Uteroglobin Recombinant Rabbit mAb (S-6021)

Uteroglobin, also known as Clara cell secretory protein (CC16) or secretoglobin family 1A member 1 (SCGB1A1), is a steroid hormone-inducible, evolutionarily highly conserved homodimeric secretory protein first discovered in the uterine fluid of pregnant rabbits during early gestation, and has since been confirmed to be widely expressed in the mucosal epithelium of nearly all organs that communicate with the external environment. This protein possesses multiple biological functions, with its core role manifested in potent anti-inflammatory and immunomodulatory properties: it inhibits the activity of secretory phospholipase A2 (sPLA2), binds and sequesters various hydrophobic ligands such as progesterone, retinol, and phospholipids, and exhibits anti-chemotactic, anti-allergic, and anti-tumor activities. In the respiratory system, it is abundantly secreted by non-ciliated bronchial Clara cells and is essential for protecting the respiratory tract from oxidative stress and inflammatory damage; in addition, studies have revealed that it plays a key role in maintaining normal renal function by binding fibronectin with high affinity in the glomerulus to inhibit abnormal extracellular matrix deposition. Based on its pleiotropic effects, polymorphisms in the SCGB1A1 gene are associated with the risk of inflammatory diseases such as asthma, while gene knockout mouse models have confirmed that deficiency of this protein exacerbates lung infections and glomerular lesions, highlighting its important value in maintaining homeostasis.