Analytical Data
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Gene name
CISD2
- Application
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Alternative Names
CDGSH iron-sulfur domain-containing protein 2. Endoplasmic reticulum intermembrane small protein. MitoNEET-related 1 protein. Miner1. Nutrient-deprivation autophagy factor-1. NAF-1
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8N5K1
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Expression Region
1-135aa
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AA Sequence
MVLESVARIVKVQLPAYLKRLPVPESITGFARLTVSEWLRLLPFLGVLALLGYLAVRPFLPKKKQQKDSLINLKIQKENPKVVNEINIEDLCLTKAAYCRCWRSKTFPACDGSHNKHNELTGDNVGPLILKKKEV
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Molecular Weight
41.7 KDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
CISD2 (CDGSH iron-sulfur domain 2) is a protein that plays a crucial role in cellular iron-sulfur cluster biogenesis, which is essential for various biological processes, including mitochondrial function and oxidative stress response. Dysregulation of CISD2 has been linked to several neurodegenerative diseases, such as Alzheimer's and Parkinson's, highlighting its importance in neuronal health. Recent studies have shown that CISD2 interacts with specific signaling pathways and contributes to the maintenance of mitochondrial integrity, suggesting its potential as a therapeutic target. The recombinant expression of CISD2 is thus pivotal for investigating its structural and functional properties in vitro. Researchers aim to produce high-purity CISD2 protein to elucidate its mechanisms of action, interaction partners, and the impact of specific mutations associated with disease. Understanding the functional dynamics of CISD2 could pave the way for novel therapeutic interventions in diseases characterized by mitochondrial dysfunction and impaired iron-sulfur metabolism. Overall, the study of CISD2 recombinant protein not only enhances our comprehension of fundamental cellular processes but also holds promise for advancing strategies in drug development for neurodegenerative diseases.











