protein

Gliomedin Protein, Human (HEK293, N-hFc)

HY-P76363A

5 μg;10 μg;50 μg;100 μg

65;110;300;510 USD

Gliomedin Protein, Human (HEK293, N-hFc)

proteins

HEK293

5 μg;10 μg;50 μg;100 μg

65;110;300;510 USD

Gliomedin protein is a collagen-rich homotrimer that critically binds to NRCAM and NFASC and plays a key role in establishing and preserving nodes of Ranvier on myelinated axons. It mediates Schwann cell-axon interactions and promotes sodium channel clustering for efficient action potential propagation. Gliomedin Protein, Human (HEK293, N-hFc) is the recombinant human-derived Gliomedin protein, expressed by HEK293 , with N-hFc labeled tag. The total length of Gliomedin Protein, Human (HEK293, N-hFc) is 427 a.a., with molecular weight of 95-112 kDa.

Human

Gliomedin, a homotrimeric protein characterized by collagen-like domains, acts as a crucial ligand for NRCAM and NFASC/neurofascin, playing a pivotal role in the establishment and preservation of nodes of Ranvier along myelinated axons. Its significance lies in mediating the interaction between Schwann cell microvilli and axons through binding to NRCAM and NFASC. Nodes of Ranvier are essential regions on myelinated axons housing clustered sodium channels vital for the saltatory propagation of action potentials. Gliomedin is specifically involved in the formation of nodes during development by facilitating the fusion of heminodes, and it is indispensable for the proper clustering of sodium channels at heminodes. Additionally, in collaboration with NRCAM, Gliomedin contributes to the maintenance of NFASC and sodium channel clusters at fully mature nodes of Ranvier. Furthermore, its interaction with glial NRCAM enhances its binding affinity with axonal NFASC. Gliomedin's intricate involvement underscores its significance in the structural integrity and functional organization of nodes of Ranvier.

Gliomedin; GLDN; COLM

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm filtered solution of PBS, pH 7.4.

Room temperature in continental US; may vary elsewhere.