Demyelinating Disease Targets Antibody Sampler Kit#42135,Cell Signaling Technology (CST),42135

Reactivity

0

Platform ID

BAB973534532

Cell Signaling Technology (CST)

Headquarters

3 Trask Lane Danvers, MA 01923

Contact

Tel: 877-616-2355,978-867-2388
Fax: 877-616-2355

Product Specifications
Scientific Background

Specifications

NameDemyelinating Disease Targets Antibody Sampler Kit#42135
Cat. No.42135
Accession NumberQ13509, P02686, Q9UHC6, P78357, O94856, Q16653, P60201, P20916
Gene ID (Entrez)13509, 02686, 78357, 94856, 16653, 60201, 20916, 10381, 4155, 26047, 8506, 23114, 4340, 5354, 4099
Reactivity0
Regulatory StatusResearch Use Only

Scientific Background

Myelin is the insulating material surrounding neuronal axons. The function of myelin is to promote action potential propagation down the axon to the axon terminal. Myelin is formed in the central nervous system (CNS) by specialized glial cells called oligodendrocytes and by Schwann cells in the peripheral nervous system (PNS). Oligodendrocytes and Schwann cells make concentric rings, called the myelin sheath, around the axon at regular intervals. These intervals, called nodes of ranvier, are enriched in structural proteins and ion channels, which help promote action potential propagation. Several proteins are enriched in the myelin sheath and likely help mediate the tight multi-layered membranes that make up the sheath. These proteins include myelin basic protein (MBP, [1]), myelin-associated glycoprotein (MAG, [2]), myelin proteolipid protein (PLP1, [3]) and  myelin-oligodendrocyte glycoprotein (MOG, [4]). Contactin-associated protein (Caspr) 1 & 2 (5,6) and neurofascin 155 & 186 (7,8) are nodes of ranvier-associated proteins that may play roles in generating the regular intervals of myelin along the axon. Expression of several of these proteins are altered in demyelinating diseases such as multiple sclerosis (MS). Additionally, mislocalization and/or altered expression of these proteins, compared to the axonal protein Î23-tubulin, may represent altered myelin function.ÂHarauz, G. and Boggs, J.M. (2013)J Neurochem125, 334-61.Li, M. et al. (1996)J Neurosci Res46, 404-14.Thomson, C.E. et al.Dev Neurosci27, 27-36.Johns, T.G. and Bernard, C.C. (1999)J Neurochem72, 1-9.Rios, J.C. et al. (2000)J Neurosci20, 8354-64.Einheber, S. et al. (1997)J Cell Biol139, 1495-506.Charles, P. et al. (2002)Curr Biol12, 217-20.Thaxton, C. et al. (2011)Neuron69, 244-57.

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