Analytical Data
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Gene name
MFF
- Application
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Alternative Names
MFF；C2orf33；Mitochondrial fission factor
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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
1-342aa
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AA Sequence
MSKGTSSDTSLGRVSRAAFPSPTAAEMAEISRIQYEMEYTEGISQRMRVPEKLKVAPPNADLEQGFQEGVPNASVIMQVPERIVVAGNNEDVSFSRPADLDLIQSTPFKPLALKTPPRVLTLSERPLDFLDLERPPTTPQNEEIRAVGRLKRERSMSENAVRQNGQLVRNDSLWHRSDSAPRNKISRFQAPISAPEYTVTPSPQQARVCPPHMLPEDGANLSSARGILSLIQSSTRRAYQQILDVLDENRRPVLRGGSAAATSNPHHDNVRYGISNIDTTIEGTSDDLTVVDAASLRRQIIKLNRRLQLLEEENKERAKREMVMYSITVAFWLLNSWLWFRR
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Molecular Weight
38.4 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 pivotal protein involved in the regulation of mitochondrial dynamics, particularly mitochondrial fission. Mitochondrial fission is essential for various cellular processes, including apoptosis, mitophagy, and maintaining cellular energy homeostasis. Research on MFF has gained momentum due to its implications in several pathophysiological conditions, including neurodegenerative diseases, metabolic disorders, and cancer. Understanding the structural and functional attributes of MFF, especially its interactions with other key proteins involved in mitochondrial division, can provide insights into the mechanisms of mitochondrial dysfunction. Furthermore, the study of MFF has potential therapeutic implications, as targeting its pathways may help in developing strategies to mitigate diseases linked to impaired mitochondrial dynamics. Recombination technologies have enabled researchers to create MFF fusion proteins, allowing detailed investigation of its functional domains and post-translational modifications. These studies aim to elucidate the role of MFF in cellular health and disease, paving the way for novel interventions in mitochondria-related disorders.
