Analytical Data
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Gene name
SUMF1
- Application
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Alternative Names
FGE; C-alpha-formylglycine-generating enzyme 1
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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
Q8NBK3
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Expression Region
Glu113~Ser356
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Molecular Weight
31kDa
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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
SUMF1, or Sulfatase Modifying Factor 1, is a pivotal protein involved in the post-translational modification of sulfatases, a family of enzymes critical for the degradation of sulfated glycosaminoglycans and other sulfated compounds. Mutations in the SUMF1 gene can lead to sulfatase deficiencies, resulting in a range of lysosomal storage disorders, with notable examples including Multiple Sulfatase Deficiency (MSD), which is characterized by severe neurological, skeletal, and systemic abnormalities. The study of SUMF1 and its role in the functional activation of sulfatases is essential for understanding the biochemical pathways involved in these ailments, as well as for exploring potential therapeutic strategies. Researchers are increasingly focused on elucidating the mechanisms through which SUMF1 facilitates the maturation of sulfatases, particularly by characterizing its structural features and interactions with other molecular partners. Given that sulfatase deficiencies are often linked to complex phenotypes and significant morbidity, developing SUMF1-targeted therapies or enzyme replacement strategies offers promise for improving clinical outcomes for affected individuals. Furthermore, investigating the broader implications of SUMF1 in various biological processes, including cell signaling and metabolic regulation, may reveal new insights into its functions beyond sulfatase activation. Thus, the ongoing research into SUMF1 not only advances our understanding of specific genetic disorders but also highlights the intricate regulatory networks that govern cellular homeostasis and disease.











