Anti-Neuroligin 1 + Neuroligin 4 antibody [EPR13108] - BSA and Azide free

Supplementary info

This supplementary information is collated from multiple sources and compiled automatically.

Activity summary

Neuroligin 1 and Neuroligin 4 are cell adhesion proteins that play an important role in the development and function of synaptic connections in the nervous system. These proteins are part of the neuroligin family with Neuroligin 1 sometimes referred to as NLGN1 and Neuroligin 4 as NLGN4. Neuroligin 1 has a molecular mass of approximately 110 kDa while Neuroligin 4 has a mass of about 100 kDa. These proteins are primarily expressed in neurons where they contribute to the formation and maintenance of synaptic junctions between neurons.

Biological function summary

Neuroligin 1 and Neuroligin 4 facilitate the formation and maturation of excitatory and inhibitory synapses in the brain. These proteins work as part of a complex with their binding partners neurexins which reside on the presynaptic membrane to bridge the synaptic cleft. This interaction helps stabilize synaptic contacts and promotes the balance of synaptic transmission. Their role in synaptic specialization highlights their significance in maintaining proper neuronal network communication.

Pathways

Neuroligin 1 and Neuroligin 4 are positioned within the synaptic signaling pathways notably in the involvement of synapse organization and plasticity. These pathways ensure that synaptic signals are correctly transmitted and received which is essential for learning and memory processes. Neuroligins interact closely with the SHANK proteins and PSD-95 which are important components of the postsynaptic density. This interaction contributes to the structural and functional integrity of synapses allowing for precise cellular communication.

Associated diseases and disorders

Mutations in Neuroligin 1 and Neuroligin 4 have been linked to neural developmental disorders including autism spectrum disorders and X-linked mental retardation. Aberrant neuroligin function affects synaptic stability and connectivity contributing to the pathophysiology of these conditions. Studies have identified interactions with proteins like neurexins and SHANK3 to be significant highlighting the complexity of neuronal circuitry affected in these disorders. Understanding this connection is key for exploring therapeutic strategies targeting synaptic dysfunction.