Analytical Data
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Gene name
SP-C
- Application
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Alternative Names
SP-C；GC1QBP；HABP1；SF2P32；Complement component 1 Q subcomponent-binding Protein. mitochondrial
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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
P11686
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Expression Region
24-58aa
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AA Sequence
FGIPCCPVHLKRLLIVVVVVVLIVVVIVGALLMGL
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Molecular Weight
5.7kDa
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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
Surfactant Protein C (SP-C) is a pivotal component of pulmonary surfactant, crucial for reducing surface tension in the alveoli, thereby preventing lung collapse during exhalation and ensuring efficient gas exchange. The gene encoding SP-C is located on chromosome 8, and mutations or deficiencies in this protein can lead to severe respiratory conditions, such as surfactant dysfunction disorders and interstitial lung disease. The study of SP-C has become increasingly significant, particularly in understanding its role in lung health and disease, as well as in the development of therapeutic interventions. Recombinant SP-C proteins, produced using biotechnological methods, have emerged as potential therapeutic agents in treating surfactant abnormalities. Research has focused on the structure-function relationship of SP-C, exploring how modifications in the protein can enhance its stability and functionality. Furthermore, investigations into the molecular mechanisms by which SP-C interacts with lipids and other proteins in surfactant complexes provide valuable insights into respiratory physiology. Recent advances in gene therapy and protein engineering aim to correct SP-C deficiencies, offering hope for patients suffering from related pulmonary disorders. This underscores the importance of SP-C recombinant protein research in developing novel strategies for the prevention and treatment of various lung diseases.
