Description
Key facts
Species or organism:Human,
Form:LiquidSee storage information
Product details:
ab94170 is a 293T cell transfected lysate in which Human MTMR1 has been transiently over-expressed using a pCMV-MTMR1 plasmid. The lysate is provided in 1X Sample Buffer.
Properties and Storage Information:
Shipped at conditions-Dry Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Aliquoting information-Upon delivery aliquot, Storage information-Avoid freeze / thaw cycle
Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
MTMR1 also known as Myotubularin-related protein 1 belongs to the myotubularin family of phosphatidylinositol (PI) phosphatases. It plays a role in regulating phosphoinositide levels. The protein has a molecular mass of approximately 72 kDa. Scientists have found its expression in various tissues including skeletal muscle and the nervous system. MTMR1 is important for cellular homeostasis by modulating lipid signaling pathways.
Biological function summary
The protein functions as a phosphatase that removes phosphate groups from phosphatidylinositol 3-phosphate and phosphatidylinositol 35-bisphosphate. It does not work alone but as part of complexes that include other proteins from the same family. This collaboration allows for regulating PI levels which are involved in membrane trafficking and signal transduction. Its activity impacts cellular processes like endocytosis and autophagy which are important for cell maintenance and survival.
Pathways
MTMR1 is involved in pathways that include lipid signaling and autophagy. It particularly affects the PI3K-Akt signaling pathway which is important for controlling cell growth and apoptosis. MTMR1 can interact with other members of the myotubularin family like MTMR2 to execute its functions in these pathways. The interconnected work of these proteins ensures the correct functioning of signal transduction and cellular homeostasis.
MTMR1 has connections with muscular and neurological diseases. Particularly its dysfunction has been noted in types of muscular dystrophy. Researchers have linked its activity with proteins such as MTMR13 showing combined roles in disease mechanisms especially those affecting muscle tissue. Studies continue to explore these associations to understand better and manage related disorders.
