|Other Names||Pikachurin, Agrin-like protein, EGF-like, fibronectin type-III and laminin G-like domain-containing protein, EGFLAM, AGRINL, AGRNL|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Involved in both the retinal photoreceptor ribbon synapse formation and physiological functions of visual perception. Necessary for proper bipolar dendritic tip apposition to the photoreceptor ribbon synapse. Promotes matrix assembly and cell adhesiveness (By similarity).|
|Cellular Location||Secreted, extracellular space, extracellular matrix. Cell junction, synapse Note=Detected in the synaptic cleft of the ribbon synapse around the postsynaptic terminals of bipolar cells. Colocalizes with BSN, CTBP2 and DAG1 in photoreceptor synaptic terminals (By similarity).|
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EFNB3, a member of the ephrin gene family, is important in brain development as well as in its maintenance. Moreover, since levels of EFNB3 expression were particularly high in several forebrain subregions compared to other brain subregions, it may play a pivotal role in forebrain function. The EPH and EPH-related receptors comprise the largest subfamily of receptor protein-tyrosine kinases and have been implicated in mediating developmental events, particularly in the nervous system. EPH Receptors typically have a single kinase domain and an extracellular region containing a Cys-rich domain and 2 fibronectin type III repeats. The ephrin ligands and receptors have been named by the Eph Nomenclature Committee (1997). Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins.
Guey, L.T., et al. Eur. Urol. 57(2):283-292(2010) Sokolowski, M., et al. Mol. Psychiatry 15(1):10-11(2010) Shen, M., et al. Environ. Mol. Mutagen. 50(4):285-290(2009) Hosgood, H.D. III, et al. Carcinogenesis 29(10):1938-1943(2008) Xu, K., et al. Proc. Natl. Acad. Sci. U.S.A. 105(29):9953-9958(2008)
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