Analytical Data
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Gene name
SFTPC
- Application
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Alternative Names
Pulmonary surfactant-associated proteolipid SPL(Val)SP5
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Species
Human
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Source
HEK293
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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
P11686
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Expression Region
24-58aa
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Molecular Weight
7.7 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
SFTPC, or Surfactant Protein C, is a critical component of pulmonary surfactant, which plays a vital role in reducing surface tension in the alveoli and is essential for normal lung function. Dysregulation or mutations in the SFTPC gene have been linked to various pulmonary disorders, including surfactant metabolism disorders and interstitial lung diseases. Given its importance, researchers have focused on generating recombinant SFTPC proteins to better understand their structure, function, and role in disease processes. By employing techniques such as gene cloning and expression in suitable systems, scientists can produce sufficient quantities of SFTPC for biochemical studies and functional assays. This research not only enhances our understanding of lung biology but also opens up potential therapeutic avenues for diseases associated with surfactant dysfunction. Additionally, the study of SFTPC in recombinant form can provide insights into protein stability, interactions with lipids, and the mechanisms underlying surfactant aggregation and function, thereby contributing to the development of novel treatments for respiratory conditions. As the need for effective therapies for lung diseases continues to grow, the investigation of SFTPC and its recombinant forms remains a significant area of interest in biomedical research.
