19769 Results for: "1-Naphthyl+phosphate+monosodium+salt+monohydrate"

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MECT1 (also known as MucoEpidermoid Carcinoma Translocated 1, Transducer of regulated cAMP response element-binding protein 1, TORC1, and Transducer of CREB protein 1) is a nuclear protein that functions as a transcriptional coactivator for CREB1, which activates transcription through both consensus and variant cAMP response element (CRE) sites. MECT1does not appear to modulate CREB1 DNA-binding activity but enhances the interaction of CREB1 with TAF4/TAFII-130. MECT1 translocates with MAML2 (MasterMind-Like Protein 2) to yield a fusion oncogene: t(11;19) (q21;p13). This translocation occurs in mucoepidermoid carcinomas, benign Warthin tumors and clear cell hidradenomas. The novel fusion product that results disrupts the Notch signaling pathway. The fusion protein consists of the N-terminus of MECT1 joined to the C-terminus of MAML2. The reciprocal fusion protein consisting of the N-terminus of MAML2 joined to the C-terminus of MECT1 has been detected in a small number of mucoepidermoid carcinomas. Multiple isoforms have been reported for the MECT1 protein.

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Notch is synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase (S1 cleavage) in the trans-golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved (S2 cleavage) by TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called Notch extracellular truncation (NEXT). This fragment is then cleaved by presenilin-dependent gamma-secretase (S3 cleavage) to release the intracellular domain (NICD) from the membrane. Notch functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBP-J kappa and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs.

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TGF-beta-1 is a multifunctional cytokine that belongs to a superfamily of structurally related regulatory proteins, which includes three mammalian TGF-beta isoforms (TGF-beta-1, -beta-2, and -beta-3), activin/inhibins and bone morphogenetic proteins. The most abundant isoform, TGF-beta-1, is a 25 kDa homodimer composed of two 12.5 kDa subunits joined by disulfide bonds. TGF-beta-1 is a highly conserved molecule - the amino acid sequence between human and mouse differ only by one residue. Although originally defined by its ability to cause anchorage independent cell growth and changes in cell morphology of rat fibroblasts, subsequent research has revealed that TGF-beta is actually a major growth inhibitor for most cell types. It is produced by a wide variety of cell and tissue types during all stages of cell differentiation. TGF-beta-1 sources include platelets, bone and soft tissues such as placenta and kidneys.

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RPS6KB1 phosphorylates the Ribosomal Protein-S6. Activation of RPS6KB1 requires a complex, ordered series of conformational changes and phosphorylation reactions. While the role of sequential, multi-site phosphorylation has been extensively detailed, characterization of the priming step required to initiate this cascade has remained elusive. Probably this priming process is dependent on calcium. Calcium-dependent regulation of RPS6KB1 does not specifically target Thr-229 and Thr-389, the key regulatory phosphorylation sites; rather, calcium chelation results in a global inhibition of RPS6KB1 phosphorylation. The initial calcium-dependent process is required to release an inhibitory interaction between the C- and N-termini of RPS6KB1, thus allowing phosphorylation of key domains. The priming event involves formation of a calcium-dependent protein complex that releases the interaction between the N- and C-termini. RPS6KB1 is then accessible for activation by the kinases that target the known regulatory phosphorylation sites.

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Signal transducer and activator of transcription that mediates signaling by interferons (IFNs). Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state.

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Signaling adapter that couples activated growth factor receptors to signaling pathway. Isoform p46Shc and isoform p52Shc, once phosphorylated, couple activated receptor tyrosine kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p46Shc and isoform p52Shc may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span

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Myc proto-oncogene encodes nuclear DNA-binding phosphoproteins that are involved in the regulation of gene expression and DNA replication during cell growth and differentiation. Myc encodes a protein of 65 kDa which is expressed in almost all normal and transformed cells. The expression correlates with the proliferation state of the cells. Transcription is repressed in quiescent or terminally differentiated cells. Expression of Myc is generally induced after mitogenic stimulation of cells or serum induction. Myc therefore is an important positive regulator of cell growth and proliferation. Myc has been demonstrated also to be a potent inducer of apoptosis when expressed in the absence of serum or growth factors. Apoptosis may serve also as a protective mechanism to prevent tumorigenicity elicited by deregulated Myc expression. Sequences of the Myc oncogene have been highly conserved throughout evolution, from Drosophila to vertebrates

Supplier: MP Biomedicals

Chromium potassium sulfate is the potassium double sulfate of chromium.

Supplier: ProSci Inc.

Myc proto-oncogene encodes nuclear DNA-binding phosphoproteins that are involved in the regulation of gene expression and DNA replication during cell growth and differentiation. Myc encodes a protein of 65 kDa which is expressed in almost all normal and transformed cells. The expression correlates with the proliferation state of the cells. Transcription is repressed in quiescent or terminally differentiated cells. Expression of Myc is generally induced after mitogenic stimulation of cells or serum induction. Myc therefore is an important positive regulator of cell growth and proliferation. Myc has been demonstrated also to be a potent inducer of apoptosis when expressed in the absence of serum or growth factors. Apoptosis may serve also as a protective mechanism to prevent tumorigenicity elicited by deregulated Myc expression. Sequences of the Myc oncogene have been highly conserved throughout evolution, from Drosophila to vertebrates

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Signaling adapter that couples activated growth factor receptors to signaling pathway. Isoform p46Shc and isoform p52Shc, once phosphorylated, couple activated receptor tyrosine kinases to Ras via the recruitment of the GRB2/SOS complex and are implicated in the cytoplasmic propagation of mitogenic signals. Isoform p46Shc and isoform p52Shc may thus function as initiators of the Ras signaling cascade in various non-neuronal systems. Isoform p66Shc does not mediate Ras activation, but is involved in signal transduction pathways that regulate the cellular response to oxidative stress and life span. Isoform p66Shc acts as a downstream target of the tumor suppressor p53 and is indispensable for the ability of stress-activated p53 to induce elevation of intracellular oxidants, cytochrome c release and apoptosis. The expression of isoform p66Shc has been correlated with life span

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Myosin is the major component of thick muscle filaments, and is a long asymmetric molecule containing a globular head and a long tail. The molecule consists of two heavy chains each ~200,000 daltons, and four light chains each ~16,000 - 21,000 daltons. Activation of smooth and cardiac muscle primarily involves pathways that increase calcium and myosin phosphorylation resulting in contraction. Myosin light chain phosphatase acts to regulate muscle contraction by dephosphorylating activated myosin light chain. The selected peptide sequence used to generate the polyclonal antibody is located near the amino terminal end of the polypeptide corresponding to the smooth/non-muscle form of myosin regulatory light chain found in cardiac myocytes in addition to smooth and non-muscle cells. This sequence differs from that of the sarcomeric/ cardiac form of myosin regulatory light chain that has a different sequence around the phosphorylation site. Human, mouse and rat have almost identical sequences.

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NMDA receptors are members of the ionotropic class of glutamate receptors, which also includes Kainate and AMPA receptors. NMDA receptors consist of NR1 subunits combined with one or more NR2 (A-D) or NR3 (A-B) subunits. The ligand-gated channel is permeable to cations including Ca2+, and at resting membrane potentials NMDA receptors are inactive due to a voltage-dependent blockade of the channel pore by Mg2+. NMDA receptor activation, which requires binding of glutamate and glycine, leads to an influx of Ca2+ into the postsynaptic region where it activates several signaling cascades, including pathways leading to the induction of long-term potentiation (LTP) and depression (LTD). NMDA receptors have a critical role in excitatory synaptic transmission and plasticity in the CNS. They govern a range of physiological conditions including neurological disorders caused by excitotoxic neuronal injury, psychiatric disorders and neuropathic pain syndromes.

Supplier: G-Biosciences

Streptavidin Resin is designed for the single step small and large scale affinity purification of proteins and antibodies with a biotin tag. Biotin, a 244 Da vitamin (Vitamin H) molecule, exhibits an extraordinary binding affinity for avidin (Ka=10¹⁵ M⁻¹) and streptavidin (Ka=10¹⁵ M⁻¹). Biotin and (strept)avidin interaction is rapid and once the bond is established it can survive up to 3M guanidinehydrochloride and extremes of pH. Biotin-avidin bonds can only be reversed by denaturing the avidin protein molecule with 8M guanidine-hydrochloride at pH 1,5 or by autoclaving. The biotinylated molecules are efficiently probed with avidin or streptavidin conjugated to reporter molecules, such as peroxidases or phosphatases.

Supplier: Ahlstrom-Munksjö

Ahlstrom-Munksjö’s qualitative grades of filter paper are recommended for use in analytical methods which determine or identify particulate constituents of a mixture irrespective of the amount present. Qualitative filter papers are often used in routine separation work that still requires high purity and consistent performance. These filter papers covers a wide range of laboratory applications, as liquids clarification, qualitative analytical separations for precipitates and buffers filtration, and are also used for soil analysis and in food and beverage testing. Wet-strengthened grades contain a reinforcement agent that increases their resistance to rupture when wet, such as in vacuum filtration, and their resistance when filtering acidic solutions. High Purity hardened filter papers grades 1288 to 1291 are also produced from cellulose with an alpha content of nearly 100% resulting in an ash content of <0,1%.

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Signal transducer and activator of transcription that mediates signaling by interferons (IFNs). Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state.

Supplier: ProSci Inc.

Acts as a 'translational enhancer', driving specific mRNAs to polysomes and thus increasing the efficiency of protein synthesis. Its association with the translational machinery and target mRNAs results in an increased number of initiation events per molecule of mRNA and, indirectly, in stabilizing the mRNAs. Binds IGF2 mRNA, MYOD1 mRNA, ARBP/36B4 ribosomal protein mRNA and its own mRNA. Essential for skeletal muscle differentiation program through the translational up-regulation of IGF2 expression. Acts as a suppressor of microRNA (miRNA) biogenesis by specifically binding the precursor let-7 (pre-let-7), a miRNA precursor. Acts by binding pre-let-7 and recruiting ZCCHC11/TUT4 uridylyltransferase, leading to the terminal uridylation of pre-let-7. Uridylated pre-let-7 miRNAs fail to be processed by Dicer and undergo degradation. Degradation of pre-let-7 in embryonic stem (ES) cells contributes to the maintenance of ES cells.

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Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.

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Histone Deacetylases (HDACs) are a group of enzymes closely related to sirtuins. They catalyze the removal of acetyl groups from lysine residues in histones and non-histone proteins, resulting in transcriptional repression. In general, they do not act autonomously but as components of large multiprotein complexes, such as pRb-E2F and mSin3A, that mediate important transcription regulatory pathways. There are three classes of HDACs; classes 1, 2 and 4, which are closely related Zn2+-dependent enzymes. HDACs are ubiquitously expressed and they can exist in the nucleus or cytosol. Their subcellular localization is effected by protein-protein interactions (for example HDAC-14.3.3 complexes are retained in the cytosol) and by the class to which they belong (class 1 HDACs are predominantly nuclear whilst class 2 HDACs shuttle between the nucleus and cytosol). HDACs have a role in cell growth arrest, differentiation and death and this has led to substantial interest in HDAC inhibitors as possible antineoplastic agents.

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Signal transducer and activator of transcription that mediates signaling by interferons (IFNs). Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, Jak kinases (TYK2 and JAK1) are activated, leading to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize, associate with ISGF3G/IRF-9 to form a complex termed ISGF3 transcription factor, that enters the nucleus. ISGF3 binds to the IFN stimulated response element (ISRE) to activate the transcription of interferon stimulated genes, which drive the cell in an antiviral state. In response to type II IFN (IFN-gamma), STAT1 is tyrosine- and serine-phosphorylated. It then forms a homodimer termed IFN-gamma-activated factor (GAF), migrates into the nucleus and binds to the IFN gamma activated sequence (GAS) to drive the expression of the target genes, inducing a cellular antiviral state.

Supplier: ProSci Inc.

NMDA receptors are members of the ionotropic class of glutamate receptors, which also includes Kainate and AMPA receptors. NMDA receptors consist of NR1 subunits combined with one or more NR2 (A-D) or NR3 (A-B) subunits. The ligand-gated channel is permeable to cations including Ca2+, and at resting membrane potentials NMDA receptors are inactive due to a voltage-dependent blockade of the channel pore by Mg2+. NMDA receptor activation, which requires binding of glutamate and glycine, leads to an influx of Ca2+ into the postsynaptic region where it activates several signaling cascades, including pathways leading to the induction of long-term potentiation (LTP) and depression (LTD). NMDA receptors have a critical role in excitatory synaptic transmission and plasticity in the CNS. They govern a range of physiological conditions including neurological disorders caused by excitotoxic neuronal injury, psychiatric disorders and neuropathic pain syndromes.

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ATF4 encodes a transcription factor that was originally identified as a widely expressed mammalian DNA bindingprotein that could bind a tax-responsive enhancer element in the LTR of HTLV-1. The encoded protein was also isolated and characterized as the cAMP-response element binding protein 2 (CREB-2). The protein encoded by this gene belongs to a family of DNA-binding proteins that includes the AP-1 family of transcription factors, cAMP-response element binding proteins (CREBs) and CREB-like proteins. These transcription factors share a leucine zipper region that is involved in protein-protein interactions, located C-terminal to a stretch of basic amino acids that functions as a DNA binding domain. Two alternative transcripts encoding the same protein have been described. Two pseudogenes are located on the X chromsome at q28 in a region containing a large inverted duplication.

Supplier: Thermo Fisher Scientific

Ammonium cerium(IV) sulphate dihydrate 95% ACS

Supplier: Honeywell Chemicals

Ammonium cerium(IV) sulphate dihydrate ≥98.0% (RT), Puriss. p.a. ACS, Fluka™

Supplier: MP Biomedicals

Pure Canavalia ensiformis lectin (Con A) from Jackbean.

Supplier: Thermo Fisher Scientific

Ammonium iron(III) sulphate dodecahydrate 99% ACS

Supplier: Cytiva

The illustra™ plasmidPrep Mini Spin Kit uses a simple plasmid DNA purification protocol involving a modified alkaline lysis procedure and a novel silica-based membrane to achieve highly efficient plasmid DNA purification. Produces high quality plasmid DNA with excellent reproducibility for use in cloning, restriction enzyme digestion, PCR amplification, and DNA sequencing.

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Cell Culture Reagent Anhydrous 1 * 1 kg

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p53 is a nuclear protein which plays an essential role in the regulation of cell cycle specifically in the transition from G0 to G1. It is found in very low levels in normal cells however in a variety of transformed cell lines in high amounts and believed to contribute to transformation and malignancy. The open reading frame of p53 is 393 amino acids long, with the central region (consisting of amino acids from about 100 to 300) containing the DNA-binding domain. This proteolysis-resistant core is flanked by a C-terminal end mediating oligomerization and an N-terminal end containing a strong transcription activation signal. p53 binds as a tetramer to a PBS (p53-Binding Site) and activates the expression of downstream genes that inhibit growth and/or invasion. p53 binds as a tetramer to a p53-binding site (PBS) and to activate the expression of adjacent genes that inhibit growth and/or invasion. Deletion of one or both p53 alleles reduces the expression of tetramers, resulting in decreased expression of the growth inhibitory genes

Supplier: Abnova

Mouse monoclonal antibody raised against rat Camk2a. 1 * 100 µG

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eIF4F is a multi-subunit complex, the composition of which varies with external and internal environmental conditions. It is composed of at least EIF4A, EIF4E and EIF4G1/EIF4G3. Interacts with eIF3, mutually exclusive with EIF4A1 or EIFA2, EIF4E and through its N-terminus with PAPBC1. Interacts through its C-terminus with the serine/threonine kinases MKNK1, and with MKNK2. Appears to act as a scaffold protein, holding these enzymes in place to phosphorylate EIF4E. Non-phosphorylated EIF4EBP1 competes with EIF4G1/EIF4G3 to interact with EIF4E; insulin stimulated MAP-kinase (MAPK1 and MAPK3) phosphorylation of EIF4EBP1 causes dissociation of the complex allowing EIF4G1/EIF4G3 to bind and consequent initiation of translation. EIF4G1/EIF4G3 interacts with PABPC1 to bring about circularization of the mRNA. Rapamycin can attenuate insulin stimulation mediated by FKBPs. Interacts with EIF4E3. Interacts with MIF4GD. Interacts with rotavirus A NSP3; in this interaction, NSP3 takes the place of PABPC1 thereby inducing shutoff of host protein synthesis