Analytical Data
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Gene name
CFTR
- Application
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Alternative Names
ABC35; ABCC7; CF; CFTR/MRP; MRP7; TNR-CFTR; ATP-Binding Cassette Subfamily C,Member 7; Channel conductance-controlling ATPase; cAMP-dependent chloride channel
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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 95% as determined by SDS-PAGE.
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Uniprot
P13569
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Expression Region
Gln359~Ser858
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Molecular Weight
68kDa
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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
Cystic fibrosis transmembrane conductance regulator (CFTR) is a membrane protein that functions as a chloride channel and is crucial for maintaining ion balance and fluid secretion in various epithelial tissues. Mutations in the CFTR gene lead to cystic fibrosis (CF), a severe genetic disorder characterized by thick secretions in the lungs and digestive system, resulting in chronic infections, inflammation, and progressive lung damage. Due to its significant role in CF pathogenesis, CFTR has been a focal point of research aimed at understanding its structure and function, along with developing therapeutic strategies to correct CFTR dysfunction. Recent advances in protein engineering techniques have facilitated the production of recombinant CFTR proteins, allowing researchers to study its functional properties in isolation and in different cellular contexts. The development of these recombinant proteins has not only provided insights into the proper folding, trafficking, and gating mechanisms of CFTR but also has enabled the assessment of potential drugs aimed at restoring normal function in mutant CFTR variants. These studies are critical for advancing personalized medicine approaches for CF patients, including the evaluation of small molecules that can modulate CFTR activity, as well as gene therapy strategies aimed at correcting the underlying genetic defect. As such, the research into CFTR recombinant proteins is pivotal for unlocking new therapeutic avenues and improving the quality of life for individuals affected by cystic fibrosis.
