PLA2G2A Recombinant Rabbit mAb

PLA2G2A, i.e., type IIA secreted phospholipase A2 (sPLA2-IIA), is a calcium-dependent secreted phospholipase of approximately 14 kDa; the mature protein contains about 144 amino acids and possesses a conserved calcium-binding loop and a catalytic His-Asp dyad active center, enabling it to hydrolyze the sn-2 ester bond of membrane phospholipids to release arachidonic acid and lysophospholipids. As an acute-phase protein, its plasma concentration can rise markedly in systemic inflammatory states such as sepsis and rheumatoid arthritis, and it is regarded as a biomarker of inflammatory responses. In terms of host defense, sPLA2-IIA exhibits potent bactericidal activity against Gram-positive bacteria; the high concentration of sPLA2-IIA in tears accounts for the major antibacterial function of tears, and transgenic mice overexpressing this protein show reduced mortality after Staphylococcus aureus infection. In addition, the protein participates in inflammatory regulation through catalysis-independent mechanisms, for example, promoting COX-2 expression and prostaglandin E2 production in a manner independent of catalytic activity. In tumor biology, the role of sPLA2-IIA is context-dependent: in prostate and breast cancer, its high expression is associated with aggressive progression and poor prognosis, and inhibiting its expression or activity can attenuate tumor growth and metastasis, whereas in colorectal cancer it may exert tumor-suppressive functions. Serum sPLA2-IIA levels are elevated in patients with various advanced malignancies and correlate with inflammatory and coagulation markers, suggesting its potential value as a prognosis-related biomarker.