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Selenoprotein-P(SelP) is the major selenoprotein in human blood plasma and a transport protein which is carrying selenium to various extrahepatic tissues. Though its expression is detected in most tissues, highest amounts are produced by the liver, which secretes highly glycosylated SelP into plasma. Purification of human SelP yields two distinct isoforms with 61 and 55 kDa, differing in selenium content. SelP also has been shown to chelate heavy metals such as cadmium and mercury, and there are several evidences about its serum antioxidant capacity and protection against oxidative stress. Selenium deficiency predispose to several pathological condition such as cancer, coronary heart disease and liver necrosis although the biological function of SelP in various pathologic conditions has not been established.

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Protein kinase C (PKC) is a family of serine-threonine kinases that regulate a broad spectrum of cellular functions. The family is composed of nine genes that express structurally related phospholipid-dependent kinases with distinct means of regulation and tissue distribution. Based on their structures and sensitivities to Ca2+ and diacylglycerol (DAG), they have been classified into conventional PKCs (alpha, beta, and gamma), novel PKCs (Delta, Epsilon, Eta, and IPA), and atypical PKCs (Zeta and Lambda/Iota). PKC Gamma is a member of the cPKC subfamily which is activated by Ca2+ and diacylglycerol in the presence of phosphatidylserine. Physiologically, PKC Gamma is activated by a mechanism coupled with receptor-mediated breakdown of inositol phospholipid as other cPKC isotypes. PKC Gamma is expressed solely in the brain and spinal cord and its localization is restricted to neurons. Within the brain, PKC Gamma is the most abundant in the cerebellum, hippocampus and cerebral cortex, where the existence of neuronal plasticity has been demonstrated.

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Catalase is a homotetrameric heme-containing enzyme present within the matrix of all peroxisomes. It carries out a dismutation reaction in which hydrogen peroxide is converted to water and oxygen. Human catalase has the last four amino acids (-KANL) at the extreme C-terminus for peroxisome targeting. The monomer of human catalase is 61.3 kD in molecular size. Catalase has been implicated as an important factor in inflammation, mutagenesis, prevention of apoptosis, and stimulation of a wide spectrum of tumors. Loss of catalase leads to the human genetic disease, acatalasemia, or Takahara’s disease (1).

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Platelet-derived growth factors (PDGFs) have been implicated in the control of cell proliferation, survival and migration. The PDGF family of growth factors consists of five different disulphide-linked dimers built up of four different polypeptide chains encoded by four different genes. Theses isoforms, PDGF-AA, PDGF-AB, PDGF-BB, PDGF-CC and PDGF-DD, act via two receptor tyrosine kinases, PDGF receptors α and β. Thus far, gene-targeting experiments have been attempted to create knockout mice deficient for PDGFR-α or PDGFR-β. Those mice, however, died either at the embryonic stage or several days after birth. Platelet-derived growth factor receptors, PDGFR-α and PDGFR-β, have five extracellular immunoglobulin-like domains and an intracellular tyrosine kinase domain. Upon binding a PDGF, the receptors form homo- and heterodimers. Dimerization of the receptors juxtaposes the intracellular part of the receptors, which allow phosphorylation in trans between the two receptors in the complex. These autophosphorylation provide docking sites for downstream signal transduction molecules. More than 10 different SH2–domain-containing molecules have been shown to bind to different autophosphorylation sites in the PDGF α- and β-receptors. There are signal transduction molecules with enzymatic activity, such as PI3-kinase, PLC-γ, Src, SHP-2, GAP, as well as adaptor molecules such as Grb2, Shc, Nck, Grb7 and Crk, and Stats. Each of the different partners recruited by the activated receptor initiates different signaling pathways, making possible a great variety of cellular response.

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The epidermal growth factor receptor (EGFR) is a transmembrane receptor tyrosine kinase of the ErbB (also known as HER) family in which four members have been identified: EGFR (ErbB1), HER2/Neu (ErbB2), HER3 (ErbB3), and HER4 (ErbB4). All four erbB receptors are composed of an extracellular ligand-binding region consisting of glycosylated domains, a transmembrane domain containing a single hydrophobic anchor sequence, an intracellular region containing the catalytic tyrosine kinase domain, and a carboxyl-terminal region containing several tyrosine residues that become phosphorylated after receptor activation.
The epidermal growth factor receptor (EGFR) signaling pathway is one of the most important pathways that regulate growth, survival, proliferation, and differentiation in mammalian cells. EGFR and other members of the erbB family form either homodimers or heterodimers upon ligand binding, resulting in conformational changes that allow activation of protein kinases and transphosphorylation of key tyrosine residues within the carboxyl-terminal domain. After the induction of tyrosine phosphorylation, some signaling pathways appear to start with the recognition of the C-terminal phosphotyrosines by appropriate adaptor or signaling molecules. The aberrant activation of the EGFR leads to enhanced proliferation and other tumor-promoting activities. Several mechanisms lead to aberrant receptor activation, including receptor overexpression, gene amplification, activating mutations, overexpression of receptor ligands, and/or loss of their negative regulatory mechanisms.
The epidermal growth factor receptor (EGFR) has been extensively investigated as a target for anti-neoplastic therapy. Anti-EGFR antibodies that interfere with ligand-dependent receptor activation have shown clinical activity in a variety of solid tumors.

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Superoxide dismutase (SOD) is an antioxidant enzyme involved in the defense system against reactive oxygen species (ROS). SOD catalyzes the dismutation reaction of superoxide radical anion (O2-) to hydrogen peroxide, which is then catalyzed to innocuous O2 and H2O by glutathione peroxidase and catalase. Several classes of SOD have been identified. These include intracellular copper, zinc SOD (Cu, Zn-SOD/SOD-1), mitochondrial manganese SOD (Mn-SOD/SOD-2) and extracellular Cu, Zn-SOD (EC-SOD/SOD-3) (1). SOD-1 is found in all eukaryotic species as a homodimeric 32-kDa enzyme containing one each of Cu and Zn ion per subunit (2). The manganese containing 80-kDa tetrameric enzyme SOD2, is located in the mitochondrial matrix in close proximity to a primary endogenous source of superoxide, the mitochondrial respiratory chain (3). SOD-3 is a heparin-binding multimer of disulfide-linked dimers, primarily expressed in human lungs, vessel walls and airways (4). SOD-4 is a copper chaperone for superoxide dismutase (CCS), which specifically delivers Cu to copper/zinc superoxide dismutase. CCS may activate copper/zinc superoxide dismutase through direct insertion of the Cu cofactor.

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Mitogen- and stress-activated protein kinases (MSK2) is nuclear kinase that act downstream of mitogen-activated protein/extracellular signal-regulated kinase pathways. It contains two kinase domains in the N-terminal and C-terminal region, respectively. MSK2 is activated in response to mitogenic stimuli via Erk1/2MAPK pathway and also by stress stimuli via p38MAPK pathway. Signals from mitogens and cellular stresses are involved in many functions including cell proliferation, differentiation, and survival through the phosphorylation of cyclic AMP response element-binding protein (CREB) at Ser133 which is catalyzed by MSK2. Recently, MSK2 has been shown to be required for stress-induced phosphorylation of histone H3-Ser and transcriptional activation of several immediate early genes.

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NF-κB (Nuclear Factor kappa B) is a nuclear transcription factor found in all cell types and is involved in cellular responses to stimuli such as stress, cytokines, free radicals, ultraviolet irradiation, and bacterial or viral antigens. NF-κB plays a key role in regulating the immune response to infection. Consistent with this role, incorrect regulation of NF-κB has been linked to cancer, inflammatory and autoimmune diseases, septic shock, viral infection and improper immune development. There are five members in the NF-κB family: NF-κB1, NF-κB2, RelA (also named p65), RelB, and c-Rel. The RelB protein is present in the cytosol, bound to p50 or p52 and an inhibitory IκB protein, forming an inactive trimeric complex. Following cell signalling events leading to IκB degradation, Rel/NFκ-B proteins are translocated to the nucleus where they regulate gene expression. The genes controlled by Rel/NF-κB family members are predominantly genes involved in the host response to infection, stress and injury. RelB mediates the regulation of genes involved in immune and inflammatory processes.

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NCK1 is one of the adaptor proteins which mediate specific protein-protein interactions in signaling processes. Adaptor proteins usually contain several domains like SH2 (Src homology 2) and SH3 which allow specific interactions with other specific proteins.
NCK1 and NCK2 showing high sequence identity (68%) have three SH3 domains and a C-terminal SH2 domain. Both of them bind receptor tyrosine kinases such as PDGFR and other tyrosine phosphorylated
proteins via their SH2 domains. Various molecules which interact with SH domains of Nck and regulate signaling process of actin cytoskeleton reorganization have been identified. Ncks are thought to have important functions in the development of mesodermal structures during embryogenesis, linked to a role in cell movement and cytoskeletal reorganization.
Nck also have a function in modulating mRNA translation at the level of initiation by interacting eukayotic initiation factor 2 (eIF2). Under the stressed conditions, protein synthesis is reduced by inhibiting the activity of eIF2 through the phosphorylation, transiently inhibiting recycling of eIF2
into its active form.

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Interferon alpha-2(IFNa2) which have antiviral activities, produced by macrophages. Three forms exist; alpha-2a, alpha-2b and alpha-2c.

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Ataxia telangiectasia mutated (ATM) is a serine/threonine-specific protein kinase that is activated by DNA double-strand breaks. It phosphorylates several key proteins that initiate activation of the DNA damage checkpoint, leading to cell cycle arrest, DNA repair or apoptosis. Several of these targets are p53, CHK2, BRCA1, and H2AX.
ATM triggers the G1/S checkpoint; ATR (Ataxia telangiectasia and Rad3-related) prevents G1/S stasis. In this single point in the cell cycle, it would appear that ATM and ATR function in opposition to one another.
Ataxia telangiectasia (AT) is a rare neurodegenerative, autosomal recessive disorder characterized by chromosome instability, radiosensitivity, immunodeficiency and a predisposition for cancer.
The ATR (ATM and Rad3-related) kinase and its downstream effector kinase, Chk1, are central regulators of the replication checkpoint. Loss of these checkpoint proteins causes replication fork collapse and chromosomal rearrangements. ATR are thought to be master controllers of cell cycle checkpoint signaling pathways that are required for cell response to DNA damage and for genome stability.

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The two ubiquitin C-terminal hydrolase (UCH) enzymes, UCHL1 and UCHL3, deubiquitinate ubiquitin-protein conjugates and control the cellular balance of ubiquitin. UCHL1 and UCHL3 are both small proteins of ~220 amino acids that share more than 40% amino acid sequence identity.
UCHL3 is universally expressed in all tissues, while UCHL1 is expressed exclusively in neuronal tissue, testis and ovary.
The activity of UCHL3 is more than 200 fold higher than UCHL1 when a fluorogenic ubiquitin substrate is used. UCHL1 associates with monoubiquitin and UCHL3 binds to Nedd8, ubiquitin-like protein.
UCHL1 and UCHL3 play a role in the regulation of neuronal development and spermatogenesis.
UCHL1 is involved in the pathogenesis of Parkinson’s disease (PD) and Alzheimer’s disease (AD). Down-regulation and extensive oxidative modification of UCHL1 have been observed in the brains of AD patients as well as PD patients.

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Cyclin-dependent kinases (cdk) belong to a group of protein kinases originally discovered as being involved in the regulation of the cell cycle. Cdks are also involved in the regulation of transcription and mRNA processing. A Cdk is activated by association with a cyclin, forming a cyclin-dependent kinase complex.
Cdk1, also known as cell division control protein 2 (cdc2), is one of the components of the maturation promoting factor (MPF) which is essential for G1/S and G2/M phase transitions of eukaryotic cell cycle. Cdk1, when bound to cyclin B, allows a dividing cell to enter into mitosis from G2 and permits the transition from G1 through S in conjunction with cyclin A and cyclin E. The Cdk1 protein is constantly present throughout the cell division cycle, but its activity is finely tuned by means of protein-protein interactions and reversible phosphorylation.
Cdk1 can also enhance cell migration. Increased levels of Cdk1 promote cell migration together with cyclin B2 and the actin-stabilizing protein caldesmon. Phosphorylation of caldesmon bound to actin results in the displacement of caldesmon from actin followed by the altered interaction of actin with myosin. These events contribute to increased cell migration.

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Sequential activation of protein kinases within the MAPK (mitogen-activated protein kinases) cascades is a common mechanism of signal transduction in many cellular processes. The ERK signaling cascade is a central MAPK pathway that plays a role in the regulation of various cellular processes such as proliferation, differentiation, development, learning, and survival. Mitogen-activated protein kinase kinases (MAPKK) phosphorylate MAPK. MEK (MAP kinase or ERK kinase) is the immediate upstream activator kinase of ERK.
MEK6 encodes a 334-amino acid protein with 82% identity to MKK3. MEK6 is highly expressed in skeletal muscle like many other members of this family, but in contrast to MKK3 its expression in leukocytes is very low. The human MEKs (MEK1, MEK2, MEK3) show remarkably different activity toward ERKl and ERK2. MEK2 is the most active ERK activator. MEK3 is inactive toward ERKl or ERK2. MEK3, MEK4, and MEK6 phosphorylate and activate p38 MAP kinase. The p38 mitogen-activated protein (MAP) kinase signal transduction pathway is activated by proinflammatory cytokines and environmental stress. Transcription factors such as ATF2 and Elk-1 are targets of the p38 MAP kinase signal transduction pathway.

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Anti-Neuroglobulin Rabbit Polyclonal Antibody

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Anti-CREB-A Rabbit Polyclonal Antibody

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Thyroglobulin (Tg) is a 660 kDa, dimeric protein consisting of two subunits containing 2750 amino acids with a molecular weight of 330 kDa. Among twenty putative N-linked glycosylation sites, only 16 are glycosylated
in the mature protein. Tg is produced by and used entirely within the thyroid gland. Tg is the precursor of the iodinated thyroid hormones thyroxine (T4) and triiodothyronine (T3). Iodinated Tg is stored in the lumen of thyroid follicles. Upon stimulation by thyroid stimulating hormone (TSH), Tg is reabsorbed into thyrocytes and degraded to end product T3 and T4 that are subsequently secreted into the bloodstream.
Tg-specific antibodies help in the diagnosis of with Hashimoto's thyroiditis which is an autoimmune disease inducing hypothyroidism, or Graves‘ disease which is a thyroid disorder characterized by goitre, exophthalmos, and hyperthyroidism. Thyroid carcinoma developing from dyshormonogenic goiters due to Tg mutation have been reported. It has been suggested that constant and prolonged stimulation by TSH might result in the appearance of thyroid carcinoma.
Tg levels in the blood can be used as a tumor marker for papillary and follicular thyroid cancer. Tg levels in the blood can also be elevated in cases of Graves' disease. TSH (Thyroid-stimulating hormone)-stimulated Tg test using a Tg cutoff of 2 micro g/liter is sufficiently sensitive to be used as the principal test in the follow-up management of low-risk patients with DTC (differentiated thyroid cancer).

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Insulin receptor substrate (IRS) proteins play a central role in maintaining basic cellular functions such as growth and metabolism through insulin/insulin like growth factor (IGF) signaling. Four members (IRS-1, IRS-2, IRS-3, IRS-4) of this family have been identified which differ in their subcellular distribution and interaction with SH2 domain proteins. After phosphorylation by activated receptors, these intracellular signaling molecules recruit various downstream effector pathways including phosphatidylinositol 3-kinase, tyrosine protein phosphatase SHPTP-2, and several smaller adapter molecules such as the growth factor receptor-binding protein Grb-2.
IRSs are also thought to be able to induce malignant transformation.

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Anti-DUSP28 Mouse Monoclonal Antibody [clone: AF16B7]

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Transglutaminase(TGase) catalyses the crosslink of proteins by forming ε-(γ-glutamyl) lysine isopeptide bonds and requires the binding of Ca2+ for its activity. In mammals, eight distinct TGase isoenzymes have been identified. Tissue transglutaminase (tTGase), also known as TGase 2, has four distinct domains: N-terminal β-sandwich, catalytic core and two C-terminal β-barrel domains. tTGase may have a role in cell death, cell proliferation, cell differentiation, and receptor-mediated endocytosis. In the Alzheimer’s disease brain, the elevated tTGase activity is manifested by polymerization of a number of proteins, including Aβ peptide, β-amyloid precursor protein and the tau protein, with formation of neurofibrillary tangles.

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Peroxiredoxin (Prx) is a growing peroxidase family, whose mammalian members have been known to connect with cell proliferation, differentiation, and apoptosis.
Many isoforms (about 50 proteins), collected in accordance to the amino acid sequence homology, particularly amino-terminal region containing active site cysteine residue, and the thiol-specific antioxidant activity, distribute throughout all the kingdoms. Among them, mammalian Prx consists of 6 different members grouped into typical 2-Cys, atypical 2-Cys Prx, and 1-Cys Prx. Except Prx VI belonging to 1-Cys Prx subgroup, the other five 2-Cys Prx isotypes have the thioredoxin-dependent peroxidase (TPx) activity utilizing thioredoxin, thioredoxin reductase, and NADPH as a reducing system. Mammalian Prxs are 20 – 30 kilodalton in molecular size and vary in subcellular localization: Prx I, II, and VI in cytosol, Prx III in mitochondria, Prx IV in ER and secretion, Prx V showing complicated distribution including peroxisome, mitochondria and cytosol (1).

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Cyclin D3, ~34kDa, is a member of cyclin D family that promotes cell cycle progression to the DNA systhesis (S) phase. Cyclins complexed with cyclin-dependent kinases(CDKs) mediate phosphorylation of other proteins relevant to cell proliferation. D-type cyclins and their complexing CDKs phosphorylate the retinoblastoma gene product with influences transcription of growth-controlling genes. Cyclin D3 regulates cell proliferation during hematopoiesis, carcinogenesis, and may have function in the terminally differentiated cells. In recent studies, there is reports that cyclin D3 involves in multiple myeloma and malignant precursor T cells.

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Haptoglobin (abbreviated as Hp) is a protein in the blood plasma that binds free hemoglobin released from erythrocytes with high affinity and thereby inhibits its oxidative activity. Hp in its simplest form consists of two α- and two β-chains, connected by disulfide bridges. The chains originate from a common precursor protein which is proteolytically cleaved during protein synthesis. Hp exists in two allelic forms in the human population, so called Hp1 and Hp2; the latter one having arisen due to the partial duplication of Hp1 gene. Three phenotypes of Hp are found in humans: Hp1-1, Hp2-1, and Hp2-2. Hp phenotypes are associated with pathogenesis of a number of human disorders, such as diabetes, cardiovascular disease, etc. Hp plays a role in the host defence responses to infection and inflammation, acting as a natural antagonist for receptor-ligand activation of the immune system, also.

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Platelet-derived growth factors (PDGFs) have been implicated in the control of cell proliferation, survival and migration. The PDGF family of growth factors consists of five different disulphide-linked dimers built up of four different polypeptide chains encoded by four different genes. Theses isoforms, PDGF-AA, PDGF-AB, PDGF-BB, PDGF-CC and PDGF-DD, act via two receptor tyrosine kinases, PDGF receptors α and β. Thus far, gene-targeting experiments have been attempted to create knockout mice deficient for PDGFR-α or PDGFR-β. Those mice, however, died either at the embryonic stage or several days after birth. Platelet-derived growth factor receptors, PDGFR-α and PDGFR-β, have five extracellular immunoglobulin-like domains and an intracellular tyrosine kinase domain. Upon binding a PDGF, the receptors form homo- and heterodimers. Dimerization of the receptors juxtaposes the intracellular part of the receptors, which allow phosphorylation in trans between the two receptors in the complex. These autophosphorylation provide docking sites for downstream signal transduction molecules. More than 10 different SH2–domain-containing molecules have been shown to bind to different autophosphorylation sites in the PDGF α- and β-receptors. There are signal transduction molecules with enzymatic activity, such as PI3-kinase, PLC-γ, Src, SHP-2, GAP, as well as adaptor molecules such as Grb2, Shc, Nck, Grb7 and Crk, and Stats. Each of the different partners recruited by the activated receptor initiates different signaling pathways, making possible a great variety of cellular response.

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Akt(protein kinase B, PKB) is a serine/threonine protein kinase. Akt is activated by PI3 kinase, which is itself activated by tyrosine kinase (Thr308, Ser473). Akt/PKB controls vital cellular functions such as cell survival/apoptosis, cell cycle progression and glucose metabolism. It also acts down-stream from growth factors and hormones.
Akt/PKB can inhibit cell cycle arrest by phosphorylating p21. Also, Akt/PKB may potentiate cell cycle progression through increased translation of cyclin D. Akt/PKB directly affects the apoptosis pathway by, for example, targeting the pro-apoptotic Bcl-2 related protein, BAD. It also can phosphorylate three kinases upstream of SAPK. The SAPK system consists of two groups of kinases, and JNK and p38 MAP kinase pathways. The SAPK pathway is an important target for Akt/PKB regulation to promote cell survival. Akt/PKB is able to regulate cell survival through transcriptional factors(Forkhead, nuclear factor-kB(NF-kB), Murine double minute 2(Mdm2)) that are responsible for pro- as well as anti-apoptotic genes. One of the first physiological targets of PKB to be identified was glycogen synthase kinase-3(GSK3), which has been associated with the control of many cellular processes, including glycogen and protein synthesis, and the modulation of transcription factor activity. The involvement of Akt in disease processes like malignancy, neurodegeneration and abnormal glucose metabolism has also been demonstrated.

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The p90 ribosomal S6 kinases (RSKs) comprise a family of serine/threonine kinases that lie at the terminus of the ERK pathway. In humans, the RSK family consists of four isoforms (RSK1 to -4). RSK family members are unusual among serine/threonine kinases in that they contain two distinct kinase domains, both of which are catalytically functional. Theses kinase dimains are activated in a sequential manner by a series of phosphorylations. RSK regulates gene expression via association and phosphorylation of transcriptional regulators including c-Fos, estrogen receptor, NFkappaB/IkappaB α, cAMP-response element-binding protein (CREB).
ERK activates the C-terminal kinase of RSK, leading to activation of the N-terminal kinase. Members of the RSK family are present in the cytoplasm as well as the nucleus. Addition of growth factor to the cells results in the activation of both cytosolic and nuclear RSK and the translocation of the cytosolic RSK into the nucleus upon activation. The activation and nuclear translocation of RSK result in phosphorylation and activation of transcription factors.

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NF-κB (Nuclear Factor kappa B) is a nuclear transcription factor found in all cell types and is involved in cellular responses to stimuli such as stress, cytokines, free radicals, ultraviolet irradiation, and bacterial or viral antigens. NF-κB plays a key role in regulating the immune response to infection. Consistent with this role, incorrect regulation of NF-κB has been linked to cancer, inflammatory and autoimmune diseases, septic shock, viral infection and improper immune development. There are five members in the NF-κB family: NF-κB1, NF-κB2, RelA (also named p65), RelB, and c-Rel.
The most common form of NF-κB is the p50/RelA heterodimer, although other forms of NF-κB dimers, such as p50/p50, p52/p52, p52/RelA, p50/c-Rel, c-Rel/c-Rel, p52/RelB, and p50/RelB, have also been identified in some types of cells.
The primary role of NF-κB is to maintain normal cellular functions that range from cell-to-cell communication to cell motility, cell cycle progression, and cell lineage development. The activity of NF-κB is tightly regulated by interaction with inhibitory IκB proteins.

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Ubiquitin carboxy-terminal h d l L1 hydrolase (UCHL1) is a deubiqutinating enzyme. Ubiquitin UCHL1, also known as PGP9.5, is a protein of 223 amino acids and one of the most abundant proteins in the brain (1-2% of the total soluble protein). Although it was originally characterized as a deubiquitinating enzyme recent studies indicate that it also functions as a ubiquitin (Ub) ligase and a mono-Ub stabilizer. A large amount of mono-Ub is tightly associated with UCHL1, inhibiting the degradation of mono-Ub in the brain. The precise regulation of UCHL1 is essential for neurons to survive and to maintain their proper function. UCHL1 is involved in the pathogenesis of Parkinson's disease (PD) and Alzheimer's disease (AD). Down-regulation and extensive oxidative modification of UCHL1 have been observed in the brains of AD patients as well as PD patients. A post-translational modification of UCHL1 that controls the function of UCHL1 is mono-ubiquitination. It occurs reversibly to a lysine residue near the active site of UCHL1.

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The human Catecholamine-Sulfating Phenol Sulfotransferase (CSPS) is the only sulfotransferase that catalyses the sulfation of catecholamins, in particular the neurotransmitter dopamine, with high activity. CSPS is required for stimulation by Mn2+ of the sulfating activity and expressed in the human intestine, brain, platelet and other tissues. In the brain it may play a role in regulating the levels of dopamine. It also serves as a detoxifying function in the intestine, where it may detoxify potentially lethal dietary monoamines.

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Coilin is a component of the nuclear Cajar(coiled) bodies (CBs) which are involved in the function or assembly/disassembly of nucleoplasmic snRNPs.
Human coilin is a 576-amino acid protein found enriched in CBs, but is also found in large amounts in the nucleoplasm.
Coilin is a constitutive phosphoprotein that is hyperphosphorylated during mitosis and it is thought that hyperphosphorylation triggers CB disassembly during cell replication. Self-interaction and localization have been shown to depend on the phosphorylation state of coilin.