Analytical Data
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Gene name
CFTR
- Application
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Alternative Names
CFTR；ABCC7；Cystic fibrosis transmembrane conductance regulator
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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
P13569
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Expression Region
1381-1480aa
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AA Sequence
YQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKL LNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL
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Molecular Weight
37 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
The cystic fibrosis transmembrane conductance regulator (CFTR) is a vital protein that functions as a chloride channel in epithelial cells, playing a crucial role in maintaining the balance of salt and water across cell membranes. Mutations in the CFTR gene lead to cystic fibrosis (CF), a genetic disorder characterized by thick mucus production, respiratory problems, and impaired pancreatic function. Research on CFTR recombinant proteins has gained significant attention due to their potential to elucidate the mechanisms underlying CFTR function and dysfunction. The study of CFTR's structure, dynamics, and interaction with various cellular components is essential for understanding the molecular basis of CF and developing targeted therapies. By employing techniques such as protein expression in heterologous systems, site-directed mutagenesis, and advanced imaging methods, scientists aim to dissect the channel's gating mechanisms and ion transport properties. Furthermore, the characterization of CFTR recombinant proteins offers insights into how specific mutations affect its function, paving the way for the design of novel pharmacological agents, such as small molecules and gene therapies, that could restore CFTR activity and improve outcomes for individuals with cystic fibrosis. As research progresses, the integration of structural biology, biophysics, and pharmacology continues to enhance our understanding of CFTR, highlighting its significance as a therapeutic target and a model for studying ion channel diseases.
