BPIFA1 Protein, Human

BPIFA1 Protein, a lipid-binding protein, exhibits high specificity for the surfactant phospholipid DPPC. It plays a crucial role in the innate immune responses of the upper airways, reducing surface tension, inhibiting biofilm formation by pathogenic bacteria, and negatively regulating proteolytic cleavage of SCNN1G, contributing to airway surface liquid homeostasis. BPIFA1 may also attract macrophages and neutrophils. BPIFA1 Protein, Human is the recombinant human-derived BPIFA1 protein, expressed by E. coli , with tag free. The total length of BPIFA1 Protein, Human is 237 a.a., with molecular weight of 24.8 kDa.

BPIFA1 protein, a lipid-binding molecule with a distinct affinity for the surfactant phospholipid dipalmitoylphosphatidylcholine (DPPC), plays a pivotal role in the innate immune responses within the upper airways. By reducing surface tension in airway secretions and impeding biofilm formation by pathogenic Gram-negative bacteria, such as P. aeruginosa and K. pneumoniae, BPIFA1 contributes to the host's defense mechanisms. Furthermore, it negatively regulates the proteolytic cleavage of SCNN1G, a crucial event for the activation of the epithelial sodium channel (ENaC), thereby maintaining airway surface liquid homeostasis and facilitating proper mucus clearance. BPIFA1 also participates in the inflammatory response following exposure to irritants and may attract immune cells like macrophages and neutrophils. Structurally, BPIFA1 functions as a monomer and interacts with SCNN1B, a subunit of the heterotrimeric ENaC, inhibiting its proteolytic activation. This multifaceted role highlights the importance of BPIFA1 in orchestrating various aspects of airway defense and homeostasis.

Human

E. coli

Tag Free

Q9NP55-1 (Q20-V256)

51297  [NCBI]

24.8 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.