54781 Wyniki dla: „tripolifosforan+sodu&pageNo=48”

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Chromosome 7 has been linked to Osteogenesis imperfecta, Pendred syndrome, Lissencephaly, Citrullinemia and Shwachman-Diamond syndrome. The deletion of a portion of the q arm of chromosome 7 is associated with Williams-Beuren syndrome, a condition characterised by mild mental retardation, an unusual comfort and friendliness with strangers and an elfin appearance. Deletions of portions of the q arm of chromosome 7 are also seen in a number of myeloid disorders including cases of acute myelogenous leukemia and myelodysplasia. The C7orf57 gene product has been provisionally designated C7orf57 pending further characterisation.

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Granulocyte/macrophage colony-stimulating factors are cytokines that act in hematopoiesis by controlling the production, differentiation, and function of 2 related white cell populations of the blood, the granulocytes and the monocytes-macrophages. This CSF induces granulocytes.

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Probably important in cardiac repolarization. Associates with KCNE1 (MinK) to form the I(Ks) cardiac potassium current. Elicits a rapidly activating, potassium-selective outward current. Muscarinic agonist oxotremorine-M strongly suppresses KCNQ1/KCNE1 current in CHO cells in which cloned KCNQ1/KCNE1 channels were coexpressed with M1 muscarinic receptors. May associate also with KCNE3 (MiRP2) to form the potassium channel that is important for cyclic AMP-stimulated intestinal secretion of chloride ions, which is reduced in cystic fibrosis and pathologically stimulated in cholera and other forms of secretory diarrhea.

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SNARE that may be involved in targeting and fusion of Golgi-derived retrograde transport vesicles with the ER. Required for maintenance of ER network. Implicated in the suppression of cell death.Tissue specificity: Isoform 1 is highly expressed in heart, brain, liver skeletal muscle and pancreas. Isoform 3 is moderately expressed in placenta, lung and kidney. Isoform 4 is highly expressed in testis and small intestine.

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Inhibits the synthesis of a number of cytokines, including IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells.

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May mediate the control of various cellular processes by insulin. When phosphorylated by the insulin receptor binds specifically to various cellular proteins containing SH2 domains such as phosphatidylinositol 3-kinase p85 subunit or GRB2. Activates phosphatidylinositol 3-kinase when bound to the regulatory p85 subunit (By similarity).

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Tubulin family members are globular proteins important in the assembly of microtubules. Microtubules are structural components that play important roles in mitosis, cytokinesis and vesicle transport. TPPP (Tubulin polymerization-promoting protein), also known as p24 and p25, is a widely expressed 219 amino acid protein found in the perinuclear region of the cytoplasm. TPPP may form dimers and functions in polymerizing tubulin into double-walled tubules, polymorphic aggregates, or stabilized blocks. TPPP overexpression prevents formation of the mitotic spindle assembly and breakdown of the nuclear envelope. TPPP is phosphorylated by TPK II and is encoded by a gene that maps to human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome.

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Tau proteins are important Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. Tau proteins subcellular located in the axons of neurons, in the cytoso l and in association with plasma membrane components. It expressed in neurons. PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.

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Signaling adapter that controls various cellular protrusions by regulating actin cytoskeleton dynamics and architecture. Depending on its association with other signal transducers, can regulate different processes. Together with SOS1 and ABI1, forms a trimeric complex that participates in transduction of signals from Ras to Rac by activating the Rac-specific guanine nucleotide exchange factor (GEF) activity. Acts as a direct regulator of actin dynamics by binding actin filaments and has both barbed-end actin filament capping and actin bundling activities depending on the context. Displays barbed-end actin capping activity when associated with ABI1, thereby regulating actin-based motility process: capping activity is auto-inhibited and inhibition is relieved upon ABI1 interaction. Also shows actin bundling activity when associated with BAIAP2, enhancing BAIAP2-dependent membrane extensions and promoting filopodial protrusions. Involved in the regulation of processes such as axonal filopodia growth, stereocilia length, dendritic cell migration and cancer cell migration and invasion. Acts as a regulator of axonal filopodia formation in neurons: in the absence of neurotrophic factors, negatively regulates axonal filopodia formation via actin-capping activity. In contrast, it is phosphorylated in the presence of BDNF leading to inhibition of its actin-capping activity and stimulation of filopodia formation. Component of a complex with DFNB31 and MYO15A that localizes at stereocilia tips and is required for elongation of the stereocilia actin core. Indirectly involved in cell cycle progression; its degradation following ubiquitination being required during G2 phase to promote cell shape changes.

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The protein encoded by this gene is a proton-linked monocarboxylate transporter that catalyzes the movement of many monocarboxylates, such as lactate and pyruvate, across the plasma membrane. Mutations in this gene are associated with erythrocyte lactate transporter defect. Alternatively spliced transcript variants have been found for this gene.

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The transcription factor NFkB is retained in the cytoplasm in an inactive form by the inhibitory protein IkB. Activation of NFkB requires that IkB be phosphorylated on specific serine residues, which results in the targeted degradation of IkB (1). IkB kinase alpha (IKK alpha), previously designated CHUK (2), interacts with IkB-alpha and specifically phosphorylates IkB-alpha on the sites that trigger its degradation, serines 32 and 36 (3). IKKalpha appears to be critical for NFkB activation in response to proinflammatory cytokines (4). Phosphorylation of the IkB by IKK alpha is stimulated by the NFkB inducing kinase (NIK), which itself is a central regulator for NFkB activation in response to TNF and IL-1 (5). The functional IKK complex contains three subunits, IKK alpha, IKK beta and IKK gamma (also designated NEMO), and each appears to make essential contributions to IkB phosphorylation (6). IKAP (IKK-complex-associated protein) is a protein that acts as a scaffold, interacting with NIK, IKK alpha and IKK beta and assembling them into an active kinase complex (7,8)

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HN1L

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Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF and other growth factors. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the interleukin-6 (IL-6)-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. Cytoplasmic STAT3 represses macroautophagy by inhibiting EIF2AK2/PKR activity. Plays an important role in host defense in methicillin-resistant S.aureus lung infection by regulating the expression of the antimicrobial lectin REG3G (By similarity).

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Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) that is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (By similarity). This is the largest subunit of complex I and it is a component of the iron-sulfur (IP) fragment of the enzyme. It may form part of the active site crevice where NADH is oxidized.

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Carries out a dual function: signal transduction and activation of transcription. Involved in IL4/interleukin-4- and IL3/interleukin-3-mediated signaling.

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Key negative regulator of Shh signaling, which promotes the processing of GLI3 into GLI3R during neural tube development. Recruited by TULP3 and the IFT-A complex to primary cilia and acts as a regulator of the PKA-dependent basal repression machinery in Shh signaling by increasing cAMP levels, leading to promote the PKA-dependent processing of GLI3 into GLI3R and repress the Shh signaling. In presence of SHH, it is removed from primary cilia and is internalised into recycling endosomes, preventing its activity and allowing activation of the Shh signaling. Its ligand is unknown (By similarity).

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Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK1 and RIP, are mediators of apoptosis. Two novel serine/threonine kinases that induce apoptosis were recently identified and designated DRAK1 and DRAK2 (for DAP kinase related apoptosis inducing protein kinases). DRAKs contain an N terminal kinase domain and a C terminal regulation domain. Overexpression of DRAK2 induces apoptosis. DRAKs have high sequence homology to DAP and ZIP kinases, and they represent a novel family of serine/threonine kinases, which mediates apoptosis through their catalytic activities. DRAK2 is located in nucleus and the messenger RNA was ubiquitously expressed in human tissues.

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PLEKHM3 (pleckstrin homology domain containing, family M, member 3), also known as DAPR or PLEKHM1L (pleckstrin homology domain containing, family M, member 1-like), is a 761 amino acid phosphoprotein that contains two pleckstrin homology (PH) domains and one phorbol-ester/DAG-type zinc finger. Conserved in chimpanzee, dog, cow, mouse, rat, chicken and zebrafish, PLEKHM3 exists as three alternatively spliced isoforms that participate in metal ion binding. The gene that encodes PLEKHM3 maps to human chromosome 2q33.3. As the second largest human chromosome, chromosome 2 makes up approximately 8% of the human genome and contains 237 million bases encoding over 1,400 genes. Chromosome 2 contains a probable vestigial second centromere, as well as vestigial telomeres, which gives credence to the hypothesis that human chromosome 2 formed as a result of an ancient fusion of two ancestral chromosomes, which are still present in modern day apes.

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Plays a role in a late step of leukocyte extravasation helping cells to overcome the endothelial basement membrane. Acts at the same site as, but independently of, PECAM1 (By similarity). Homophilic adhesion molecule, but these interactions may not be required for cell aggregation (By similarity).

Supplier: Bioss

Stimulates the release of tumor necrosis factor alpha and IL-1-beta from the monocytic cell line THP-1.

Supplier: Bioss

Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by TAU/MAPT localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization.

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Calcium signaling in mitochondria is important in order for it to function in response to a variety of extracellular stimuli. Signaling begins with Ca(2+) entry in mitochondria via the Ca(2+) uniporter followed by Ca(2+) activation of three dehydrogenases in the mitochondrial matrix. ARALAR, the neuronal Ca(2+)-binding mitochondrial aspartate-glutamate carrier, has Ca(2+) binding domains facing the extramitochondrial space and functions in the malate-aspartate NADH shuttle (MAS). ARALAR is encoded by the SLC25A12 gene and is expressed in brain and skeletal muscle. ARALAR is required for the synthesis of brain aspartate and N-acetylaspartatemay and plays a role in myelin formation. It is also essential for the transmission of small Ca(2+) signals to mitochondria via an increase in mitochondrial NADH. In addition, ARALAR is implicated in conferring susceptibility to schizophrenia.

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The AAA ATPase family of molecular chaperones are characterized by a highly conserved AAA motif. Composed of 200-250 residues, the AAA domain contains Walker homology sequences and imparts ATPase activity. Members of the AAA ATPase family act as DNA helicases as well as transcription factors and are thought to be involved in several cellular functions such as cell-cycle regulation, protein proteolysis, organelle biogenesis and vesicle-mediated protein transport. Mitochondrial membrane proteins ATAD3A and ATAD3B contribute to the stabilization of nucleoids which are large mitochondrial DNA (mtDNA)-protein complexes. ATAD3A/B may participate in the transformation pathway and the chemosensitivity of oligodendrogliomas. The genes encoding ATAD3A/B/C maps to human chromosome 1, which houses over 3,000 genes and is the largest human chromosome spanning about 260 million base pairs and making up 8% of the human genome.

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FNDC1, also known as MEL4B3, Ags8, Expressed in synovial lining protein and Activation-associated cDNA protein, is a 1888 amino acid secreted protein that contains five fibronectin type-III domains. FNDC1 is moderately expressed in skeletal muscle, pancreas, heart, kidney, spinal cord, ovary and lung. Expression of FNDC1 is induced in response to hypoxia in ventricular cardiomyocytes. Since FNDC1 interacts with G∫ and G©, it is likely that FNDC1 is an activator for G-protein signaling. Though normally absent in healthy skin, FNDC1 expression is induced by TGF-beta signaling in skin tumors and psoriasis. There are two isoforms of FNDC1 that are produced as a result of alternative splicing events.

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PHC1 is a 1,004 amino acid nuclear protein that is a component of the PcG multiprotein PRC1 complex. Specifically, the PcG PRC1 complex modifies histones, remodels chromatin and mediates monoubiquination of Histone H2A. Other constituent proteins involved in the PcG PRC1 complex are Mel-18, Bmi-1, M33, MPc2, MPc3, RING1, Ring1b, as well as several others. Existing as a homodimer, PHC1 contains one FCS-type zinc finger and a SAM (sterile alpha motif) domain. PHC1 is encoded by a gene located on human chromosome 12, which encodes over 1,100 genes and comprises approximately 4.5% of the human genome.

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IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. Exerts its antiviral activity on a wide range of DNA and RNA viruses including hepatitis C virus (HCV), hepatitis B virus (HBV), measles virus (MV) and herpes simplex virus 1 (HHV-1). Inhibits viral replication via phosphorylation of the alpha subunit of eukaryotic initiation factor 2 (EIF2S1), this phosphorylation impairs the recycling of EIF2S1 between successive rounds of initiation leading to inhibition of translation which eventually results in shutdown of cellular and viral protein synthesis. Also phosphorylates other substrates including p53/TP53, PPP2R5A, DHX9, ILF3, IRS1 and the HHV-1 viral protein US11. In addition to serine/threonine-protein kinase activity, also has tyrosine-protein kinase activity and phosphorylates CDK1 at 'Tyr-4' upon DNA damage, facilitating its ubiquitination and proteosomal degradation. Either as an adapter protein and/or via its kinase activity, can regulate various signaling pathways (p38 MAP kinase, NF-kappa-B and insulin signaling pathways) and transcription factors (JUN, STAT1, STAT3, IRF1, ATF3) involved in the expression of genes encoding proinflammatory cytokines and IFNs. Activates the NF-kappa-B pathway via interaction with IKBKB and TRAF family of proteins and activates the p38 MAP kinase pathway via interaction with MAP2K6. Can act as both a positive and negative regulator of the insulin signaling pathway (ISP). Negatively regulates ISP by inducing the inhibitory phosphorylation of insulin receptor substrate 1 (IRS1) at 'Ser-312' and positively regulates ISP via phosphorylation of PPP2R5A which activates FOXO1, which in turn up-regulates the expression of insulin receptor substrate 2 (IRS2).

Supplier: Bioss

Stress-activated serine/threonine-protein kinase involved in cytokines production, endocytosis, reorganization of the cytoskeleton, cell migration, cell cycle control, chromatin remodeling, DNA damage response and transcriptional regulation. Following stress, it is phosphorylated and activated by MAP kinase p38-alpha/MAPK14, leading to phosphorylation of substrates. Phosphorylates serine in the peptide sequence, Hyd-X-R-X(2)-S, where Hyd is a large hydrophobic residue. Phosphorylates ALOX5, CDC25B, CDC25C, ELAVL1, HNRNPA, HSF1, HSP27/HSPB1, KRT18, KRT2, LIMK1, LSP1, PABPC1, PARN, PDE4A, RCSD1, RPS6KA3, TAB3 and TTP/ZFP36. Mediates phosphorylation of HSP27/HSPB1 in response to stress, leading to dissociate HSP27/HSPB1 from large small heat-shock protein (sHsps) oligomers and impair their chaperone activities and ability to protect against oxidative stress effectively. Involved in inflammatory response by regulating tumor necrosis factor (TNF) and IL6 production post-transcriptionally: acts by phosphorylating AU-rich elements (AREs)-binding proteins ELAVL1, HNRNPA, PABPC1 and TTP/ZFP36, leading to regulate the stability and translation of TNF and IL6 mRNAs. Phosphorylation of TTP/ZFP36, a major post-transcriptional regulator of TNF, promotes its binding to 14-3-3 proteins and reduces its ARE mRNA affinity leading to inhibition of dependent degradation of ARE-containing transcript. Also involved in late G2/M checkpoint following DNA damage through a process of post-transcriptional mRNA stabilization: following DNA damage, relocalizes from nucleus to cytoplasm and phosphorylates HNRNPA and PARN, leading to stabilize GADD45A mRNA. Involved in toll-like receptor signaling pathway (TLR) in dendritic cells: required for acute TLR-induced macropinocytosis by phosphorylating and activating RPS6KA3.

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DZIP1 (DAZ interacting protein 1) is also known as DZIP or DZIP2 and is a 867 amino acid protein which is expressed as three isoforms, designated DZIPb, DZIPt1 and DZIPt2. DZIP1 is localized to testis, oocytes, ovary and fetal brain, as well as in embryonic stem cells and germ cells. In testis, DZIP1 is localized to the nucleus and also shows some cytoplasmic distribution in spermatogonia. DZIP1 belongs to the C2H2-type zinc-finger protein family, and, characteristc of the C2H2-type zinc-finger protein family, DZIP1 contains one C2H2-type zinc-finger region through which it is thought to interact with DAZ, an interaction that promotes spermiogenesis. DZIP1 expression is not found in those afflicted with Sertoli cell-only syndrome (characterized by the absence of germ cells in the testis), suggesting that the lack of DZIP1 may be involved in the pathogenesis of Sertoli cell-only syndrome-induced male sterility.

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Brutons tyrosine kinase (BTK) is a member of the BTK/Tec family of cytoplasmic tyrosine kinases. Like other BTK family members, it contains a pleckstrin homology (PH) domain, Src homology SH3 and SH2 domains. BTK plays an important role in B cell development. Activation of B cells by various ligands is accompanied by BTK membrane translocation mediated by its PH domain binding to phosphatidylinositol-3,4,5-trisphosphate. The membrane located BTK is active and associated with transient phosphorylation of two tyrosine residues, Tyr551 and Tyr223. Tyr551 in the activation loop is transphosphorylated by the Src family tyrosine kinase, leading to autophosphorylation at Tyr223 within the SH3 domain, which is necessary for full activation. The activation of BTK is negatively regulated by PKC beta through phosphorylation of BTK at Ser180, which results in reduced membrane recruitment, transphosphorylation and subsequent activation. The PKC/BTK inhibitory signal is likely to be a key determinant of the B cell receptor signaling threshold to maintain optimal BTK activity.

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C7orf62.