Other Proteins

KIP1 (cyclin-dependent kinase inhibitor 1B) is a kinesin-related motor protein required for mitotic spindle assembly and chromosome segregation (1). Many tumorigenic processes modulate cell-cycle progression by regulating the levels of the cyclin-dependent kinase inhibitor KIP1. KIP1 binds to and inhibits cyclinE-Cdk2 complex, cyclinA-CDK2 and cyclinD1-CDK4 (2). The phosphorylation- and ubiquitination-dependent proteolysis of KIP1 is implicated in control of the G1-S transition in the cell cycle. KIP1 is critical for retinoblastoma protein (Rb)-induced cellular proliferative senescence. p27KIP1 Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, Cancer, and Cell Cycle research.

p53 is a key regulator of cell growth and acts as a tumor suppressor gene. Wild-type p53 gene can suppress transformation of rat embryo fibroblasts in cell culture by other oncogenes such as the adenovirus E1A and Ras (1). DNA tumor viruses such as SV40 large T antigen and the adenovirus E1A plus E1B-55Kd proteins bind to p53 and inactivate its tumor suppressor activities leading to cellular transformation. Mutational inactivation of the p53 gene is detected in more than 50% of human cancers. Mutation of p53 renders cancer cells more resistant to current cancer therapies due to lack of p53-mediated apoptosis (2). p53 Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Cell Cycle, Cellular Stress, Inflammation, JNK/SAPK Pathway, Metabolic Disorder, Neurobiology, and p38 Pathway research.

HSP27 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. HSP27 plays a major role in the increased thermal resistance acquired by cells after exposure to HSP inducers (1). The level of HSP27 phosphorylation is significantly elevated after exposure of cells to heat shock, sodium arsenite, IL-1 and TNF-a. MAPKAPK2 and MAPKAPK3 are both activated by these conditions and can phosphorylate HSP27 on serine residues (2). HSP27 Protein is ideal for investigators involved in Signaling Proteins, Cell Stress & Chaperone Proteins, Cancer, Cellular Stress, and p38 Pathway research.

Interleukin-1beta (IL-1β) is a proinflammatory cytokine produced in response to inflammatory agents by a variety of cells, including monocytes, macrophages, and dendric cells (DCs). IL-1β and IL-1α are two distinct and independently regulated gene products that comprise IL-1 and signal through the Type 1 IL-1 receptor (IL-1R1). Although IL-1α is cell associated and IL-1β is secreted, they have nearly identical biological activity in that they induce adhesion molecule expression on epithelial cells, control fever induction, and play a role in arthritis and septic shock. Signaling activated by the IL-1R1 promotes these activities through a MYD88 signaling pathway similar to those associated with Toll receptors. Recombinant human IL-1β is a non-glycosylated single chain 17,376 Da protein containing 153 amino acid residues.

TNFα is secreted by macrophages, monocytes, neutrophils, T-cells, and NK- cells following their stimulation by bacterial LPS. Cells expressing CD4 secrete TNF-alpha, while CD8 cells secrete little or no TNF-alpha. The synthesis of TNF-alpha is induced by many different stimuli including interferons, IL2, and GM-CSF. Recombinant Human Tumor Necrosis Factor-alpha produced in E. coli is a single, non-glycosylated, polypeptide chain containing 158 amino acids and having a molecular mass of 17483.77 Daltons.

Cytokines of the IL6/GCSF/MGF family are glycoproteins of about 170 to 180 amino acid residues that contains four conserved cysteine residues involved in two disulfide bonds. They have a compact, globular fold (similar to other interleukins), stabilized by the 2 disulfide bonds. One half of the structure is dominated by a 4 alpha-helix bundle with a left-handed twist: the helices are anti-parallel, with 2 overhand connections, which fall into a 2-stranded anti-parallel beta-sheet. The fourth alpha-helix is important to the biological activity of the molecule. Interleukin (IL)-6 is an important proinflammatory and immunoregulatory cytokine expressed by various cells. Interleukin-6 has been shown to inhibit the growth of early stage and to promote the proliferation of advanced stage melanoma cells in vitro. Recombinant Human IL-6 produced in E.coli is a single, non-glycosylated polypeptide chain containing 184 amino acids and having a molecular mass of 21,000 Daltons.

Cytokines of the IL6/GCSF/MGF family are glycoproteins of about 170 to 180 amino acid residues that contains four conserved cysteine residues involved in two disulfide bonds. They have a compact, globular fold (similar to other interleukins), stabilized by the 2 disulfide bonds. One half of the structure is dominated by a 4 alpha-helix bundle with a left-handed twist: the helices are anti-parallel, with 2 overhand connections, which fall into a 2-stranded anti-parallel beta-sheet. The fourth alpha-helix is important to the biological activity of the molecule. Interleukin (IL)-6 is an important proinflammatory and immunoregulatory cytokine expressed by various cells. Interleukin-6 has been shown to inhibit the growth of early stage and to promote the proliferation of advanced stage melanoma cells in vitro. Recombinant Human IL-6 produced in E.coli is a single, non-glycosylated polypeptide chain containing 184 amino acids and having a molecular mass of 21,000 Daltons.

Interleukin-8 is a chemokine produced by macrophages and other cell types such as epithelial cells. Human IL-8 (CXCL8) antibody is commonly used in many experiments focused around inflammation. IL-8 is ideal for investigators involved in Cancer, Immunology and Cardiovascular research.

Granulocyte Macrophage Colony Stimulating Factor is produced in response to a number of inflammatory mediators by mesenchymal cells present in the hemopoietic environment and at peripheral sites of inflammation. Granulocyte Macrophage-CSF is able to stimulate the production of neutrophilic granulocytes, macrophages, and mixed granulocyte-macrophage colonies from bone marrow cells and can stimulate the formation of eosinophil colonies from fetal liver progenitor cells. GM-CSF can also stimulate some functional activities in mature granulocytes and macrophages. GM-CSF receptors shows significant homologies with other receptors for hematopoietic growth factors , including IL2-beta, IL-3 , IL -6 , IL-7 , EPO and the Prolactin receptors. Recombinant Human Granulocyte Macrophage CSF produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 127 amino acids and having a molecular weight of 14.5 kDa.