SNAP91. also known as clathrin assembly lymphoid myeloid leukemia protein (CALM) or PICALM, is a ubiquitously expressed protein involved in clathrin-mediated endocytosis (CME), a critical process for membrane trafficking and synaptic vesicle recycling. It plays a key role in shaping clathrin-coated pits by interacting with clathrin, AP2 adaptors, and other endocytic machinery components. In neurons, SNAP91 is particularly important for maintaining synaptic vesicle pools and regulating neurotransmitter release, linking it to synaptic plasticity and neuronal communication.
Antibodies targeting SNAP91 are essential tools for investigating its expression, localization, and function in diverse biological contexts. They are widely used in techniques like Western blotting, immunohistochemistry, and immunofluorescence to study SNAP91's role in cellular processes such as receptor internalization, intracellular signaling, and synaptic transmission. Researchers also utilize these antibodies to explore pathological mechanisms in neurodegenerative diseases (e.g., Alzheimer's and Parkinson's), where disrupted endocytosis is implicated, as well as in cancer studies, given SNAP91's association with leukemias through chromosomal translocations.
Additionally, SNAP91 antibodies help validate genetic models (e.g., knockout mice) and assess protein interactions via co-immunoprecipitation. Their specificity and reliability are critical for advancing our understanding of CME-related disorders and developing targeted therapeutic strategies.