214851
Compared to wild type control littermates, mice with a knockout of CHCHD4 exhibit reduced weight gain when fed a high-fat diet. PMID: 26178476
Data show that the redox state of cytochrome c oxidase assembly protein 17 (Cox17), mitochondrial membrane transport protein Mia40 and superoxide dismutase 1 (SOD1) in the cytoplasm were directly observed with in-cell NMR spectroscopy. PMID: 26589182
our findings suggest that MIA40 reduction contributes to the effects of AIF deficiency on OXPHOS, as it may impact on the correct assembly and maintenance of the respiratory subunits. PMID: 26158520
results demonstrate an indispensable role for hMIA40 for the export of Fe-S clusters from mitochondria. PMID: 26275620
Data indicate that poptosis-inducing factor (AIF) controls the mitochondrial import of mitochondrial membrane transport protein CHCHD4. PMID: 26004228
In aggregate these data suggest that the Mia40/lfALR system has a broad sequence specificity and that potential substrates may be protected from adventitious oxidation by kinetic sequestration within the mitochondrial IMS. PMID: 26014136
Import and oxidative folding of proteins are kinetically and functionally coupled and depend on the expression of Mia40, ALR, and the intracellular glutathione pool. PMID: 23676665
Data indicate that decreased CHCHD4 expression prevents the mitochondrial translocation of p53 while augmenting its nuclear localization and activity. PMID: 24101517
illustrate a very atypical behaviour for the Mia40 precursor compared to other substrates of the MIA pathway. By contrast, interaction with Erv1 occurs after 5 min of import and relies on a more stringent specificity PMID: 23937629
mitochondrial localization of MIA40 requires sulfhydryl oxidase ALR in heterologous expression yeast system. PMID: 23186364
Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR. PMID: 21383138
biogenesis and function of MIA40 in the mitochondrial intermembrane space is dependent on redox processes involving conserved cysteine residues PMID: 16185709
After passage across the translocase of the mitochondrial outer membrane Erv1 interacts via disulfide bonds with Mia40. PMID: 17336303
analysis of how mitochondrial biogenesis switches the sorting pathway of the intermembrane space receptor Mia40 PMID: 18779329
Catalysis involves a flow of reducing equivalents from the reduced CxC cysteine motif of Mia40 to distal and then proximal CxxC motifs of long-form ALR to the flavin ring and, finally, to cytochrome c or molecular oxygen. PMID: 19397338

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.