Proteins & Peptides

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.

HSP70 is a member of the heat shock protein family and is synthesized by cells of many organisms in response to stress (1). HSP70 is found mostly but not exclusively in the nucleus of unstressed cells. For several hours after a short heat shock, however, it is strongly concentrated in nucleoli (2). Nucleoli are transiently damaged by such a heat shock: their morphology changes and assembly and export of ribosomes is blocked for several hours. HSP70 helps to stabilize the morphological changes of the nucleoli. HSP70 Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Cellular Stress, and Inflammation research.

HSP70 is a member of the heat shock protein family and is synthesized by cells of many organisms in response to stress (1). HSP70 is found mostly but not exclusively in the nucleus of unstressed cells. For several hours after a short heat shock, however, it is strongly concentrated in nucleoli (2). Nucleoli are transiently damaged by such a heat shock: their morphology changes and assembly and export of ribosomes is blocked for several hours. HSP70 helps to stabilize the morphological changes of the nucleoli. HSP70 Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Cellular Stress, and Inflammation research.

HSP90α is a member of the HSP90 family of proteins which are important molecular chaperones involved in signal transduction, cell cycle control, stress management, folding, degradation, and transport of proteins (1). HSP90 is a molecular chaperone that plays a key role in the conformational maturation of oncogenic signaling proteins, including HER2/ERBB2, AKT, RAF1, BCR-ABL and mutated p53. HSP90 inhibitors bind to HSP90, and induce the proteasomal degradation of HSP90 client proteins. HSP90α is an important mediator of cancer cell invasion and is expressed extracellularly on fibrosarcoma and breast cancer cells where it interacts with MMP2 (2). HSP90α Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, and Cellular Stress research.

HSP90α is a member of the HSP90 family of proteins which are important molecular chaperones involved in signal transduction, cell cycle control, stress management, folding, degradation, and transport of proteins (1). HSP90 is a molecular chaperone that plays a key role in the conformational maturation of oncogenic signaling proteins, including HER2/ERBB2, AKT, RAF1, BCR-ABL and mutated p53. HSP90 inhibitors bind to HSP90, and induce the proteasomal degradation of HSP90 client proteins. HSP90α is an important mediator of cancer cell invasion and is expressed extracellularly on fibrosarcoma and breast cancer cells where it interacts with MMP2 (2). HSP90α Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, and Cellular Stress research.

HSP90β is a member of the HSP90 family of proteins which are important molecular chaperones involved in signal transduction, cell cycle control, stress management, and folding, degradation, and transport of proteins (1). HSP90 proteins have been found in a variety of organisms suggesting that they are ancient and conserved. HSP90 binds to client proteins (such as steroid receptors, AKT, Bcr-Abl, Apaf-1, survivin, cyclin dependent kinases) and acts as a molecular chaperone. Failure of Hsp90 chaperone activity leads to misfolding of client proteins, which leads to ubiquitination and proteasome degradation, and thus deregulation of cellular homeostasis (2). HSP90β Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, and Cellular Stress research.

HSP90β is a member of the HSP90 family of proteins which are important molecular chaperones involved in signal transduction, cell cycle control, stress management, and folding, degradation, and transport of proteins (1). HSP90 proteins have been found in a variety of organisms suggesting that they are ancient and conserved. HSP90 binds to client proteins (such as steroid receptors, AKT, Bcr-Abl, Apaf-1, survivin, cyclin dependent kinases) and acts as a molecular chaperone. Failure of Hsp90 chaperone activity leads to misfolding of client proteins, which leads to ubiquitination and proteasome degradation, and thus deregulation of cellular homeostasis (2). HSP90β Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Cancer, and Cellular Stress research.

SOD2 (superoxide dismutase 2) is a member of the iron/manganese superoxide dismutase family. SOD2 binds to the superoxide byproducts of the mitochondrial electron transport chain and converts them to hydrogen peroxide and diatomic oxygen. Failure of SOD2 to remove the superoxide byproducts leads to an increase in mitochondrial reactive oxygen species resulting in biochemical aberrations with features reminiscent of mitochondrial myopathy, Friedreich ataxia, and HMGCL deficiency (1). Mutations in SOD2 have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer (2). SOD2 Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Cellular Stress, Inflammation, Neurobiology, and p38 Pathway research.

SOD2 (superoxide dismutase 2) is a member of the iron/manganese superoxide dismutase family. SOD2 binds to the superoxide byproducts of the mitochondrial electron transport chain and converts them to hydrogen peroxide and diatomic oxygen. Failure of SOD2 to remove the superoxide byproducts leads to an increase in mitochondrial reactive oxygen species resulting in biochemical aberrations with features reminiscent of mitochondrial myopathy, Friedreich ataxia, and HMGCL deficiency (1). Mutations in SOD2 have been associated with idiopathic cardiomyopathy (IDC), premature aging, sporadic motor neuron disease, and cancer (2). SOD2 Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Cellular Stress, Inflammation, Neurobiology, and p38 Pathway research.