BioLegend Synaptic Function
The neuron is a critical functional unit of the nervous system, which relays electrical and chemical signals to other neurons at junctions known as the neural synapse. The differentiated mammalian central nervous system is estimated to contain at least 100 billion neurons, which communicate with each other through numerous synaptic connections. The neural synapse most often occurs between the axon of one neuron and the dendrites of another and is composed of hundreds of proteins that function together to coordinate the exquisitely tuned signals that are the physical basis for higher nervous system functions, such as cognition, memory, and movement. BioLegend provides an extensive selection of antibodies and reagents for the analysis of synaptic function.
Neurodegeneration   Adhesion Molecules   Receptors   Vesicular Trafficking   Products
Many distinct types of electrical synapses exist that relay hundreds of known chemical signals, termed neurotransmitters, from one neuron to another, or form a direct contact. Synapses can weaken or strengthen in response to a number of factors, a phenomenon which is termed neural plasticity. Neurodegenerative diseases, such as Alzheimer's and Parkinson's, display a loss of synaptic function and a subsequent degradation of these structures. This degeneration occurs more prominently at particular locations in the central nervous system, such as the substantia nigra for Parkinson's disease, which is highly enriched in synapses that transmit the neurotransmitter dopamine. With the support of BioLegend reagents, investigations into the mechanisms that lead to dysfunction and synaptic loss, may provide new avenues for preventative and therapeutic intervention.
Purified anti-MAGUK (pan reactive) (clone K28/86)
Membrane-associated guanylate kinases (MAGUK) are a superfamily of scaffolding proteins defined by the presence of a guanylate kinase (GUK) domain. MAGUKs, such as PSD-95, SAP97, PSD-83, CASK, and MAGIs are involved in the synaptic development and function where they are important for the spatial organization of both pre- and postsynaptic proteins, including glutamate and other receptors.
Staining of Clone K28/86 on formalin-fixed paraffin-embedded rat hippocampus at 1 µg/mL.

Purified anti-Ankyrin-B (clone N105/13)
Ankyrins are adaptor proteins that mediate the attachment of membrane proteins to the cytoskeleton. Ankyrin-B (Ankyrin-2) is highly expressed in cardiac tissue where it has an essential role in stabilizing ion transporters and channels in cardiomyocytes in the membrane. Mutations in ankyrin-B are associated with cardiac arrhythmia and ankyrin-B may be involved in human heart failure.
Staining of Clone N105/13 on formalin-fixed paraffin-embedded rat brain tissue.

Purified anti-PSD95 (clone K28/43)
PSD95, also known as SAP-90, is a member of the MAGUK family, encoded by the the DLG4 gene. At postsynaptic sites, it mediates the scaffolding of NMDA receptors, AMPA receptors, potassium channels, and other associated signaling protein clusters. It plays an important role in synaptic plasticity and the stabilization of synaptic changes during long-term potentiation.
Staining of PSD-95 (K28/43) on formalin-fixed paraffin-embedded rat brain.

Purified anti-Neuroligin-1 (clone N97A/31)
Neuroligin is a postsynaptic membrane protein that binds to Neurexin, helping to form and maintain neuronal synapses. Within the postsynaptic neuron, it binds to proteins such as PSD-95, which recruits receptors and channels to the synapse.
Staining of Clone N97A/31 on formalin-fixed paraffin-embedded rat brain tissue.

Purified anti-Synaptotagmin-12 (clone N277/7)
Synaptotagmin 12 (Syt12) is regulated by protein kinase A (PKA) and is unique from other synaptotagmins in that it does not bind to Ca2+. Syt12 interaction with Syt1 prevents SNARE complex binding. Expression of Syt12 induces spontaneous neurotransmitter release, providing a mechanism for spontaneous synaptic-vesicle exocytosis that is Ca2+-independent.
Staining of Synaptotagmin-12 on formalin-fixed paraffin-embedded rat brain tissue.

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