The cystic fibrosis transmembrane conductance regulator (CFTR) is a critical protein that maintains the salt and water balance across various human organs, including the lungs, pancreas, and sweat glands. The primary function of CFTR is to act as a chloride channel, regulating the transport of chloride and bicarbonate ions across epithelial cell membranes, thereby maintaining tissue fluid balance and pH. This process is ATP-dependent and also modulates the activity of other ion channels and transport proteins ^[1-2]. Mutations in the CFTR gene can lead to chloride channel dysfunction, resulting in various diseases, with cystic fibrosis (CF) being the most common. CF is the most prevalent lethal genetic disease among Caucasians, with an incidence of approximately 1/2,500 to 1/1,800, and about 90,000 cases globally ^[3-4]. The disease is characterized by thickened mucus in the lungs, frequent respiratory infections, pancreatic insufficiency, and male infertility, typically due to vas deferens obstruction. The G551D mutation is a clinically significant genetic defect in the CFTR gene, which is classified as a Class III mutation and is the third most common CF-associated mutation worldwide, occurring in about 3% of CF patients ^[5]. This missense mutation involves a single amino acid substitution where Glycine (G) is replaced by Aspartic Acid (D) at position 551 within the first Nucleotide Binding Domain (NBD1) of the CFTR protein. The defining molecular pathology is a severe gating defect; while the CFTR chloride channel is correctly processed and successfully trafficked to the apical membrane of epithelial cells, its probability of opening is drastically reduced (approximately 100-fold lower than the wild-type channel). This impairment in channel opening results in a critical reduction in chloride and bicarbonate transport, leading to the characteristic buildup of thick, dehydrated mucus in multiple organs and a severe clinical phenotype. Current treatments for CF mainly focus on CFTR modulators to restore the function of the mutated CFTR protein. CFTR modulators are classified into potentiators (which enhance CFTR function) and correctors (which assist in the proper folding and trafficking of CFTR to the cell membrane). Representative drugs include Ivacaftor, Lumacaftor, and triple-combination CFTR modulating therapy Elexacaftor-Tezacaftor-Ivacaftor ^[6]. The G551D mutation holds particular importance in CF research and therapy as it was the first genotype-specific mutation to be successfully targeted by a CFTR potentiator drug, Ivacaftor, which functions by increasing the opening probability of the mutant channel. huCFTR-G551D mice were developed by introducing the G551D mutation into the CFTR-humanized mouse model (Catalog Number: C001964), creating a humanized disease model. It is suitable for research into CF mechanisms and the development of therapies targeting the CFTR G551D mutation. This strain requires feeding with intestinal cleansers to maintain survival. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on the CFTR-humanized strain and provide customized services for specific mutations to meet the experimental needs in pharmacology and other fields.

The cystic fibrosis transmembrane conductance regulator (CFTR) is a critical protein that maintains the salt and water balance across various human organs, including the lungs, pancreas, and sweat glands. The primary function of CFTR is to act as a chloride channel, regulating the transport of chloride and bicarbonate ions across epithelial cell membranes, thereby maintaining tissue fluid balance and pH. This process is ATP-dependent and also modulates the activity of other ion channels and transport proteins ^[1-2]. Mutations in the CFTR gene can lead to chloride channel dysfunction, resulting in various diseases, with Cystic Fibrosis (CF) being the most common. CF is the most prevalent lethal genetic disease among Caucasians, with an incidence of approximately 1/2,500 to 1/1,800, and about 90,000 cases globally ^[3-4]. The disease is characterized by thickened mucus in the lungs, frequent respiratory infections, pancreatic insufficiency, and male infertility, typically due to vas deferens obstruction. The F508del and G542X are the most common mutations found in US patients, accounting for 86.4% and 4.6% of all mutations, respectively ^[5]. The G542X mutation is a common and severe cause of Cystic Fibrosis (CF), resulting from a single point mutation in the CFTR gene that creates a premature termination codon (PTC) at amino acid position 542; this classifies G542X as a Class I nonsense mutation. The presence of this PTC triggers a cellular quality control mechanism known as Nonsense-Mediated Decay (NMD), which targets the mutant mRNA for degradation, leading to a near-complete absence of functional CFTR protein at the epithelial cell surface. Consequently, patients with two copies of G542X often exhibit a severe form of CF, characterized by major organ dysfunction, and this lack of protein makes it a primary target for novel therapeutic strategies, such as readthrough agents and gene editing. Current treatments for CF mainly focus on CFTR modulators to restore the function of the mutated CFTR protein. CFTR modulators are classified into potentiators (which enhance CFTR function) and correctors (which assist in the proper folding and trafficking of CFTR to the cell membrane). Representative drugs include Ivacaftor, Lumacaftor, and triple-combination CFTR modulating therapy Elexacaftor-Tezacaftor-Ivacaftor ^[6]. huCFTR-G542* mice were developed by introducing the G542X mutation into the CFTR-humanized mouse model (Catalog Number: C001964), creating a humanized disease model. It is suitable for research into CF mechanisms and the development of therapies targeting the CFTR G542X mutation. This strain requires feeding with intestinal cleansers to maintain survival. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on the CFTR-humanized strain and provide customized services for specific mutations to meet the experimental needs in pharmacology and other fields.

The cystic fibrosis transmembrane conductance regulator (CFTR) is a critical protein that maintains the salt and water balance across various human organs, including the lungs, pancreas, and sweat glands. The primary function of CFTR is to act as a chloride channel, regulating the transport of chloride and bicarbonate ions across epithelial cell membranes, thereby maintaining tissue fluid balance and pH. This process is ATP-dependent and also modulates the activity of other ion channels and transport proteins ^[1-2]. Mutations in the CFTR gene can lead to chloride channel dysfunction, resulting in various diseases, with cystic fibrosis (CF) being the most common. CF is the most prevalent lethal genetic disease among Caucasians, with an incidence of approximately 1/2,500 to 1/1,800, and about 90,000 cases globally ^[3-4]. The disease is characterized by thickened mucus in the lungs, frequent respiratory infections, pancreatic insufficiency, and male infertility, typically due to vas deferens obstruction. The W1282X mutation is a prevalent and severe class I nonsense mutation (c.3846G>A, p.Trp1282Ter) in the CFTR gene, notably common in the Ashkenazi Jewish population ^[5]. This genetic alteration introduces a premature termination codon at position 1282, which prematurely truncates the synthesis of the CFTR protein. Consequently, the resulting shortened polypeptide is unstable and the corresponding mRNA is often degraded via the nonsense-mediated mRNA decay (NMD) pathway, leading to a near-complete absence of functional CFTR protein and an associated severe clinical phenotype of Cystic Fibrosis (CF). Current treatments for CF mainly focus on CFTR modulators to restore the function of the mutated CFTR protein. CFTR modulators are classified into potentiators (which enhance CFTR function) and correctors (which assist in the proper folding and trafficking of CFTR to the cell membrane). Representative drugs include Ivacaftor, Lumacaftor, and triple-combination CFTR modulating therapy Elexacaftor-Tezacaftor-Ivacaftor ^[6]. huCFTR-W1282* mice were developed by introducing the W1282X mutation into the CFTR-humanized mouse model (Catalog Number: C001964), creating a humanized disease model. It is suitable for research into CF mechanisms and the development of therapies targeting the CFTR W1282X mutation. This strain requires feeding with intestinal cleansers to maintain survival. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on the CFTR-humanized strain and provide customized services for specific mutations to meet the experimental needs in pharmacology and other fields.

The cystic fibrosis transmembrane conductance regulator (CFTR) is a critical protein that maintains the salt and water balance across various human organs, including the lungs, pancreas, and sweat glands. The primary function of CFTR is to act as a chloride channel, regulating the transport of chloride and bicarbonate ions across epithelial cell membranes, thereby maintaining tissue fluid balance and pH. This process is ATP-dependent and also modulates the activity of other ion channels and transport proteins ^[1-2]. Mutations in the CFTR gene can lead to chloride channel dysfunction, resulting in various diseases, with cystic fibrosis (CF) being the most common. CF is the most prevalent lethal genetic disease among Caucasians, with an incidence of approximately 1/2,500 to 1/1,800, and about 90,000 cases globally ^[3-4]. The disease is characterized by thickened mucus in the lungs, frequent respiratory infections, pancreatic insufficiency, and male infertility, typically due to vas deferens obstruction. The F508del (ΔF508) mutation is the most common pathogenic mutation in CF, with about 80% of CF patients carrying at least one allele of this mutation, and approximately 40% being homozygous ^[5]. This mutation causes the deletion of phenylalanine (F508) in the first nucleotide-binding domain (NBD1) of the CFTR protein, leading to misfolding and endoplasmic reticulum (ER)-mediated degradation, preventing CFTR from reaching the cell membrane and compromising chloride channel function, which results in chronic pulmonary symptoms ^[6-7]. Current treatments for CF mainly focus on CFTR modulators to restore the function of the mutated CFTR protein. CFTR modulators are classified into potentiators (which enhance CFTR function) and correctors (which assist in the proper folding and trafficking of CFTR to the cell membrane). Representative drugs include Ivacaftor, Lumacaftor, and triple-combination CFTR modulating therapy Elexacaftor-Tezacaftor-Ivacaftor ^[8]. This strain was developed by introducing the F508del mutation into the CFTR-humanized mouse model (Catalog Number: C001964), creating a humanized disease model. The introduction of the mutation results in the manifestation of CF-related phenotypes in mice, making it suitable for research into CF mechanisms and the screening, development, and evaluation of therapies targeting the CFTR F508del mutation. This strain requires feeding with intestinal cleansers to maintain survival after 3 weeks of age. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on the CFTR-humanized strain and provide customized services for specific mutations to meet the experimental needs in pharmacology and other fields.

The cystic fibrosis transmembrane conductance regulator (CFTR) is a critical protein that maintains the salt and water balance across various human organs, including the lungs, pancreas, and sweat glands. The primary function of CFTR is to act as a chloride channel, regulating the transport of chloride and bicarbonate ions across epithelial cell membranes, thereby maintaining tissue fluid balance and pH. This process is ATP-dependent and also modulates the activity of other ion channels and transport proteins ^[1-2]. Mutations in the CFTR gene can lead to chloride channel dysfunction, resulting in various diseases, with cystic fibrosis (CF) being the most common. CF is the most prevalent lethal genetic disease among Caucasians, with an incidence of approximately 1/2,500 to 1/1,800, and about 90,000 cases globally ^[3-4]. The disease is characterized by thickened mucus in the lungs, frequent respiratory infections, pancreatic insufficiency, and male infertility, typically due to vas deferens obstruction. The c.3718-2477C>T mutation is a relatively rare pathogenic cause of Cystic Fibrosis (CF). As a deep intronic variant, c.3718-2477C>T is classified as a splicing mutation, meaning its primary effect is likely to disrupt the normal process of mRNA splicing (the removal of non-coding introns and joining of coding exons) after transcription. This disruption can lead to a faulty or absent CFTR protein, ultimately resulting in the clinical manifestations of CF. Current treatments for CF mainly focus on CFTR modulators to restore the function of the mutated CFTR protein. CFTR modulators are classified into potentiators (which enhance CFTR function) and correctors (which assist in the proper folding and trafficking of CFTR to the cell membrane). Representative drugs include Ivacaftor, Lumacaftor, and triple-combination CFTR modulating therapy Elexacaftor-Tezacaftor-Ivacaftor ^[5]. B6-huCFTR*c.3718-2477C>T mice were developed by introducing the c.3718-2477C>T mutation into the CFTR-humanized mouse model (Catalog Number: C001964), creating a humanized disease model. It is suitable for research into CF mechanisms and the development of therapies targeting the CFTR c.3718-2477C>T mutation. This strain requires feeding with intestinal cleansers to maintain survival. In addition, based on the independently developed TurboKnockout fusion BAC recombination technology, Cyagen can also generate hot mutation models based on the CFTR-humanized strain and provide customized services for specific mutations to meet the experimental needs in pharmacology and other fields.

The huCFTR-G542X/hACE2 mouse is a humanized model obtained by mating the huCFTR-G542* mouse (Catalog Number: C001877) with the hACE2 mouse (Catalog Number: C001191). The huCFTR-G542* mouse requires feeding with intestinal cleansers to maintain survival. This model is mainly used in research on respiratory tract infections related to cystic fibrosis, as well as the development and evaluation of respiratory drugs.