Analytical Data
-
基因名
MFSD8
- Application
-
别名
Ceroid-lipofuscinosis neuronal protein 7
-
种属
Human
-
表达系统
E. coli
-
标签
N- His-GST
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
Q8NHS3
-
表达区间
1-40aa
-
分子量
34.8 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
-
稳定性测试
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.
-
保存条件 & 期限
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.
-
运输条件
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.
