BAK1 (BRI1-Associated Receptor Kinase 1), also known as SERK3 (Somatic Embryogenesis Receptor Kinase 3), is a leucine-rich repeat receptor-like kinase (LRR-RLK) that functions as a critical co-receptor in plant signaling pathways. Initially identified for its role in brassinosteroid (BR) signaling through interaction with the BR receptor BRI1. BAK1 is now recognized as a multifunctional regulator in plant innate immunity and development. It forms ligand-induced complexes with pattern recognition receptors (PRRs) like FLS2 and EFR, mediating responses to pathogen-associated molecular patterns (PAMPs) such as flagellin and EF-Tu, thereby activating PAMP-triggered immunity (PTI).
BAK1 antibodies are essential tools for studying its protein expression, localization, and interaction dynamics. They are widely used in techniques like Western blotting, immunoprecipitation, and immunofluorescence to investigate BAK1's involvement in immune signaling cascades, cell death regulation, and stress responses. These antibodies are typically raised against specific epitopes of BAK1. often in rabbits or mice, and require rigorous validation for specificity due to high homology with other SERK family members. Researchers rely on BAK1 antibodies to explore its phosphorylation status, subcellular distribution, and tissue-specific expression under various biotic/abiotic stresses. Their applications extend to genetic studies, including mutant phenotyping and transgenic plant analysis, providing insights into BAK1's dual roles in growth-defense trade-offs. Proper controls, such as using bak1 mutant lines, are critical to avoid cross-reactivity artifacts.