Proteins & Peptides

AKT1 is a component of the PI-3 kinase pathway and is activated by phosphorylation at Ser 473 and Thr 308. AKT is a cytoplasmic protein also known as Protein Kinase B (PKB) and RAC (Related to A and C kinases). AKT is a key regulator of many signal transduction pathways, and it exhibits tight control over cell proliferation and cell viability. Overexpression or inappropriate activation of AKT is noted in many types of cancer. AKT mediates many of the downstream events of PI 3-kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI 3-kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus. AKT has two main roles: (i) inhibition of apoptosis; (ii) promotion of proliferation. AKT1 recombinant protein is ideal for investigators involved in Cell Signaling, Neuroscience and Signal Transduction research.

AKT1 is a component of the PI-3 kinase pathway and is activated by phosphorylation at Ser 473 and Thr 308. AKT is a cytoplasmic protein also known as Protein Kinase B (PKB) and RAC (Related to A and C kinases). AKT is a key regulator of many signal transduction pathways, and it exhibits tight control over cell proliferation and cell viability. Overexpression or inappropriate activation of AKT is noted in many types of cancer. AKT mediates many of the downstream events of PI 3-kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI 3-kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus. AKT has two main roles: (i) inhibition of apoptosis; (ii) promotion of proliferation. AKT1 mutant (T308 / S473A) recombinant protein is ideal for investigators involved in Cell Signaling, Neuroscience and Signal Transduction researc

AKT2 is a component of the PI-3 kinase pathway and is activated by phosphorylation at Ser 473 and Thr 308. AKT is a cytoplasmic protein also known as Protein Kinase B (PKB) and RAC (Related to A and C kinases). AKT is a key regulator of many signal transduction pathways, and it exhibits tight control over cell proliferation and cell viability. Overexpression or inappropriate activation of AKT is noted in many types of cancer. AKT mediates many of the downstream events of PI 3-kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI 3-kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus. AKT has two main roles: (i) inhibition of apoptosis; (ii) promotion of proliferation. AKT2 recombinant protein is ideal for investigators involved in Cell Signaling, Neuroscience and Signal Transduction research.

AKT3 is a component of the PI-3 kinase pathway and is activated by phosphorylation at Ser 473 and Thr 308. AKT is a cytoplasmic protein also known as Protein Kinase B (PKB) and RAC (Related to A and C kinases). AKT is a key regulator of many signal transduction pathways, and it exhibits tight control over cell proliferation and cell viability. Overexpression or inappropriate activation of AKT is noted in many types of cancer. AKT mediates many of the downstream events of PI 3-kinase (a lipid kinase activated by growth factors, cytokines and insulin). PI 3-kinase recruits AKT to the membrane, where it is activated by PDK1 phosphorylation. Once phosphorylated, AKT dissociates from the membrane and phosphorylates targets in the cytoplasm and the cell nucleus. AKT has two main roles: (i) inhibition of apoptosis; (ii) promotion of proliferation. AKT3 recombinant protein is ideal for investigators involved in Cell Signaling, Neuroscience and Signal Transduction research.

14-3-3α/β is a member of the highly conserved 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins (1). 14-3-3α/β protein has been shown to interact with RAF1 and CDC25 phosphatases, suggesting that it may play a role in linking mitogenic signaling and the cell cycle machinery. 14-3-3-β interacts with the TSC1-TSC2 dimer (2). The interaction required phosphorylation of TSC2 at Ser1210. Binding of 14-3-3-β to TSC2 did not alter the interaction between TSC1 and TSC2, but it reduced the ability of the complex to inhibit phosphorylation of ribosomal protein S6 kinase impairing the ability of the complex to inhibit cell growth. 14-3-3 alpha/beta Protein is ideal for investigators involved in Cell Stress & Chaperone Proteins, Cell Signaling, Cancer research, Cell Cycle, Cellular Stress, Neurobiology, and WNT Signaling research.

14-3-3α/β is a member of the highly conserved 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins (1). 14-3-3α/β protein has been shown to interact with RAF1 and CDC25 phosphatases, suggesting that it may play a role in linking mitogenic signaling and the cell cycle machinery. 14-3-3-β interacts with the TSC1-TSC2 dimer (2). The interaction required phosphorylation of TSC2 at Ser1210. Binding of 14-3-3-β to TSC2 did not alter the interaction between TSC1 and TSC2, but it reduced the ability of the complex to inhibit phosphorylation of ribosomal protein S6 kinase impairing the ability of the complex to inhibit cell growth. 14-3-3 alpha/beta Protein is ideal for investigators involved in Cell Stress & Chaperone Proteins, Cell Signaling, Cancer research, Cell Cycle, Cellular Stress, Neurobiology, and WNT Signaling research.

14-3-3α/β is a member of the highly conserved 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins (1). 14-3-3α/β protein has been shown to interact with RAF1 and CDC25 phosphatases, suggesting that it may play a role in linking mitogenic signaling and the cell cycle machinery. 14-3-3-β interacts with the TSC1-TSC2 dimer (2). The interaction required phosphorylation of TSC2 at Ser1210. Binding of 14-3-3-β to TSC2 did not alter the interaction between TSC1 and TSC2, but it reduced the ability of the complex to inhibit phosphorylation of ribosomal protein S6 kinase impairing the ability of the complex to inhibit cell growth. 14-3-3 alpha/beta Protein is ideal for investigators involved in Cell Stress & Chaperone Proteins, Cell Signaling, Cancer research, Cell Cycle, Cellular Stress, Neurobiology, and WNT Signaling research.

14-3-3α/β is a member of the highly conserved 14-3-3 family of proteins which mediate signal transduction by binding to phosphoserine-containing proteins (1). 14-3-3α/β protein has been shown to interact with RAF1 and CDC25 phosphatases, suggesting that it may play a role in linking mitogenic signaling and the cell cycle machinery. 14-3-3-β interacts with the TSC1-TSC2 dimer (2). The interaction required phosphorylation of TSC2 at Ser1210. Binding of 14-3-3-β to TSC2 did not alter the interaction between TSC1 and TSC2, but it reduced the ability of the complex to inhibit phosphorylation of ribosomal protein S6 kinase impairing the ability of the complex to inhibit cell growth. 14-3-3 alpha/beta Protein is ideal for investigators involved in Cell Stress & Chaperone Proteins, Cell Signaling, Cancer research, Cell Cycle, Cellular Stress, Neurobiology, and WNT Signaling research.

14-3-3ε also known as tyrosine 3-monooxygenase/tryptophan 5-monooxygenase activation protein is a member of the 14-3-3 family. 14-3-3ε has been reported to be involved in heat shock transcription factor 1 (HSF1) and extracellular signal regulated protein kinase (ERK) pathways (1). 14-3-3ε interaction with the deubiquitinating enzyme UBPY, also known as USP8, regulates cargo sorting and membrane traffic at early endosomes. Association of 14-3-3ε, HSF1 with ERK during heat shock may modulate the amplitude of the response and control the termination of HSP expression on resumption of growth conditions (2). 14-3-3ε protein is ideal for investigators involved in Cell Stress & Chaperone Proteins, Cell Signaling, Cancer research, Cell Cycle, Cellular Stress, Neurobiology, and WNT Signaling research.