Analytical Data
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Gene name
MFSD8
- Application
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Alternative Names
Ceroid-lipofuscinosis neuronal protein 7
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Species
Human
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Source
E. coli
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Tag
N- His-GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8NHS3
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Expression Region
1-40aa
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Molecular Weight
34.8 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
MFSD8 (Major Facilitator Superfamily Domain Containing 8) is a member of the major facilitator superfamily of transport proteins, which play crucial roles in the transportation of various substrates across cellular membranes. Recent studies have highlighted the importance of MFSD8 in human health, particularly its association with certain neurological disorders. Mutations in the MFSD8 gene have been linked to a rare lysosomal storage disease known as "sialic acid storage disorder," characterized by severe neurological deficits due to impaired lysosomal function and accumulation of sialic acid. Understanding the structure and function of MFSD8 is vital for elucidating its role in cellular metabolism and disease mechanisms. The reconstitution of MFSD8 as a recombinant protein enables detailed functional and structural studies, facilitating insights into its transport activity and substrate specificity. Furthermore, this research may pave the way for potential therapeutic interventions and strategies aimed at correcting the underlying molecular defects associated with MFSD8 dysfunction. Investigating the biophysical properties of MFSD8, its interaction with its substrates, and its regulatory mechanisms could contribute significantly to our understanding of lysosomal pathophysiology and the development of targeted treatments for related disorders.
