The myotubularin (MTM) family constitutes one of the largest and most highly conserved protein-tyrosine phosphatase (PTP) subfamilies. Myotubularins, contain the consensus active site of tyrosine phosphatases but otherwise shows no homology to other phosphatases. PTP′s usually act on substrates containing only phosphotyrosine sites, but myotubularins were shown to act on both phosphotyrosine and phosphoserine (dual specific). The enzymatic activity of myotubularins had not been demonstrated previously because it lacks catalytically active residues in tyrosine phosphatase/dual-specific phosphatase active site. The active site is however sufficiently preserved to bind phosphorylated substrates, and may protect from phosphatases. It was reported that interaction of myotubularin family members makes one of them catalytically active. MTMR5 can interact with MTMR2 and regulates the enzymatic activity and the subcellular localization of MTMR2. MTMR5 inhibits myoblast differentiation in vitro and induces oncogenic transformation in fibroblasts.Other suggested roles for MTMR5 are in spermatogenesis and germ cell differentiation. Binding partners for MTMR5 include the SET domain of MLL/HRX and SUV39H1.
Immunogen
MTMR5 (1836-1871) This antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide selected from the C-terminal region of human MTMR5.
Physical form
Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide.
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