**Background of MYLK Antibodies**
MYLK (myosin light-chain kinase) is a calcium/calmodulin-dependent enzyme that phosphorylates the regulatory light chain of myosin, triggering smooth muscle contraction and modulating cytoskeletal reorganization in non-muscle cells. The MYLK gene encodes multiple isoforms, including the long (MYLK1) and short (MYLK2) forms, which exhibit tissue-specific expression. MYLK1 is predominantly expressed in smooth muscle and endothelial cells, playing a critical role in vascular tone regulation, while MYLK2 is associated with cardiac and skeletal muscle function.
MYLK dysregulation has been implicated in cardiovascular diseases (e.g., hypertension, aortic aneurysm), inflammatory conditions, and cancer metastasis. Antibodies targeting MYLK are essential tools for studying its expression, localization, and activity in these contexts. They enable detection of MYLK isoforms via techniques like Western blotting, immunohistochemistry, and immunofluorescence. Specific antibodies may distinguish phosphorylated (active) or total MYLK, aiding in research on signaling pathways involving Rho-associated kinase (ROCK) or calcium-dependent contraction mechanisms.
Recent studies also explore MYLK's role in endothelial barrier dysfunction and tumor cell migration, highlighting its potential as a therapeutic target. Commercial MYLK antibodies are typically validated in human, mouse, or rat models, with applications spanning basic research and clinical diagnostics. However, isoform specificity and cross-reactivity remain key considerations during experimental design.