BEGAIN Antibodies

Background

The BEGAIN gene encodes a postsynaptic protein that is highly expressed in the brain, especially in the hippocampus and olfactory bulb, and its protein products are involved in regulating neuronal signal transduction and synaptic plasticity. This protein plays a significant role in the formation of learning and memory by influencing the function of glutamatergic synapses and is associated with the underlying mechanisms of neural development and certain neurological diseases. Since its first identification in 1996, BEGAIN has become one of the important molecular models for studying neural cell signaling networks and complex brain functions due to its key role in neural circuit specificity and cognitive function, providing continuous research value for understanding the development and functional mechanisms of the nervous system.

Structure Function Application Advantage Our Products

Structure of BEGAIN

BEGAIN is a postsynaptic protein with a molecular weight of approximately 50 kDa. This weight may vary slightly among different species.

Species	Human	Mouse	Rat
Molecular Weight (kDa)	~50	~50	~50
Primary Structural Differences	Contains multiple PDZ domains that mediate protein interaction	Highly conserved sequence	The structural function is highly homologous to human

This protein is composed of approximately 440 amino acids. Its structure includes the N-terminal PDZ domain and the C-terminal region rich in proline, which together form its functional modules. Its three-dimensional structure enables it to act as a scaffold protein and specifically bind to various signaling molecules (such as GluA1 subunits and PICK1) in the postsynaptic dense region (PSD) of neurons, thereby regulating the transport of AMPA receptors and synaptic plasticity. Its expression is brain region-specific and is particularly abundant in the hippocampus and olfactory bulb.

Fig. 1 Schematic of the BEGAIN Gene and iCre-3xVenus Knock-in Construct.¹

Key structural properties of BEGAIN:

Contains the N-terminal PDZ domain, which serves as the core protein interaction module
Has the c-terminal region rich in proline, mediating specific molecular recognition
Overall conformational allow it as postsynaptic scaffolding protein, integration of a variety of signal molecules

Functions of BEGAIN

The main function of the BEGAIN gene-encoded protein is to act as a scaffold in the synaptic of neurons and regulate signal transduction. Its specific functions are as follows:

Function	Description
Synaptic scaffold	As the core scaffold protein of the postsynaptic dense region (PSD), it integrates and anchors multiple signaling molecules to maintain the stability of synaptic structure.
Regulation of AMPA receptors	By binding to the AMPA receptor subunit (such as GluA1) through its PDZ domain, it regulates the transport, endocytosis and membrane localization of the receptor on the synaptic membrane, thereby directly affecting synaptic strength.
Regulation of synaptic plasticity	Participating in synaptic plasticity processes such as long-term enhancement (LTP) and long-term inhibition (LTD) is crucial for the formation of learning and memory.
Neuron development support	During the development of the nervous system, it affects the formation, maturation and specific connection of synapses, especially playing a significant role in the olfactory bulb and the hippocampus.
Signal path integration	With PICK1, GRIP, such as protein interactions, connected to the cell surface receptors and intracellular signaling network, coordination of postsynaptic signaling precise space-time dynamic.

Unlike some widely expressed scaffold proteins, the expression of BEGAIN is highly specific to brain regions, suggesting that it plays a fine regulatory role in information processing and storage in specific neural circuits.

Applications of BEGAIN and BEGAIN Antibody in Literature

Wang, Xinyue, et al. "A novel rabbit anti-myoglobin monoclonal antibody's potential application in rhabdomyolysis associated acute kidney injury." International Journal of Molecular Sciences 24.9 (2023): 7822. https://doi.org/10.18632/aging.205275

Studies have shown that the increase in father's age can reduce the methylation level of the BEGAIN gene in sperm and the umbilical cord blood of male offspring, and this phenomenon is associated with the risk of autism spectrum disorder in men, suggesting that it may mediate the influence of father's age on the neurodevelopment of offspring.

Dastsooz, Hassan, et al. "Involvement of N4BP2L1, PLEKHA4, and BEGAIN genes in breast cancer and muscle cell development." Frontiers in Cell and Developmental Biology 12 (2024): 1295403. https://doi.org/10.3389/fcell.2024.1295403

Research has found that the N4BP2L1, PLEKHA4 and BEGAIN genes are highly expressed in normal breast myoepithelial cells, but significantly down-regulated in breast cancer tissues. Low expression is associated with a higher risk in specific patient groups, suggesting that they may have tumor suppressor effects.

Katano, Tayo, et al. "Brain-enriched guanylate kinase-associated protein, a component of the post-synaptic density protein complexes, contributes to learning and memory." Scientific reports 13.1 (2023): 22027. https://doi.org/10.1038/s41598-023-49537-9

Research has found that BEGAIN protein is enriched in the dense postsynaptic region of the hippocampus and is related to learning and memory functions. Gene knockout mice showed significant impairment in behavioral tests such as spatial reference memory and fear conditioning, confirming their key role in excitatory synapses.

Katano, Tayo, et al. "Involvement of brain-enriched guanylate kinase-associated protein (BEGAIN) in chronic pain after peripheral nerve injury." eneuro 3.5 (2016). https://doi.org/10.1523/ENEURO.0110-16.2016

Research has found that the BEGAIN protein is a key molecule in maintaining neuropathic pain. It is located at the spinal dorsal horn synapse, and its expression is regulated by tyrosine phosphorylation of the GluN2B subunit. Its absence can alleviate abnormal pain but does not affect the normal pain threshold.

Yao, Ikuko, et al. "Synaptic and nuclear localization of brain-enriched guanylate kinase-associated protein." Journal of Neuroscience 22.13 (2002): 5354-5364. https://doi.org/10.1523/JNEUROSCI.22-13-05354.2002

Research has found that the BEGAIN protein has both nuclear localization and synaptic targeting functions in neurons. It is located at the synapse through N-terminal region-dependent PSD-95/SAP90 and NMDA receptor activity and participates in postsynaptic signal regulation.

Creative Biolabs: BEGAIN Antibodies for Research

Creative Biolabs specializes in the production of high-quality BEGAIN antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom BEGAIN Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our BEGAIN antibodies, custom preparations, or technical support, contact us at email.

Reference

Katano, Tayo, et al. "Brain-enriched guanylate kinase-associated protein, a component of the post-synaptic density protein complexes, contributes to learning and memory." Scientific reports 13.1 (2023): 22027. https://doi.org/10.1038/s41598-023-49537-9