Proteins & Peptides

MO25α (mouse protein 25 alpha) is a 40-kDa protein that interacts with the STE20-related adaptor-alpha (STRADα) pseudo kinase to form a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase (1). LKB1 plays a critical role in cell proliferation, polarity and energy metabolism. LKB1 is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). MO25α binds directly to a conserved Trp-Glu-Phe sequence at the STRADα C terminus, and markedly enhances the binding of STRADα to LKB1 thereby increasing LKB1 catalytic activity (2). MO25α Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cardiovascular Disease, and Metabolic Disorder research.

MO25α (mouse protein 25 alpha) is a 40-kDa protein that interacts with the STE20-related adaptor-alpha (STRADα) pseudo kinase to form a regulatory complex capable of stimulating the activity of the LKB1 tumor suppressor protein kinase (1). LKB1 plays a critical role in cell proliferation, polarity and energy metabolism. LKB1 is mutated in the inherited Peutz-Jeghers cancer syndrome (PJS). MO25α binds directly to a conserved Trp-Glu-Phe sequence at the STRADα C terminus, and markedly enhances the binding of STRADα to LKB1 thereby increasing LKB1 catalytic activity (2). MO25α Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cardiovascular Disease, and Metabolic Disorder research.

Moesin (or membrane-organizing extension spike protein) belongs to ERM family that modulates epithelial integrity by regulating cell-signalling events that affect actin organization and polarity (1). The effects of Moesin on epithelial cells appear to result from inhibition of Rho signaling. ERM proteins serve a structural role in linkage of the cytoskeleton to the plasma membrane and the rescue of cells lacking Moesin by modulation of Rho signaling indicates that inhibition of Rho activity may be a more critical function of Moesin. The negative feedback loop produced by Rho's activation of ERM may be an important mechanism that prevents the excessive migratory and invasive properties characteristic of metastatic cancer cells (2). Moesin Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, Inflammation, and PKA/PKC Pathway research.

Moesin (or membrane-organizing extension spike protein) belongs to ERM family that modulates epithelial integrity by regulating cell-signalling events that affect actin organization and polarity (1). The effects of Moesin on epithelial cells appear to result from inhibition of Rho signaling. ERM proteins serve a structural role in linkage of the cytoskeleton to the plasma membrane and the rescue of cells lacking Moesin by modulation of Rho signaling indicates that inhibition of Rho activity may be a more critical function of Moesin. The negative feedback loop produced by Rho's activation of ERM may be an important mechanism that prevents the excessive migratory and invasive properties characteristic of metastatic cancer cells (2). Moesin Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, Inflammation, and PKA/PKC Pathway research.

Mortalin is a mitochondrial chaperone and a member of the heat shock protein 70 family that is constitutively expressed in cells. Mortalin plays a central role in mitochondrial biogenesis through its capacity to direct the import of nuclear-encoded proteins into the mitochondria. Mortalin plays a role in the control of cell proliferation and elevated levels of mortalin have correlated with malignant transformation and poor cancer prognosis. Mortalin can support cancer cell resistance to complement-dependent cytotoxicity (1). Mortalin expression was decreased in the mitochondrial fraction of neurons from the substantia nigra of Parkinson disease patients (2). Mortalin Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, Apoptosis/Autophagy, and Cancer research.

Mortalin is a mitochondrial chaperone and a member of the heat shock protein 70 family that is constitutively expressed in cells. Mortalin plays a central role in mitochondrial biogenesis through its capacity to direct the import of nuclear-encoded proteins into the mitochondria. Mortalin plays a role in the control of cell proliferation and elevated levels of mortalin have correlated with malignant transformation and poor cancer prognosis. Mortalin can support cancer cell resistance to complement-dependent cytotoxicity (1). Mortalin expression was decreased in the mitochondrial fraction of neurons from the substantia nigra of Parkinson disease patients (2). Mortalin Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, Apoptosis/Autophagy, and Cancer research.

MOS or v-mos Moloney murine sarcoma viral oncogene homolog is a serine/threonine kinase that activate the MAP kinase cascade through direct phosphorylation of the MAP kinase activator MEK (1). The early site-specific phosphorylation of CPEB , which was catalyzed by Eg2 is essential for the polyadenylation of c-mos mRNA, subsequent translation of c-mos, and oocyte maturation (2). The interaction with and phosphorylation of MYOD by MOS enhances muscle differentiation. MOS is an essential component of the cytostatic factor that acts almost exclusively in the second meiotic metaphase arrest. MOS Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cell Cycle, and Ser/Thr Kinases research.

MOS or v-mos Moloney murine sarcoma viral oncogene homolog is a serine/threonine kinase that activate the MAP kinase cascade through direct phosphorylation of the MAP kinase activator MEK (1). The early site-specific phosphorylation of CPEB , which was catalyzed by Eg2 is essential for the polyadenylation of c-mos mRNA, subsequent translation of c-mos, and oocyte maturation (2). The interaction with and phosphorylation of MYOD by MOS enhances muscle differentiation. MOS is an essential component of the cytostatic factor that acts almost exclusively in the second meiotic metaphase arrest. MOS Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cell Cycle, and Ser/Thr Kinases research.

N6AMT2 is a putative DNA methyltransferase, belongs to the methyltransferase superfamily, AML1 family. The N6AMT2 gene is conserved in human, mouse, rat, chimpanzee, dog, cow, chicken, zebrafish, fruit fly, mosquito, C.elegans, S.cerevisiae, K.lactis, N.crassa, A.thaliana, and rice (1). The N6AMT2 phosphorylation at Ser-2 has been reported (2). The function of this protein has not been widely studied yet. N6AMT2 Protein is ideal to investigators involved in Signaling Proteins, Acetyl/Methyltransferase Proteins, Apoptosis/Autophagy, Cancer, Cell Cycle, and Neurobiology research.