Analytical Data
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Gene name
MFF
- Application
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Alternative Names
C2orf33
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9GZY8
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Expression Region
1-322aa
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Molecular Weight
39.9 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
Related Products
Protein Description
MFF (Mitochondrial Fission Factor) is a critical protein involved in the regulation of mitochondrial dynamics, particularly in the process of mitochondrial fission, which is vital for maintaining cellular health and function. Research into MFF has gained momentum due to its implications in various physiological and pathological contexts, including metabolic disorders, neurodegenerative diseases, and cancer. The ability of mitochondria to undergo fission and fusion is essential for their integrity and functionality, as well as for the maintenance of cellular homeostasis. MFF acts by recruiting dynamin-related protein 1 (Drp1) to the outer mitochondrial membrane, facilitating the constriction and division of mitochondria. Dysregulation of this process can lead to an excessive or insufficient mitochondrial fission, contributing to the pathogenesis of several diseases. Consequently, understanding the molecular mechanisms governing MFF and its interactions with other cellular proteins can provide insights into therapeutic strategies aimed at restoring proper mitochondrial function. Recent advances in recombinant protein technology have enabled the production and study of MFF in detail, allowing researchers to explore its structure, functional domains, and regulatory mechanisms. This research not only enhances our understanding of mitochondrial biology but also opens new avenues for potential interventions in diseases linked to mitochondrial dysfunction.
