PLAA Recombinant Monoclonal Antibody

Phospholipase A-2-activating protein (PLAA) serves as a critical regulator of phospholipase A2 activity, positioning it at the intersection of lipid signaling, membrane dynamics, and cellular stress responses. This protein has garnered research attention for its roles in inflammatory pathways and its emerging connections to protein quality control mechanisms, making it a valuable target for investigators studying diverse cellular processes.

This recombinant monoclonal antibody, generated in rabbit against a synthetic peptide derived from human PLAA, offers the reproducibility and consistency that demanding experimental workflows require. Because the antibody sequence is defined and production occurs through recombinant technology, researchers can expect reliable performance across experiments and over time, eliminating the lot-to-lot variability that can complicate long-term studies.

Validation data demonstrates robust performance across multiple applications. Western blot analysis confirms specific detection of PLAA at the predicted 87 kDa molecular weight across a diverse panel of human cell lines, including neuroblastoma (SH-SY5Y), glioblastoma (U-251MG), embryonic kidney (HEK293T), colorectal adenocarcinoma (HT-29), and epidermoid carcinoma (A431) lysates. This broad detection profile across neural, epithelial, and other cell types provides flexibility for researchers working with various model systems. Immunofluorescence staining in HeLa cells reveals clear cytoplasmic localization patterns, while flow cytometry analysis demonstrates effective discrimination between specific signal and background, enabling quantitative single-cell studies.

The antibody's compatibility with ELISA, western blotting, immunofluorescence, and flow cytometry makes it well-suited for researchers investigating lipid signaling cascades, inflammatory responses, or protein homeostasis mechanisms where PLAA function may be implicated.