Proteins & Peptides

MDM2 is a nuclear phosphoprotein that binds and inhibits transactivation by p53, as part of an autoregulatory negative feedback loop (1). Overexpression of the MDM2 gene product can lead to excessive inactivation of p53 thereby diminishing its tumor suppressor function. The inactivation of p53 is mediated by the E3 ubiquitin ligase activity of MDM2 which targets p53 for proteasomal degradation. MDM2 also affects the cell cycle, apoptosis, and tumorigenesis through interactions with other proteins, including retinoblastoma 1 and ribosomal protein L5 (2). Amplification of MDM2 is frequently observed in human sarcomas and this is consistent with the hypothesis that MDM2 binds to p53 which then leads to escape from p53-regulated growth control. MDM2 Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, Cell Cycle, and Cellular Stress research.

MDM2 is a nuclear phosphoprotein that binds and inhibits transactivation by p53, as part of an autoregulatory negative feedback loop (1). Overexpression of the MDM2 gene product can lead to excessive inactivation of p53 thereby diminishing its tumor suppressor function. The inactivation of p53 is mediated by the E3 ubiquitin ligase activity of MDM2 which targets p53 for proteasomal degradation. MDM2 also affects the cell cycle, apoptosis, and tumorigenesis through interactions with other proteins, including retinoblastoma 1 and ribosomal protein L5 (2). Amplification of MDM2 is frequently observed in human sarcomas and this is consistent with the hypothesis that MDM2 binds to p53 which then leads to escape from p53-regulated growth control. MDM2 Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, Cell Cycle, and Cellular Stress research.

MDM2 is a nuclear phosphoprotein that binds and inhibits transactivation by p53, as part of an autoregulatory negative feedback loop (1). Overexpression of the MDM2 gene product can lead to excessive inactivation of p53 thereby diminishing its tumor suppressor function. The inactivation of p53 is mediated by the E3 ubiquitin ligase activity of MDM2 which targets p53 for proteasomal degradation. MDM2 also affects the cell cycle, apoptosis, and tumorigenesis through interactions with other proteins, including retinoblastoma 1 and ribosomal protein L5 (2). Amplification of MDM2 is frequently observed in human sarcomas and this is consistent with the hypothesis that MDM2 binds to p53 which then leads to escape from p53-regulated growth control. MDM2 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.

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.

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.

MGRN1 or mahogunin ring finger 1, E3 ubiquitin protein ligase is a C3HC4 RING-containing protein with E3 ubiquitin ligase activity in vitro (1). MGRN1 gene encodes 4 mRNA isoforms that contain a central C3HC4 RING domain as the only recognizable protein motif and regions flanking the RING domain and the N-terminal region of the protein are also conserved between vertebrate and invertebrate genome and MGRN1 is highly expressed in brain (2). MGRN1 has been detected in the adrenal cortex in kidney and its role may relate to the trafficking and/or degradation of the melanocortin 2 receptor. MGRN1 Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Angiogenesis, Apoptosis/Autophagy, Cancer, Cell Cycle, Cellular Stress, Inflammation, Invasion/Metastasis, and Neurobiology research.

MGRN1 or mahogunin ring finger 1, E3 ubiquitin protein ligase is a C3HC4 RING-containing protein with E3 ubiquitin ligase activity in vitro (1). MGRN1 gene encodes 4 mRNA isoforms that contain a central C3HC4 RING domain as the only recognizable protein motif and regions flanking the RING domain and the N-terminal region of the protein are also conserved between vertebrate and invertebrate genome and MGRN1 is highly expressed in brain (2). MGRN1 has been detected in the adrenal cortex in kidney and its role may relate to the trafficking and/or degradation of the melanocortin 2 receptor. MGRN1 Protein is ideal for investigators involved in Signaling Proteins, Ubiquitin Proteins, Angiogenesis, Apoptosis/Autophagy, Cancer, Cell Cycle, Cellular Stress, Inflammation, Invasion/Metastasis, and Neurobiology research.