JMY (C-terminal region) Antibody

JMY (junction mediating and regulatory protein) is a transcription co-factor, originally identified as a p300-binding protein involved in p53-dependent transcription. Upon DNA damage, JMY is released from Mdm2 inhibition and forms a complex with Strap and p300. This complex recruits PRMT5 to activate the p53 response. Through regulation of p53-dependent transcription, JMY has important roles in the DNA damage response. In addition, JMY contains three carboxyl-terminal WH2 actin binding domains which are are commonly found in WASP family proteins. JMY can bind to actin and to the Arp2/3 complex, as well as direct the assembly of actin filaments in vitro. These actin-regulating effects of JMY may have important roles in cell migration. When slow migrating HL-60 cells are differentiated into highly motile neutrophil-like cells, JMY moves from the nucleus to the cytoplasm and is concentrated at the actin-rich leading edge of cells. The loss of JMY leads to decreased cell migration in HL-60 cells. Thus, JMY represents a new class of multifunctional actin assembly factors whose activity may be regulated by cellular localization.

The antibody detects a 130 kDa* protein corresponding to the molecular mass of JMY on SDS-PAGE immunoblots of human HeLa, Jurkat cells, rat PC12 cells, and mouse brain and heart. This sequence is highly conserved in human, rat, frog, and zebrafish JMY proteins, and has low homology to other WASP family members.