Other Proteins

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.

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.

GAB1 is a member of the IRS1-like multisubstrate docking protein family and is a direct substrate of the epidermal growth factor receptor and the insulin receptor (1). GAB1 is tyrosine phosphorylated upon stimulation of cells with various cytokines, growth factors, and antigen receptor. Tyrosine phosphorylation of GAB1 mediates interaction with several proteins that contain SH2 domains such as SHP2 and phosphatidylinositol 3-kinase. GAB1 is an important mediator of branching tubulogenesis and plays a central role in cellular growth response, transformation and apoptosis (2). GAB1 Protein is ideal for investigators involved in Signaling Proteins, Adaptor Proteins, Angiogenesis, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, ERK/MAPK Pathway, Invasion/Metastasis, JAK/STAT Pathway, and Neurobiology research.

PARP1 is the primary member of the poly(ADP-ribose) polymerase family, whose function is to signal DNA damage (and to recruit repair proteins) by PARylation. PARP1 is also involved in multiple cell death pathways, including apoptosis, necroptosis, autophagy, and a relatively new pathway termed parthanatos. PARP1 can also promote tissue survival by shifting the balance of cell death programs between autophagy and necrosis. Clinical studies have shown vulnerability to PARP inhibitors in DNA repair defective cancers. PARP1-ZF is useful for researchers interested in cellular processes including DNA damage, transcriptional control, and stem cell identity research.

MEK1 recombinant protein was produced in Sf9 cells. Mitogen-activated protein kinase kinase 1, also known as MKK or MEK, is an integral component of the MAP kinase cascade that regulates cell growth and differentiation. This pathway also plays a key role in synaptic plasticity in the brain. Activated MEK 1 acts as a dual specificity kinase phosphorylating both a threonine and a tyrosine residue on MAP kinase. MEK1 and MEK2 are about 80% identical to each other, and nearly identical within the kinase domain. Recombinant MEK1 protein is ideal for investigators involved in Neuroscience, Cell Signaling and Cancer Research.

MEK2 recombinant protein was produced in Sf9 cells. Mitogen-activated protein kinase kinase 2, also known as MAP2K2, MEK, MEK2, MKK2, MEK-2, is an integral component of the MAP kinase cascade that regulates cell growth and differentiation. This pathway also plays a key role in synaptic plasticity in the brain. Activated MEK 1 acts as a dual specificity kinase phosphorylating both a threonine and a tyrosine residue on MAP kinase. MEK1 and MEK2 are about 80% identical to each other, and nearly identical within the kinase domain. Recombinant MEK2 protein is ideal for investigators involved in Neuroscience, Cell Signaling and Cancer Research.

MEK2 pS222-pS226 is an activated recombinant protein was produced in Sf9 cells by co-expression of B-raf. Mitogen-activated protein kinase kinase 2, also known as MAP2K2, MEK, MEK2, MKK2 is an integral component of the MAP kinase cascade that regulates cell growth and differentiation. This pathway also plays a key role in synaptic plasticity in the brain. Activated MEK 2 acts as a dual specificity kinase phosphorylating both a threonine and a tyrosine residue on MAP kinase. This recombinant protein is the MEK2 isoform and is ideal for investigators involved in Neuroscience, Cell Signaling and Cancer Research.