Proteins & Peptides

Vimentin is a member of intermediate filament family of proteins and is an important structural feature of eukaryotic cells (1). Along with microtubules and actin microfilaments, Vimentin make up the cytoskeleton component of cells. Studies have shown that Vimentin is attached to the nucleus, endoplasmic reticulum and mitochondria, either laterally or terminally. Vimentin plays a significant role in supporting and anchoring the position of the organelles in the cytosol (2). Thus, Vimentin plays a key role in maintaining cell shape, integrity of the cytoplasm, and stabilizing cytoskeletal interactions. Vimentin Protein is ideal for investigators involved in Signaling Proteins, Microtubule/Actin Associated Proteins, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Cell Cycle, Cellular Stress, Inflammation, Invasion/Metastasis, and Neurobiology research.

Vimentin is a member of intermediate filament family of proteins and is an important structural feature of eukaryotic cells (1). Along with microtubules and actin microfilaments, Vimentin make up the cytoskeleton component of cells. Studies have shown that Vimentin is attached to the nucleus, endoplasmic reticulum and mitochondria, either laterally or terminally. Vimentin plays a significant role in supporting and anchoring the position of the organelles in the cytosol (2). Thus, Vimentin plays a key role in maintaining cell shape, integrity of the cytoplasm, and stabilizing cytoskeletal interactions. Vimentin Protein is ideal for investigators involved in Signaling Proteins, Microtubule/Actin Associated Proteins, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Cell Cycle, Cellular Stress, Inflammation, Invasion/Metastasis, and Neurobiology research.

HSP40 is a member of heat shock proteins (HSPs) which are synthesized in cells in response to heat shock and other metabolic stresses and provide a transient state of thermotolerance. HSP40 is localized faintly throughout the cell in non-heat-shocked cells and accumulates in the nuclei and nucleoli in heat-shocked cells (1). The intracellular localization of HSP40 is very similar to that of HSP70. Overexpression of HSP40 reduces aggregate formation and suppresses apoptosis in a neuronal cell model of spinal and bulbar muscular atrophy (inherited neurodegenerative diseases caused by polyglutamine expansion) (2). HSP40 is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, Cancer, Cellular Stress,and Inflammation research.

HSP40 is a member of heat shock proteins (HSPs) which are synthesized in cells in response to heat shock and other metabolic stresses and provide a transient state of thermotolerance. HSP40 is localized faintly throughout the cell in non-heat-shocked cells and accumulates in the nuclei and nucleoli in heat-shocked cells (1). The intracellular localization of HSP40 is very similar to that of HSP70. Overexpression of HSP40 reduces aggregate formation and suppresses apoptosis in a neuronal cell model of spinal and bulbar muscular atrophy (inherited neurodegenerative diseases caused by polyglutamine expansion) (2). HSP40 is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, Cancer, Cellular Stress, and Inflammation research.

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.

HSF1 is a member of the heat shock transcription factor family. Protein-damaging stress lead to the activation of HSF1 which binds to upstream regulatory sequences in the promoters of heat shock genes leading to enhanced heat shock gene expression (1). The activation of HSF1 proceeds through a multi-step pathway, involving a monomer-to-trimer transition, nuclear accumulation and extensive posttranslational modifications. HSF1 activity is regulated at different levels by heat shock proteins and co-chaperones and is modulated further by a number of mechanisms involving other stress-regulated aspects of cell metabolism (2). HSF1 Protein is ideal for investigators involved in Signaling Proteins, Transcription Proteins, Cancer, Cardiovascular Disease, Cellular Stress, Inflammation, and JNK/SAPK Pathway research.

HSF1 is a member of the heat shock transcription factor family. Protein-damaging stress lead to the activation of HSF1 which binds to upstream regulatory sequences in the promoters of heat shock genes leading to enhanced heat shock gene expression (1). The activation of HSF1 proceeds through a multi-step pathway, involving a monomer-to-trimer transition, nuclear accumulation and extensive posttranslational modifications. HSF1 activity is regulated at different levels by heat shock proteins and co-chaperones and is modulated further by a number of mechanisms involving other stress-regulated aspects of cell metabolism (2). HSF1 Protein is ideal for investigators involved in Signaling Proteins, Transcription Proteins, Cancer, Cardiovascular Disease, Cellular Stress, Inflammation, and JNK/SAPK Pathway research.

HSP60 is a chaperonin protein, required for ATP-dependent folding of precursor polypeptides and complex assembly and prevents aggregation and mediates protein refolding after heat shock. Mutations and variations in the HSP 60 gene product may be implicated in genetic diseases (1). HSP60 has been strongly implicated as an example of molecular mimicry in the pathogenicity of autoimmune diseases in T cell-mediated protection. Human HSP60 was found to activate the complement system in normal human serum in a dose-dependent manner. Since complement activation plays an important role in the development of atherosclerosis, the levels of complement-activating anti-HSP60 antibodies are elevated in atherosclerosis-related diseases. (2) HSP60 Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, Cancer, Cardiovascular Disease, Cellular Stress, and Inflammation research.