Other Proteins

NFATC1 is a member of the NFAT family of proteins which are Ca2+/calcineurin-responsive transcription factors primarily recognized for their central roles in T lymphocyte activation and cardiac valve development (1). NFAT consists of at least two components: a preexisting cytosolic component that translocates to the nucleus upon T-cell receptor (TCR) stimulation, and an inducible nuclear component. Proteins belonging to the NFAT family of transcription factors play a central role in inducible gene transcription during immune response. The product of NFATC1 is an inducible nuclear component and functions as a major molecular target for the immunosuppressive drugs such as cyclosporin A (2). NFATC1 Protein is ideal for investigators involved in Signaling Proteins, Transcription Proteins, Cardiovascular Disease, Inflammation, JNK/SAPK Pathway, NfkB Pathway, and p38 Pathway research.

NFKB2 is a part of the NFKB complex that is present in various cell types that express cytokines, chemokines, growth factors, cell adhesion molecules, and some acute phase proteins in health and disease states. NFKB protein is activated by a wide variety of stimuli such as cytokines, oxidant-free radicals, inhaled particles, ultraviolet irradiation, and bacterial or viral products (1). Inappropriate activation of NFKB has been linked to inflammatory events associated with autoimmune arthritis, asthma, septic shock, lung fibrosis, glomerulonephritis, atherosclerosis, and AIDS (2). Overexpression of NFKB2 protects androgen sensitive LNCaP cells from apoptotic cell death and cell cycle arrest induced by androgen-deprivation. NFKB2 Protein is ideal for investigators involved in Signaling Proteins, Transcription Proteins, AKT/PKB Pathway, Apoptosis/Autophagy, Inflammation, and p38 Pathway research.

OSR1 is a member of the Ser/Thr family of protein kinases. OSR1 is activated by osmotic stresses and regulates the downstream protein kinase such as PAK1 in order to establish the sensor/signaling modules that initiate the cellular response to environmental stress (1). OSR1 can be phosphorylated by ATM or ATR during DNA damage process (2). OSR1 Protein is ideal for investigators involved in Signaling Proteins, Cellular Proteins, Cardiovascular Disease, and Ser/Thr Kinases research.

p18INK4C is a member of the INK4 family of proteins that regulate the G1 to S cell cycle transition by binding to and inhibiting the pRb kinase activity of cyclin-dependent kinases 4 and 6 (1). Mutation of p18INK4C impairs B-cell terminal differentiation and confers increased susceptibility to tumor development. p18INK4C can function as a tumor suppressor gene in Hodgkins lymphoma and its inactivation may contribute to the cell cycle deregulation and defective terminal differentiation characteristic of the Reed-Sternberg cells (2). p18INK4C Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, Cancer, and Cell Cycle research.

p19INK4D protein is associated with CDK6 in several hematopoietic cell lines. It has been demonstrated that p19INK4D expression enhances cell survival under genotoxic conditions (1). By using p19INK4D-overexpressing cells, it has been demonstrated that p19INK4D expression correlates with the cellular resistance to UV treatment with increased DNA repair activity against UV-induced lesions. p19INK4D regulates protein network that integrate DNA repair, apoptosis and checkpoint mechanisms in order to maintain the genomic integrity (2). p19INK4D Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, Cancer, and Cell Cycle research.

P300 encodes the adenovirus E1A-associated cellular p300 transcriptional co-activator protein (1). P300 is related by sequence to CBP and like CBP can stimulate transcription through activation of CREB. The P300 activity is specifically inhibited by the adenovirus oncoprotein E1A. P300 has also been identified as a co-activator of HIF1A (hypoxia-inducible factor 1 alpha), and thus plays a role in the stimulation of hypoxia-induced genes such as VEGF. P300 is a components of DRAF1 (double-stranded RNA-activated factor-1), a positive regulator of interferon-stimulated gene transcription that functions as a direct response to viral infection (2). P300 Protein is ideal for investigators involved in Signaling Proteins, Acetyl/Methyltransferase Proteins, Apoptosis/Autophagy, Cancer, Cardiovascular Disease, Cell Cycle, ERK/MAPK Pathway, Inflammation, Invasion/Metastasis, Metabolic Disorder, Neurobiology, NfkB Pathway, and PKA/PKC Pathway research.

p33ING1 displays characteristics of a tumor suppressor protein and can induce cell growth arrest and apoptosis. p33ING1 is a nuclear protein and acute expression of p33 ING1 inhibits cell growth. p33ING1 physically interacts with the tumor suppressor protein TP53 and is a component of the p53 signaling pathway. Mutation of p33ING1 gene occurs in neuroblastoma cells and reduced expression is observed in some breast cancer cell lines (1). It has been proposed that p33ING1 can act as a potent growth regulator in normal and in established cells and plays a role as a candidate tumor suppressor gene whose inactivation may contribute to the development of cancers (2). p33ING1 Protein is ideal for investigators involved in Signaling Proteins, Cell Cycle Proteins, Cancer, and Cell Cycle research.

p33ING2 is a member of the inhibitor of growth (ING) family that is associate with and modulates the activity of histone acetyltransferase (HAT) and histone deacetylase (HDAC) complexes and function in DNA repair and apoptosis. P33ING2 is a DNA damage-inducible gene that negatively regulates cell proliferation through activation of p53 by enhancing its acetylation (1). P33ING2 is required for initial DNA damage sensing and chromatin remodeling in the nucleotide excision repair process (2). p33ING2 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.