anti-Synaptophysin (human), Rabbit Monoclonal (RM258)

Synaptophysin (major synaptic vesicle protein p38) is a calcium-binding and integral membrane glycoprotein present in presynaptic vesicles in almost all neurons. Synaptophysin has four transmembrane domains and it forms a complex with dynamin at high calcium concentrations suggesting an involvement in synaptic vesicle endocytosis. It is also involved in the regulation of short-term and long-term synaptic plasticity. Synaptophysin is currently the most widely used marker for nerve terminals and for differentiating neuroendocrine tumors and its ubiquity at the synapse has led to the use of synaptophysin immunostaining for quantification of synapses. Mutations in the gene can result in mental retardation, increased exploratory behavior, impaired object novelty recognition and reduced spatial learning. Using immunohistochemistry, synaptophysin can be demonstrated in a range of neural and neuroendocrine tissues, including cells of the adrenal medulla and pancreatic islets. As a specific marker for these tissues, it can be used to identify tumours arising from them, such as neuroblastoma, retinoblastoma, phaeochromocytoma, carcinoid, small-cell carcinoma, medulloblastoma and medullary thyroid carcinoma.