Proteins & Peptides

14-3-3θ (also known as tyrosine 3-monooxygenase/ tryptophan 5-monooxygenase activation protein, theta polypeptide) is a member of the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. Through interaction with ASK1, c-jun NH-terminal kinase, and p38 mitogen-activated protein kinase (MAPK), 14-3-3θ plays an important role in controlling apoptosis (1). Induced expression of 14-3-3θ protein has been reported in patients with amyotrophic lateral sclerosis. Additionally, 14-3-3θ has been observed to mediate nucleocytoplasmic shuttling of the N protein (coronavirus nucleocapsid protein) which causes severe acute respiratory syndrome (2). 14-3-3θ Protein is ideal for investigators involved in Cell Stress& Chaperone Proteins, AKT/PKB Pathway, Cancer, Cell Cycle, Cellular Stress, ERK/MAPK Pathway, Neurobiology, PKA/PKC Pathway, and WNT Signaling research.

14-3-3θ (also known as tyrosine 3-monooxygenase/ tryptophan 5-monooxygenase activation protein, theta polypeptide) is a member of the 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins. Through interaction with ASK1, c-jun NH-terminal kinase, and p38 mitogen-activated protein kinase (MAPK), 14-3-3θ plays an important role in controlling apoptosis (1). Induced expression of 14-3-3θ protein has been reported in patients with amyotrophic lateral sclerosis. Additionally, 14-3-3θ has been observed to mediate nucleocytoplasmic shuttling of the N protein (coronavirus nucleocapsid protein) which causes severe acute respiratory syndrome (2). 14-3-3θ Protein is ideal for investigators involved in Cell Stress& Chaperone Proteins, AKT/PKB Pathway, Cancer, Cell Cycle, Cellular Stress, ERK/MAPK Pathway, Neurobiology, PKA/PKC Pathway, and WNT Signaling research.

14-3-3σ or stratifin is a protein that is strongly induced by gamma irradiation and other DNA-damaging agents (1). The induction of 14-3-3σ is mediated by a p53 responsive element. Exogenous introduction of 14-3-3σ into cycling cells results in a G2 cell cycle arrest (2). Knockout of 14-3-3σ in cells showed that the cells are unable to maintain cell cycle arrest after DNA damage. The 14-3-3σ -/- cells die as they enter mitosis. This process is associated with a failure of the 14-3-3σ -deficient cells to sequester the proteins that initiate mitosis and prevent them from entering the nucleus. Thus, 14-3-3σ plays an important role in maintaining the G2 checkpoint in cells and preventing mitotic death. 14-3-3σ Protein is ideal for investigators involved in Cell Stress& Chaperone Proteins, AKT/PKB Pathway, Cancer, Cell Cycle, Cellular Stress, ERK/MAPK Pathway, Neurobiology, PKA/PKC Pathway, and WNT Signaling research.

14-3-3σ or stratifin is a protein that is strongly induced by gamma irradiation and other DNA-damaging agents (1). The induction of 14-3-3σ is mediated by a p53 responsive element. Exogenous introduction of 14-3-3σ into cycling cells results in a G2 cell cycle arrest (2). Knockout of 14-3-3σ in cells showed that the cells are unable to maintain cell cycle arrest after DNA damage. The 14-3-3σ -/- cells die as they enter mitosis. This process is associated with a failure of the 14-3-3σ -deficient cells to sequester the proteins that initiate mitosis and prevent them from entering the nucleus. Thus, 14-3-3σ plays an important role in maintaining the G2 checkpoint in cells and preventing mitotic death. 14-3-3σ Protein is ideal for investigators involved in Cell Stress& Chaperone Proteins, AKT/PKB Pathway, Cancer, Cell Cycle, Cellular Stress, ERK/MAPK Pathway, Neurobiology, PKA/PKC Pathway, and WNT Signaling research.

14-3-3σ or stratifin is a protein that is strongly induced by gamma irradiation and other DNA-damaging agents (1). The induction of 14-3-3σ is mediated by a p53 responsive element. Exogenous introduction of 14-3-3σ into cycling cells results in a G2 cell cycle arrest (2). Knockout of 14-3-3σ in cells showed that the cells are unable to maintain cell cycle arrest after DNA damage. The 14-3-3σ -/- cells die as they enter mitosis. This process is associated with a failure of the 14-3-3σ-deficient cells to sequester the proteins that initiate mitosis and prevent them from entering the nucleus. Thus, 14-3-3σ plays an important role in maintaining the G2 checkpoint in cells and preventing mitotic death. 14-3-3σ Protein is ideal for investigators involved in Cell Stress& Chaperone Proteins, AKT/PKB Pathway, Cancer, Cell Cycle, Cellular Stress, ERK/MAPK Pathway, Neurobiology, PKA/PKC Pathway, and WNT Signaling research.

14-3-3σ or stratifin is a protein that is strongly induced by gamma irradiation and other DNA-damaging agents (1). The induction of 14-3-3σ is mediated by a p53 responsive element. Exogenous introduction of 14-3-3σ into cycling cells results in a G2 cell cycle arrest (2). Knockout of 14-3-3σ in cells showed that the cells are unable to maintain cell cycle arrest after DNA damage. The 14-3-3σ -/- cells die as they enter mitosis. This process is associated with a failure of the 14-3-3σ-deficient cells to sequester the proteins that initiate mitosis and prevent them from entering the nucleus. Thus, 14-3-3σ plays an important role in maintaining the G2 checkpoint in cells and preventing mitotic death. 14-3-3σ Protein is ideal for investigators involved in Cell Stress& Chaperone Proteins, AKT/PKB Pathway, Cancer, Cell Cycle, Cellular Stress, ERK/MAPK Pathway, Neurobiology, PKA/PKC Pathway, and WNT Signaling research.

4EBP1 is a member of a family of translation repressor proteins that directly interact with eukaryotic translation initiation factor 4E (EIF4E). Interaction of 4EBP1 with EIF4E inhibits the multisubunit complex that recruits 40S ribosomal subunits to the 5' end of mRNAs thereby leading to repression of translation. Insulin treatment of adipose cells increases the phosphorylation of 4EBP1 and leads to reduced interaction of 4EBP1 with EIF4E (1). 4EBP1 is expressed in most tissues, with highest levels seen in adipose tissue, pancreas, and skeletal muscle (2). 4EBP1 Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, AKT/PKB Pathway, Angiogenesis, Cancer, and Metabolic Disorder research.

4EBP1 is a member of a family of translation repressor proteins that directly interact with eukaryotic translation initiation factor 4E (EIF4E). Interaction of 4EBP1 with EIF4E inhibits the multisubunit complex that recruits 40S ribosomal subunits to the 5' end of mRNAs thereby leading to repression of translation. Insulin treatment of adipose cells increases the phosphorylation of 4EBP1 and leads to reduced interaction of 4EBP1 with EIF4E (1). 4EBP1 is expressed in most tissues, with highest levels seen in adipose tissue, pancreas, and skeletal muscle (2). 4EBP1 Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, AKT/PKB Pathway, Angiogenesis, Cancer, and Metabolic Disorder research.

4EBP1 is a member of a family of translation repressor proteins that directly interact with eukaryotic translation initiation factor 4E (EIF4E). Interaction of 4EBP1 with EIF4E inhibits the multi-subunit complex that recruits 40S ribosomal subunits to the 5' end of mRNAs thereby leading to repression of translation. Insulin treatment of adipose cells increases the phosphorylation of 4EBP1 and leads to reduced interaction of 4EBP1 with EIF4E (1). 4EBP1 is expressed in most tissues, with highest levels seen in adipose tissue, pancreas, and skeletal muscle (2). 4EBP1 Protein is ideal for investigators involved in Signaling Reagents, Protein Substrates, AKT/PKB Pathway, Angiogenesis, Cancer, and Metabolic Disorder research.