Other Proteins

MDM4 is a nuclear protein that contains a p53 binding domain at the N-terminus and a RING finger domain at the C-terminus. MDM4 shows structural similarity to p53-binding protein MDM2 and both proteins bind the p53 tumor suppressor protein and inhibit its activity. However, unlike MDM2, MDM4 does not cause nuclear export or degradation of p53. Instead, MDM4 inhibits p53 activity by binding to the transcriptional activation domain of p53. MDM4 is overexpressed in a variety of human cancers (1). Expression level of MDM4 is significantly higher in chronic lymphocytic leukemia. MDM4 is a specific chemotherapeutic target for treating retinoblastoma (2). MDM4 Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, Cell Cycle, and Cellular Stress research.

MDM4 is a nuclear protein that contains a p53 binding domain at the N-terminus and a RING finger domain at the C-terminus. MDM4 shows structural similarity to p53-binding protein MDM2 and both proteins bind the p53 tumor suppressor protein and inhibit its activity. However, unlike MDM2, MDM4 does not cause nuclear export or degradation of p53. Instead, MDM4 inhibits p53 activity by binding to the transcriptional activation domain of p53. MDM4 is overexpressed in a variety of human cancers (1). Expression level of MDM4 is significantly higher in chronic lymphocytic leukemia. MDM4 is a specific chemotherapeutic target for treating retinoblastoma (2). MDM4 Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, Cell Cycle, and Cellular Stress research.

MGMT or O-6-methylguanine-DNA methyltransferase is the major mutagenic and carcinogenic lesion in DNA induced by simple alkylating mutagens. The methylation of the MGMT promoter in gliomas is a useful predictor of the responsiveness of the tumors to alkylating agents (1). The clinical trial substantiates the predictive value of O-6-methylguanine-DNA methyltransferase promoter methylation in glioblastoma patients treated with temozolomide (2). Methylation of the MGMT promoter in tumors is associated with longer survival in glioblastoma patients. MGMT Protein is ideal for investigators involved in Signaling Proteins, Acetyl/Methyltransferase Proteins, Apoptosis/Autophagy, Cancer, Cell Cycle, and Neurobiology 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.

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.

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.

NCK (or non-catalytic region of tyrosine kinase adaptor protein 1) is an adaptor protein that is located in the cytoplasm and involved in transducing signals from receptor tyrosine kinases to downstream signal recipients such as RAS (1). NCK is a signaling and transforming protein that contains Src homology 2 and 3 (SH2 and SH3) domains. NCK functions by coupling tyrosine phosphorylation via SH2 domains to downstream effectors through SH3 domains. Furthermore, NCK couples tyrosine phosphorylation guidance signals to cytoskeletal events required for the ipsilateral projections of spinal cord neurons and for normal limb movement (2). NCK Protein is ideal for investigators involved in Signaling Proteins, Adaptor Proteins, Angiogenesis, Cancer, Inflammation, and Invasion/Metastasis research.