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BEND5 ELISA Kits

The BEN domain (BEND) is an ~90-amino-acid _-helical module conserved in diverse polydnavirus and cellular metazoan proteins. A family of �BEN-solo� factors is characterized by the presence of BEND as a single conserved module of the proteins. Based on contextual conservation of BEND-containing proteins, it was predicted that they function as DNA-binding factors or adaptor molecules that recruit chromatin-modifying complexes. Drosophila BEN solo protein Insv promotes peripheral nervous system development, acts as a nuclear corepressor for Su(H), a Notch transcription factor, and is recruited to chromatin via binding to the CSL-type transcription factor, a primary effector of Notch signaling. Mammalian proteins BEND5 and BEND6 are highly homologous to Insv. Murine BEND5 is strongly expressed in the brain cortex, and human BEND5 can substitute for Insv in transient transfection assays.

The highly malignant primitive neuroectodermal tumors of the CNS (CNS-PNETs) have been challenging to distinguish from other forms of brain tumors but the molecular profiling now helps with the classification of these cancers. A study identified interchromosomal gene fusions between meningioma (disrupted in balanced translocation) 1 (MN1, 22q12.3) and BEN domain containing 2 (BEND2, Xp22.13) in three samples, and MN1 and CXXC-type zinc-finger protein 5 (CXXC5, 5q31.2) in one sample from RNA sequencing data of four tumors. High-level gene expression of the fusion partner BEND2 was observed specifically in CNS HGNET-MN1 tumors, while being absent in other CNS tumor types. Fused to BEND2, the encoded chimeric protein combines the transactivating domains of MN1 and the two BEN domains in the C terminus of BEND2, which have been suggested to mediate protein-DNA and protein-protein interactions during chromatin organization and transcription.

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