Analytical Data
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Gene name
SFTPB
- Application
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Alternative Names
SFTPB；SFTP3；Pulmonary surfactant-associated Protein B
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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
P07988
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Expression Region
201-279aa
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AA Sequence
FPIPLPYCWLCRALIKRIQAMIPKGALAVAVAQVCRVVPLVAGGICQCLAERYSVILLDTLLGRMLPQLVCRLVLRCSM
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Molecular Weight
8.7 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
SFTPB (Surfactant Protein B) is a critical component of pulmonary surfactant, which plays a vital role in reducing surface tension in the alveoli of the lungs, thus facilitating efficient gas exchange and preventing alveolar collapse. The study of SFTPB and its recombinant protein form has garnered significant attention due to its importance in lung physiology and pathophysiology. Deficiencies or mutations in the SFTPB gene are linked to various respiratory disorders, including neonatal respiratory distress syndrome and interstitial lung disease. By investigating the structure and function of recombinant SFTPB, researchers aim to understand its role in surfactant function and explore therapeutic implications for conditions associated with surfactant dysfunction. Furthermore, recombinant SFTPB offers potential for applications in drug delivery systems and the development of artificial surfactants that could benefit patients with compromised lung function. This ongoing research not only enhances our comprehension of lung biology but also contributes to the advancement of clinical strategies aimed at managing respiratory diseases, thus representing a significant area of interest within biomedical science.
