Recombinant human CHCHD3 protein
€0.00
In stock
SKU
ATGP2378
Description
Coiled-coil-helix-coiled-coil-helix domain containing protein 3, also known as CHCHD3, is required for maintenance of mitochondrial crista integrity and mitochondrial function. This protein may act as a scaffolding protein that stabilizes protein complexes involved in crista architecture and protein import. It has also been shown to function as a transcription factor which binds to the BAG1 promoter and represses BAG1 transcription. Recombinant human CHCHD3 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.Alternative Names
Coiled-coil-helix-coiled-coil-helix domain containing protein 3, MINOS3, PPP1R22Concentration
0.25mg/ml (determined by Bradford assay)Concentration
Liquid in. 20mM Tris-HCl buffer (pH 8.0) containing 0.2M NaCl, 50% glycerol, 2mM DTTStorage: Can be stored at +2C to +8C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.
Coiled-coil-helix-coiled-coil-helix domain containing protein 3, also known as CHCHD3, is required for maintenance of mitochondrial crista integrity and mitochondrial function. This protein may act as a scaffolding protein that stabilizes protein complexes involved in crista architecture and protein import. It has also been shown to function as a transcription factor which binds to the BAG1 promoter and represses BAG1 transcription. Recombinant human CHCHD3 protein, fused to His-tag at N-terminus, was expressed in E. coli and purified by using conventional chromatography techniques.Alternative Names
Coiled-coil-helix-coiled-coil-helix domain containing protein 3, MINOS3, PPP1R22Concentration
0.25mg/ml (determined by Bradford assay)Concentration
Liquid in. 20mM Tris-HCl buffer (pH 8.0) containing 0.2M NaCl, 50% glycerol, 2mM DTTStorage: Can be stored at +2C to +8C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.
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