CFTR Antibody (Mouse mAb) [P23G6]

Application: Reactivity: Human

Usage Information

Dilution
WB1:1000

Application
WB, IP, IF

Reactivity
Human

Source
Mouse Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
168 kDa

Datasheet & SDS

Biological Description

Specificity
CFTR Antibody (Mouse mAb) [P23G6] detects endogenous levels of total CFTR protein.

Clone
P23G6

Synonym(s)
CFTR

Background
CFTR (cystic fibrosis transmembrane conductance regulator) is a cAMP‑regulated anion channel of the ABC transporter family that localizes predominantly to the apical membrane of secretory epithelia in the airways, pancreas, intestine and hepatobiliary tract, where it mediates chloride and bicarbonate fluxes that drive transepithelial salt and fluid movement and thereby control mucus hydration, luminal pH and host–pathogen interactions. The protein comprises two transmembrane domains forming the anion‑selective pore, two cytosolic nucleotide‑binding domains that bind and hydrolyze ATP, and a unique regulatory domain rich in phosphorylation sites; phosphorylation of the regulatory domain by cAMP‑dependent protein kinase activates CFTR, while ATP binding and hydrolysis at the nucleotide‑binding domains gate the pore, producing bursts of channel openings that sustain epithelial fluid secretion. At the apical surface of intestinal enterocytes, CFTR is the principal pathway for chloride secretion during cAMP‑mediated secretory diarrhea, with enterotoxins such as cholera toxin elevating cAMP and stimulating CFTR‑dependent chloride and water efflux into the lumen, and pharmacologic studies show that small‑molecule CFTR inhibitors and blockers of its basolateral chloride uptake partner NKCC1 markedly reduce enterotoxin‑induced fluid loss, highlighting CFTR’s central role in intestinal fluid homeostasis and its value as a therapeutic target in diarrheal disease. CFTR expression is finely regulated along the crypt–villus axis and between epithelial subtypes, and specialized CFTR High Expresser cells in the proximal small intestine show markedly elevated CFTR abundance and cAMP‑stimulated recruitment of CFTR and NKCC1, consistent with a dedicated role in high‑volume chloride‑driven fluid secretion on villi. The most common cystic fibrosis‑causing mutation, ΔF508, deletes a phenylalanine in the first nucleotide‑binding domain, destabilizes CFTR folding, impairs trafficking to the apical membrane and reduces channel activity, leading to defective chloride and bicarbonate transport, thickened airway mucus, pancreatic insufficiency, intestinal obstruction and progressive lung and liver disease; structural and functional analyses of CFTR have provided the basis for corrector and potentiator therapies that improve ΔF508 CFTR folding, trafficking and gating in patients. CFTR also participates directly in host–pathogen interactions: typhoid fever begins when Salmonella typhi crosses the intestinal epithelium, and experimental work shows that S. typhi, but not S. typhimurium, uses CFTR as an entry receptor on gastrointestinal epithelial cells, with cells expressing wild‑type CFTR internalizing more S. typhi than those expressing ΔF508 CFTR, and monoclonal antibodies or peptides corresponding to the first predicted extracellular CFTR loop blocking S. typhi uptake. In vivo, heterozygous ΔF508 Cftr mice translocate 86% fewer S. typhi into the gastrointestinal submucosa than wild‑type mice, while homozygous ΔF508 Cftr mice show no S. typhi translocation, and immunoelectron microscopy detects more CFTR bound to S. typhi in submucosa of wild‑type than ΔF508 heterozygous mice, indicating that reduced CFTR function or abundance diminishes typhoid pathogen entry and suggesting a mechanism by which CFTR mutations could confer selective resistance to typhoid in endemic regions. CFTR dysfunction from mutations or acquired regulation is also linked to gastrointestinal cancers, inflammatory bowel disease and other extra‑pulmonary pathologies through effects on epithelial barrier function, luminal pH, microbiota composition and chronic inflammation, underscoring that CFTR is both a chloride/bicarbonate channel central to epithelial fluid physiology and a modulatory receptor interface for microbes and immune responses.

Background

CFTR (cystic fibrosis transmembrane conductance regulator) is a cAMP‑regulated anion channel of the ABC transporter family that localizes predominantly to the apical membrane of secretory epithelia in the airways, pancreas, intestine and hepatobiliary tract, where it mediates chloride and bicarbonate fluxes that drive transepithelial salt and fluid movement and thereby control mucus hydration, luminal pH and host–pathogen interactions. The protein comprises two transmembrane domains forming the anion‑selective pore, two cytosolic nucleotide‑binding domains that bind and hydrolyze ATP, and a unique regulatory domain rich in phosphorylation sites; phosphorylation of the regulatory domain by cAMP‑dependent protein kinase activates CFTR, while ATP binding and hydrolysis at the nucleotide‑binding domains gate the pore, producing bursts of channel openings that sustain epithelial fluid secretion. At the apical surface of intestinal enterocytes, CFTR is the principal pathway for chloride secretion during cAMP‑mediated secretory diarrhea, with enterotoxins such as cholera toxin elevating cAMP and stimulating CFTR‑dependent chloride and water efflux into the lumen, and pharmacologic studies show that small‑molecule CFTR inhibitors and blockers of its basolateral chloride uptake partner NKCC1 markedly reduce enterotoxin‑induced fluid loss, highlighting CFTR’s central role in intestinal fluid homeostasis and its value as a therapeutic target in diarrheal disease. CFTR expression is finely regulated along the crypt–villus axis and between epithelial subtypes, and specialized CFTR High Expresser cells in the proximal small intestine show markedly elevated CFTR abundance and cAMP‑stimulated recruitment of CFTR and NKCC1, consistent with a dedicated role in high‑volume chloride‑driven fluid secretion on villi. The most common cystic fibrosis‑causing mutation, ΔF508, deletes a phenylalanine in the first nucleotide‑binding domain, destabilizes CFTR folding, impairs trafficking to the apical membrane and reduces channel activity, leading to defective chloride and bicarbonate transport, thickened airway mucus, pancreatic insufficiency, intestinal obstruction and progressive lung and liver disease; structural and functional analyses of CFTR have provided the basis for corrector and potentiator therapies that improve ΔF508 CFTR folding, trafficking and gating in patients. CFTR also participates directly in host–pathogen interactions: typhoid fever begins when Salmonella typhi crosses the intestinal epithelium, and experimental work shows that S. typhi, but not S. typhimurium, uses CFTR as an entry receptor on gastrointestinal epithelial cells, with cells expressing wild‑type CFTR internalizing more S. typhi than those expressing ΔF508 CFTR, and monoclonal antibodies or peptides corresponding to the first predicted extracellular CFTR loop blocking S. typhi uptake. In vivo, heterozygous ΔF508 Cftr mice translocate 86% fewer S. typhi into the gastrointestinal submucosa than wild‑type mice, while homozygous ΔF508 Cftr mice show no S. typhi translocation, and immunoelectron microscopy detects more CFTR bound to S. typhi in submucosa of wild‑type than ΔF508 heterozygous mice, indicating that reduced CFTR function or abundance diminishes typhoid pathogen entry and suggesting a mechanism by which CFTR mutations could confer selective resistance to typhoid in endemic regions. CFTR dysfunction from mutations or acquired regulation is also linked to gastrointestinal cancers, inflammatory bowel disease and other extra‑pulmonary pathologies through effects on epithelial barrier function, luminal pH, microbiota composition and chronic inflammation, underscoring that CFTR is both a chloride/bicarbonate channel central to epithelial fluid physiology and a modulatory receptor interface for microbes and immune responses.

References
https://pubmed.ncbi.nlm.nih.gov/9922375/ https://pubmed.ncbi.nlm.nih.gov/9590693/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%