JMY (C-terminal region) polyclonal, anti-human, mouse, rat, chicken, frog

Background:
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.

Immunogen: JMY synthetic peptide (coupled to carrier protein) corresponds to amino acids in the C-terminal region of mouse JMY. This sequence is highly conserved in human, rat, frog, and zebrafish JMY proteins, and has low homology to other WASP family members.

Specificity: This antibody was affinity purified using JMY (C-terminal region) peptide (without carrier). 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.

Buffer/Storage:
Rabbit polyclonal, affinity-purified antibody is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.