15877 Results for: "Sodium+peroxide"

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General protein kinase capable of phosphorylating several known proteins. Phosphorylates TBC1D4. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). Plays a role in glucose transport by mediating insulin-induced translocation of the GLUT4 glucose transporter to the cell surface. Mediates the antiapoptotic effects of IGF-I. Mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. Promotes glycogen synthesis by mediating the insulin-induced activation of glycogen synthase.

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Key regulator of entry into cell division that acts as a tumor suppressor. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.

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ALAS-1 (EC 2.3.1.37) is a nuclear-encoded mitochondrial matrix enzymecatalyzing the condensation of glycine with succinyl-CoA to form delta-amino levulinate, CO2 and CoA. It regulates the first and rate-limiting step of heme biosynthetic pathway. It is one of the two isoforms of ALAS and is a pyridoxal-5 phosphate dependant housekeeping enzyme. It is ubiquitously expressed and is responsible of providing heme for cytochromes and other hemoproteins. ALAS1 in liver undergoes negative feedback regulation by heme. Transcription of ALAS1 gene is stimulated by cAMP and respiratory uncoupling whereas Phorbol esters and insulin repress ALAS1 gene expression. ALAS1 is suggested to be involved in reciprocal regulation of Heme biosynthesis and circadian clock suggesting a potential target for treatment of circadian disorders. ALAS1 gene expression is down regulated in Acute Liver failure resulting in altered heme metabolism and liver function.

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CCL4 Antibody: CCL4, also known as macrophage inflammatory protein 1-beta (MIP1B), belongs to the intercrine beta (chemokine CC) family. Both CCL4 and the related protein CCL3 participate in the host response to invading bacterial, viral, parasite and fungal pathogens by regulating the trafficking and activation state of selected subgroups of inflammatory cells. While both CCL4 and CCL3 exert similar effects on monocytes, their effect on lymphocytes differ; with CCL4 selectively attracting CD4+ lymphocytes and CCL3 selectively attracting CD8+ lymphocytes. Additionally, both have been shown to be potent chemoattractants for B cells, eosinophils and dendritic cells. The processed form of CCL4 can induce down-modulation of surface expression of the chemokine receptor CCR5, thus inhibiting the CCR5-mediated entry of HIV-1 in T cells.

Supplier: Biotium

Near-infrared CF™ dye antibodies are affinity-purified antibodies labeled with near-infrared fluorescent CF™750 or CF™770, two members of the novel CF™ dye series developed by Biotium for labeling proteins and other biomolecules. CF™ dyes are designed to offer advantages in brightness, photostability, and/or specificity compared to other commercial dyes, and are available in colors spanning the visible, far-red, and near-infrared spectra.

Supplier: Biotium

Near-infrared CF™ dye antibodies are affinity-purified antibodies labeled with near-infrared fluorescent CF™750 or CF™770, two members of the novel CF™ dye series developed by Biotium for labeling proteins and other biomolecules. CF™ dyes are designed to offer advantages in brightness, photostability, and/or specificity compared to other commercial dyes, and are available in colors spanning the visible, far-red, and near-infrared spectra.

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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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GFP (Green fluorescence protein) is a 27 kDa protein derived from the jellyfish Aequorea victoria, which emits green light when excited by blue light. GFP cDNA produces a fluorescent product when expressed in prokaryotic cells, without the need for exogenous substrates or cofactors. GFP has become an invaluable tool in cell biology research, since its intrinsic fluorescence can be visualized in living cells. GFP fluorescence is stable under fixation conditions and suitable for a variety of applications. GFP has been widely used as a reporter for gene expression, enabling researchers to visualize and localize GFP-tagged proteins within living cells without the need for chemical staining. Other applications of GFP include assessment of protein protein interactions through the yeast two hybrid system and measurement of distance between proteins through fluorescence energy transfer (FRET) protocols. GFP technnology has considerably contributed to a greater understanding of cellular physiology.

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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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Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3, 4, 5-trisphosphate, phosphatidylinositol 3, 4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1, 3, 4, 5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3, 4, 5)P3 > PtdIns(3, 4)P2 > PtdIns3P > Ins(1, 3, 4, 5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue.

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INHA(A-inhibin subunit precursor, inhibin alpha subunit ),also called inhibin(alpha) ,which is located on chromosome 2q33-q36. Inhibin is a gonadal protein that preferentially suppresses the secretion of pituitary follicle-stimulating hormone (FSH). Inhibin comprises of two subunits,Inhibin A and B. Inhibin has been shown to regulate gonadal stromal cell proliferation negatively and to have tumor suppressor activity. In addition, serum levels of inhibin have been shown to reflect the size of granulosa cell tumors and can therefore be used as a marker for primary as well as recurrent disease. In addition to their role in endocrine feedback in the reproductive sytem, inhibins subserve local regulatory roles in numerous extragonadal tissues, including brain, adrenal,bone marrow, placenta, and most notably anterior pituitary. Inhibin alpha subunit gene expression is down regulated in human prostate cancer, suggesting a tumor suppressive role.

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The transcription factor ELK1 is a family of member of ETS oncogene family and of the ternary complex factor (TCF) subfamily,which is located on chromosome Xp11.2 and stimulates transcription. binds to purine-rich DNA sequences. Proteins of the TCF subfamily form a ternary complex by binding to the the serum response factor and the serum reponse element in the promoter of the c-fos proto-oncogene. The protein encoded by this gene is a nuclear target for the ras-raf-MAPK signaling cascade. Elk1 is phosphorylated by MAP kinase pathways at a cluster of S/T motifs at its C terminus,It appears to be a direct target of activated MAP kinase. Biochemical studies indicate that Elk1 is a good substrate for MAP kinase, the kinetics of Elk1phosphorylation and activation correlate with MAP kinase activity, and interfering mutants of MAP kinase block Elk1 activation in vivo. More recent studies have shown that Elk1 is also a target of the Stress Activated Kinase SAPK/JNK. Phosphorylation of Elk1 has also been implicated in synaptic plasticity in the adult hippocampus.

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The transcription factor ELK1 is a family of member of ETS oncogene family and of the ternary complex factor (TCF) subfamily,which is located on chromosome Xp11.2 and stimulates transcription. binds to purine-rich DNA sequences. Proteins of the TCF subfamily form a ternary complex by binding to the the serum response factor and the serum reponse element in the promoter of the c-fos proto-oncogene. The protein encoded by this gene is a nuclear target for the ras-raf-MAPK signaling cascade. Elk1 is phosphorylated by MAP kinase pathways at a cluster of S/T motifs at its C terminus,It appears to be a direct target of activated MAP kinase. Biochemical studies indicate that Elk1 is a good substrate for MAP kinase, the kinetics of Elk1phosphorylation and activation correlate with MAP kinase activity, and interfering mutants of MAP kinase block Elk1 activation in vivo. More recent studies have shown that Elk1 is also a target of the Stress Activated Kinase SAPK/JNK. Phosphorylation of Elk1 has also been implicated in synaptic plasticity in the adult hippocampus.

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FER (fer tyrosine kinase) is a member of the FPS/FES family of nontransmembrane receptor tyrosine kinases, which shares a functional domain and is involved in signaling pathways through receptor tyrosine kinases (RTK) and cytokine receptors. The Fes /Fps family is distinct from c-Src, c-Abl and related nRTKs and was originally distinguished as a homolog to retroviral oncoproteins. In vivo, Fer kinase assembles into homotrimers via conserved coiled-coil domains. The N-terminal coiled-coil domains of Fer can autophosphorylate in trans, thereby regulating their cellular function through differential phosphorylation states. Growth factor exposure can induce tyrosine phosphorylation of Fer and recruitment of Fer to RTK complexes containing p85. It is expressed predominantly in mature hematopoietic cells of the granulocytic and monocytic lineage, and has been shown to be expressed in vascular endothelial cells. Fer is implicated in insulin signaling, cell-cell signaling, human prostatic proliferative diseases, and is involved in the regulation of G1 progression.

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MYST1 (MYST histone acetyltransferase 1,MOF) belongs to the MYST family of histone acetyltransferases, which are employed in the cell to bring about transcriptional regulation. The MYST family includes MYST1, is named for the founding members MOZ, yeast YBF2 and SAS2, and TIP60. All members of this family contain a MYST region of about 240 amino acids with a canonical acetyl-CoA-binding site and a C2HC-type zinc finger motif. Most MYST proteins also have a chromodomain involved in protein- protein interactions and targeting transcriptional regulators to chromatin. Although MOF is expressed in both males and females, it associates with the X chromosome only in males. MOF contains a zinc-finger domain that is used to contact the globular part of the nucleosome and histone H4. The carboxy terminal domain of human MOF also has histone acetyltransferase activity directed against histones H3 and H2A, a characteristic shared with other MYST family histone.

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SORL1 (sortilin-related receptor, L A repeats containing) also known as sorting protein-related receptor containing LDLR class A (SorLA), is a Type I membrane protein that may be involved in cell-cell interaction. SorLA, a single transmembrane receptor, binds LDL and transports it into cells by endocytosis. SorLA is synthesized as a proreceptor which is processed to the mature form by a furin-like propeptidase. It can also bind to RAP (receptor-associated protein). SorLA is a multifunctional endocytis receptor important in lipoprotein and protease uptake. The N-terminal propeptide, which is removed, can be cleaved by furin or homologous proteases. Endogenous SorLA binds the neuropeptide head activator (HA) and is important for HA signaling and function. The gene encoding for the protein maps to chromosome 8p23.1. SorLA is expressed mainly in brain (cerebral cortex, cerebellum and the occipital pole), but can also be found in liver, spinal cord, kidney, testis and pancreas.

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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

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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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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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Tumor suppressor. Acts as a dual-specificity protein phosphatase, dephosphorylating tyrosine-, serine- and threonine-phosphorylated proteins. Also acts as a lipid phosphatase, removing the phosphate in the D3 position of the inositol ring from phosphatidylinositol 3, 4, 5-trisphosphate, phosphatidylinositol 3, 4-diphosphate, phosphatidylinositol 3-phosphate and inositol 1, 3, 4, 5-tetrakisphosphate with order of substrate preference in vitro PtdIns(3, 4, 5)P3 > PtdIns(3, 4)P2 > PtdIns3P > Ins(1, 3, 4, 5)P4. The lipid phosphatase activity is critical for its tumor suppressor function. Antagonizes the PI3K-AKT/PKB signaling pathway by dephosphorylating phosphoinositides and thereby modulating cell cycle progression and cell survival. The unphosphorylated form cooperates with AIP1 to suppress AKT1 activation. Dephosphorylates tyrosine-phosphorylated focal adhesion kinase and inhibits cell migration and integrin-mediated cell spreading and focal adhesion formation. May be a negative regulator of insulin signaling and glucose metabolism in adipose tissue.

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HOX11, also called homeobox11 or Tcl-3 is located at the 10q24 T-Cell translocation breakpoint region. It encodes a homeobox-domain containing protein, HOX11, containing a glycine and proline-rich amino terminus. HOX11 is required for maintenance of the developing spleen and cell survival. The HOX11protein binds to a specific DNA sequence and localizes to the cell nucleus. It transactivates transcription of a reporter gene linked to a cis-regulatory element, acting as a positive transcription activator. The HOX11 gene is highly expressed in T-ALLs as a result of a t (7:10) (q35;q24) or t(10:14)(q24;qll) translocation. The homeobox gene is deregulated upon translocation into the T-cell receptor locus and activates a specific subset of tumor-associated target genes. HOX 11 gene translocation has been attributed to T-cell leukemia and lymphoid neoplasias.

Supplier: Thermo Fisher Scientific

Thermo Scientific™ GlycoLink IP Kit provides components for effective immunoprecipitation (IP and co-IP) based on small-scale, covalent, affinity-resin immobilisation of antibodies and other glycoproteins via oxidised sugar groups.

Supplier: Thermo Fisher Scientific

The Zeba™ spin desalting plates are polypropylene devices containing high-performance Zeba™ desalting resin, offering rapid protein desalting with high recovery of proteins >7000 daltons. Zeba™ desalting devices provide trouble-free desalting and buffer exchange for sample volumes ranging from 2 µl to 4 ml. The 96-well spin plate format enables more high-throughput processing. Zeba™ 96-well spin desalting plates require no resin dispensing or hydration and provide the same high protein recovery as spin columns with at least 95% removal of salts and other small molecules.

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Vimentin is the major subunit protein of the intermediate filaments of mesenchymal cells. It is believed to be involved with the intracellular transport of proteins between the nucleus and plasma membrane. Vimentin has been implicated to be involved in the rate of steroid synthesis via its role as a storage network for steroidogenic cholesterol containing lipid droplets. Vimentin phosphorylation by a protein kinase causes the breakdown of intermediate filaments and activation of an ATP and myosin light chain dependent contractile event. This results in cytoskeletal changes that facilitate the interaction of the lipid droplets within mitochondria, and subsequent transport of cholesterol to the organelles leading to an increase in steroid synthesis. Immunohistochemical staining for Vimentin is characteristic of sarcomas (of neural, muscle and fibroblast origin) compared to carcinomas which are generally negative. Melanomas, lymphomas and vascular tumors may all stain for Vimentin. Vimentin antibodies are thus of value in the differential diagnosis of undifferentiated neoplasms and malignant tumors. They are generally used with a panel of other antibodies including those recognising cytokeratins, lymphoid markers, S100, desmin and neurofilaments.

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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.

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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.