192247 Results for: "Nucleic+Acid+Purification+Kits+and+Reagents&pageNo=50&view=easy"

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MICROSYRINGE 50µL GAS ANALYSIS MS/GF INTERCHANGEABLE NEEDLE 1 * 1 items

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BOTTLE LDPE WIDE NECK 50ML W/GASKET 1 * 160 items

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Density hydrometer, 1,060-1,120:0,001g/cm , ref. temp. 20C, with therm., 350mm long, special liquid 1 * 1 items

Supplier: Amarell

Soil therm., British type, similar specification, right angle, -7+38:0,5C, solid stem, white backed, red special liquid, round bulb with diameter 11,5-14,0mm, built-in length 75mm (MK2B), lower part 100mm, suitable for government verification 1 * 1 items

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An integrated ultrapure and pure water system that is intelligent, easy to use and environmentally friendly.

Supplier: Bioss

Chk2 is a serine/threonine kinase involved in the control of cell cycle checkpoints, and may also participate in transduction of the DNA damage and replicational stress signals. Chk2 is the mammalian ortholog of the budding yeast Rad53 and fission yeast Cds1 checkpoint kinases. The amino-terminal domain of Chk2 contains a series of seven serine and threonine residues (Ser19, Thr26, Ser28, Ser33, Ser35, Ser50 and Thr68) followed by glutamine (SQ or TQ motif). These are known to be preferred sites for phosphorylation by ATM/ATR kinases. Indeed, after DNA damage by ionizing radiation (IR), UV irradiation or hydroxyurea treatment, Thr68 and other sites in this region become phosphorylated by ATM/ATR. The SQ/TQ cluster domain, therefore, seems to have a regulatory function. Phosphorylation at Thr68 is a prerequisite for the subsequent activation step, which is attributable to autophosphorylation of Chk2 on residues Thr383 and Thr387 in the activation loop of the kinase domain. Chk2 inhibits CDC25C phosphatase by phosphorylating it on Ser-216, preventing the entry into mitosis. This kinase may have a role in meiosis as well. Kinase activity is up regulated by autophosphorylation and the protein is rapidly phosphorylated in response to DNA damage and to replication block.

Supplier: Bioss

C1orf85, also known as Lysosomal protein NCU-G1, is a 406 amino acid single-pass membrane protein that is highly glycosylated on its amino-terminal end. Transcription of the gene encoding C1orf85 is activated by TFEB, a transcription factor that specifically recognizes and binds E-box sequences. There are two isoforms of C1orf85 that are produced as a result of alternative splicing events. The C1orf85 maps to human chromosome 1, the largest human chromosome spanning about 260 million base pairs and making up 8% of the human genome. There are about 3,000 genes on chromosome 1, and considering the great number of genes there are also a large number of diseases associated with chromosome 1. Notably, the rare aging disease Hutchinson-Gilford progeria is associated with the LMNA gene which encodes lamin A. When defective, the LMNA gene product can build up in the nucleus and cause characteristic nuclear blebs. The mechanism of rapidly enhanced aging is unclear and is a topic of continuing exploration. The MUTYH gene is located on chromosome 1 and is partially responsible for familial adenomatous polyposis. Stickler syndrome, Parkinsons, Gaucher disease and Usher syndrome are also associated with chromosome 1.

Supplier: Bioss

The GGA family of proteins (Golgi-localized, ARF-binding proteins) are ubiquitous coat proteins that facilitate the trafficking of soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions with TGN-sorting receptors, ARF (ADP-ribosylation factor), and clathrin (1?). Members of the GGA family, GGA1,GGA2 (also known as VEAR) and GGA3, are multidomain proteins that bind mannose 6-phosphate receptors (MPRs) (1,2,4). GGAs have modular structures with an N-terminal VHS (VPS-27, Hrs, and STAM) domain followed by a GAT (GGA and TOM1) domain, a connecting hinge segment, and a C-terminal GAE (?adaptin ear) domain (5). The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic domains of sorting receptors by recognizing acidic-cluster di-leucine (ACLL) sequences (3). GGA1 and GGA2 do not associate with each other, but they do colocalize on perinuclear membranes (2). The cytosolic domain of memapsin 2, but not that of memapsin 1, binds the VHS domains of GGA1 and GGA2 (6). The human GGA1 gene maps to chromosome 22 and encodes a protein that shares 45% sequence identity with GGA2 and GGA3 (1).

Supplier: Bioss

The GGA family of proteins (Golgi-localized, ARF-binding proteins) are ubiquitous coat proteins that facilitate the trafficking of soluble proteins from the trans-Golgi network (TGN) to endosomes/lysosomes by means of interactions with TGN-sorting receptors, ARF (ADP-ribosylation factor), and clathrin (1?). Members of the GGA family, GGA1,GGA2 (also known as VEAR) and GGA3, are multidomain proteins that bind mannose 6-phosphate receptors (MPRs) (1,2,4). GGAs have modular structures with an N-terminal VHS (VPS-27, Hrs, and STAM) domain followed by a GAT (GGA and TOM1) domain, a connecting hinge segment, and a C-terminal GAE (?adaptin ear) domain (5). The amino-terminal VHS domains of GGAs form complexes with the cytoplasmic domains of sorting receptors by recognizing acidic-cluster di-leucine (ACLL) sequences (3). GGA1 and GGA2 do not associate with each other, but they do colocalize on perinuclear membranes (2). The cytosolic domain of memapsin 2, but not that of memapsin 1, binds the VHS domains of GGA1 and GGA2 (6). The human GGA1 gene maps to chromosome 22 and encodes a protein that shares 45% sequence identity with GGA2 and GGA3 (1).

Supplier: Bioss

Members of the NFAT (nuclear factor of activated T cells) family of transcription factors are related to NFkB/Rel proteins and form cooperative complexes with the AP-1 proteins, Fos and Jun, on DNA to regulate cytokine expression in T cells. NFAT proteins are widely expressed and alternatively modified to generate splice variants, and they are localized to both the cytosol (NFATc) and to the nucleus (NFATn). NFAT1, NFAT2, and NFAT4 are predominantly expressed in immune cells, and NFAT2 and NFAT3 are expressed at high levels in cardiac tissues. In addition to activating cytokine gene transcription, NFAT2 is also implicated in cardiac valve development, and NFAT3 is involved in cardiac hypertrophy. NFAT5 is detected in both immune and nonimmune cells and, like other NFAT proteins, contains a highly conserved Rel-like binding domain that mediates NFAT proteins associating with specific consensus sequences on DNA. NFAT proteins are activated by increases in intracellular calcium, which leads to the calmodulin-dependent phosphatase, calcineurin, dephosphorylating NFAT proteins. This activating event induces a conformational change in the protein structure that exposes the nuclear localization signal and facilitates the translocation of NFAT proteins from the cytosol into the nucleus.

Supplier: Bioss

The LIM-only (LMO) proteins, LMO1 and LMO2, are nuclear factors that are characterized by a conserved LIM domain (1). The LIM domain consists of a cysteine-rich zinc-binding motif that is present in a variety of transcription factors, including the LIM homeobox (LHX) proteins expressed in the central nervous system and involved in cell differentiation (2). LMO1 and LMO2 are expressed in the adult CNS in a cell type-specific manner, where they are differentially regulated by neuronal activity and are involved in regulating the cellular differentiated phenotype of neurons (3). LMO2 lacks a specific DNA-binding homeobox domain but rather assembles into transcriptional regulatory complexes to mediate gene expression by interacting with the widely expressed nuclear LIM interactor (NLI) (4). NLI, known also as CLIM-1, and the related protein CLIM-2 facilitate the formation of heteromeric LIM complexes and also enhance the nuclear retention of LIM proteins (5). LMO2 and the related protein LMO4 are expressed in thymic precursor cells (6). LMO4 is also expressed in mature T cells, cranial neural crest cells, somite, dorsal limb bud mesenchyme, motor neurons, and Schwann cell progenitors (7).

Supplier: Bioss

Caspases are a family of intracellular proteases that mediate cell death and are the principal effectors of apoptosis. Caspase 10 (Mch4, ICE-LAP4, FLICE2) plays an important role in apoptosis induced by a variety of inducers such as TNF alpha and Anti-Fas antibody. It is a large prodomain caspase classified together with caspases 2, 8, and 9 as a signaling caspase. Four isoforms of caspase 10 (caspase 10a, 10b, 10c, and 10d) having the same prodomain but different mature large and small subdomain, have been described. Caspase 10 contains two death domains (DED) involved in linking to the death effector domain of the adapter protein FADD and recruiting the complex to TNFR1 and Fas. The inactive procaspase 10 is variably expressed in many tissues and cell lines as a cytosolic protein. The mature form of caspase 10 comprises two subunits, p23/p17 (splice isoforms) and p12. Interestingly, a caspase 9- dependent processing of caspase 10 by caspase 6 in cell-free extracts has recently been suggested. Caspase 10 can cleave and activate caspases 3, 4, 6, 7, 8, and 9. This is followed by cleavage of numerous key proteins, including the nuclear protein PARP.

Supplier: Bioss

Class I viral fusion protein. Under the current model, the protein has at least 3 conformational states: pre-fusion native state, pre-hairpin intermediate state, and post-fusion hairpin state. During viral and plasma cell membrane fusion, the heptad repeat (HR) regions assume a trimer-of-hairpins structure, positioning the fusion peptide in close proximity to the C-terminal region of the ectodomain. The formation of this structure appears to drive apposition and subsequent fusion of viral and plasma cell membranes. Directs fusion of viral and cellular membranes leading to delivery of the nucleocapsid into the cytoplasm. This fusion is pH independent and occurs directly at the outer cell membrane. The trimer of F1-F2 (F protein) probably interacts with H at the virion surface. Upon HN binding to its cellular receptor, the hydrophobic fusion peptide is unmasked and interacts with the cellular membrane, inducing the fusion between cell and virion membranes. Later in infection, F proteins expressed at the plasma membrane of infected cells could mediate fusion with adjacent cells to form syncytia, a cytopathic effect that could lead to tissue necrosis (By similarity).

Supplier: Bioss

Members of the GATA family share a conserved zinc finger DNA-binding domain and are capable of binding the WGATAR consensus sequence. GATA-1 is erythroid-specific and is responsible for the regulated transcription of erythroid genes. It is an essential component in the generation of the erythroid lineage. GATA-2 is expressed in embryonic brain and liver, HeLa and endothelial cells, as well as in erythroid cells. Studies with a modified GATA consensus sequence, AGATCTTA, have shown that GATA-2 and GATA-3 recognize this mutated consensus while GATA-1 has poor recognition of this sequence. This indicates broader regulatory capabilities of GATA-2 and GATA-3 than GATA-1. GATA-3 is highly expressed in T lymphocytes. GATA-4, GATA-5 and GATA-6 comprise a subfamily of transcription factors. Both GATA-4 and GATA-6 are found in heart, pancreas and ovary; lung and liver tissues exhibit GATA-6, but not GATA-4 expression. GATA-5 expression has been observed in differentiated heart and gut tissues and is present throughout the course of development in the heart. Although expression patterns of the various GATA transcription factors may overlap, it is not yet apparent how the GATA factors are able to discriminate in binding their appropriate target sites.

Supplier: Bioss

Members of the GATA family share a conserved zinc finger DNA-binding domain and are capable of binding the WGATAR consensus sequence. GATA-1 is erythroid-specific and is responsible for the regulated transcription of erythroid genes. It is an essential component in the generation of the erythroid lineage. GATA-2 is expressed in embryonic brain and liver, HeLa and endothelial cells, as well as in erythroid cells. Studies with a modified GATA consensus sequence, AGATCTTA, have shown that GATA-2 and GATA-3 recognize this mutated consensus while GATA-1 has poor recognition of this sequence. This indicates broader regulatory capabilities of GATA-2 and GATA-3 than GATA-1. GATA-3 is highly expressed in T lymphocytes. GATA-4, GATA-5 and GATA-6 comprise a subfamily of transcription factors. Both GATA-4 and GATA-6 are found in heart, pancreas and ovary; lung and liver tissues exhibit GATA-6, but not GATA-4 expression. GATA-5 expression has been observed in differentiated heart and gut tissues and is present throughout the course of development in the heart. Although expression patterns of the various GATA transcription factors may overlap, it is not yet apparent how the GATA factors are able to discriminate in binding their appropriate target sites.

Supplier: Bioss

Hepatoma Derived Growth Factor (HDGF) is the original member of a family of polypeptides designated HDGF-related proteins (HRPs). HDGF was initially characterized as a secreted mitogen from the Huh-7 human hepatoma cell line. This nuclear targeted vascular smooth muscle cell mitogen (VSM) is a heparin-binding protein that is highly expressed in tumor cells where it stimulates proliferation. HDGF is also reported to be involved in organ development and lung remodeling after injury by promoting proliferation of lung epithelial cells. During development, HDGF expression is high in the nucleus and cytoplasm of smooth muscle and endothelial cells. The HRP (HDGF related proteins) family contains four proteins, HRP-1, HRP-2, HRP-3 and HRP-4. HRP-1 and HRP-4 are only expressed in testis while HRP-2 is widely expressed in different tissues. HRP-3 can solely be found in the nervous system. Specifically it is strongly expressed in bulbus, olfactorius, piriform cotrex and amygdala complex while HRP-2 in brain is located in the the thalamus, prefrontal and parietal cortex, neurohypophysis, and the cerebellum. In the central nervous system, HRP proteins are play a role in neuron proliferation and cell survival.

Supplier: Bioss

Hepatoma Derived Growth Factor (HDGF) is the original member of a family of polypeptides designated HDGF-related proteins (HRPs). HDGF was initially characterized as a secreted mitogen from the Huh-7 human hepatoma cell line. This nuclear targeted vascular smooth muscle cell mitogen (VSM) is a heparin-binding protein that is highly expressed in tumor cells where it stimulates proliferation. HDGF is also reported to be involved in organ development and lung remodeling after injury by promoting proliferation of lung epithelial cells. During development, HDGF expression is high in the nucleus and cytoplasm of smooth muscle and endothelial cells. The HRP (HDGF related proteins) family contains four proteins, HRP-1, HRP-2, HRP-3 and HRP-4. HRP-1 and HRP-4 are only expressed in testis while HRP-2 is widely expressed in different tissues. HRP-3 can solely be found in the nervous system. Specifically it is strongly expressed in bulbus, olfactorius, piriform cotrex and amygdala complex while HRP-2 in brain is located in the the thalamus, prefrontal and parietal cortex, neurohypophysis, and the cerebellum. In the central nervous system, HRP proteins are play a role in neuron proliferation and cell survival.

Supplier: Bioss

Hepatoma Derived Growth Factor (HDGF) is the original member of a family of polypeptides designated HDGF-related proteins (HRPs). HDGF was initially characterized as a secreted mitogen from the Huh-7 human hepatoma cell line. This nuclear targeted vascular smooth muscle cell mitogen (VSM) is a heparin-binding protein that is highly expressed in tumor cells where it stimulates proliferation. HDGF is also reported to be involved in organ development and lung remodeling after injury by promoting proliferation of lung epithelial cells. During development, HDGF expression is high in the nucleus and cytoplasm of smooth muscle and endothelial cells. The HRP (HDGF related proteins) family contains four proteins, HRP-1, HRP-2, HRP-3 and HRP-4. HRP-1 and HRP-4 are only expressed in testis while HRP-2 is widely expressed in different tissues. HRP-3 can solely be found in the nervous system. Specifically it is strongly expressed in bulbus, olfactorius, piriform cotrex and amygdala complex while HRP-2 in brain is located in the the thalamus, prefrontal and parietal cortex, neurohypophysis, and the cerebellum. In the central nervous system, HRP proteins are play a role in neuron proliferation and cell survival.

Supplier: Bioss

ATF2 is a member of the ATF/CREB family of basic region leucine zipper DNA binding proteins that regulates transcription by binding to a consensus cAMP response element (CRE) in the promoter of various viral and cellular genes. Many of these genes are important in cell growth and differentiation, and in stress and immune responses. ATF2 is a nuclear protein that binds DNA as a dimer and can form dimers with members of the ATF/CREB and Jun/Fos families. It is a stronger activator as a heterodimer with cJun than as a homodimer. Several isoforms of ATF2 arise by differential splicing. The stable native full length ATF2 is transcriptionally inactive as a result of an inhibitory direct intramolecular interaction of its carboxy terminal DNA binding domain with the amino terminal transactivation domain. Following dimerization ATF2 becomes a short lived protein that undergoes ubiquitination and proteolysis, seemingly in a protein phosphatase-dependent mechanism. Stimulation of the transcriptional activity of ATF2 occurs following cellular stress induced by several genotoxic agents, inflammatory cytokines, and UV irradiation. This activation requires phosphorylation of two threonine residues in ATF2 by both JNK/SAP kinase and p38 MAP kinase. ATF2 is abundantly expressed in brain.

Supplier: Bioss

In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions, including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunits have been identified, designated PP1, PP2A, PP2B (calcineurin) and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4) is a putative member of a novel PP family. The PP2A family comprises subfamily members PP2Aå and PP2A∫. The PP2A catalytic subunit associates with a variety of regulatory subunits. The B family of regulatory subunits (including B55, B56 and PR72/130 subfamilies) is believed to participate in substrate specificity and catalytic activity. PP2A-B55, also known as PP2A regulatory subunit subfamily B55 or PP2A-B1, is a B subfamily consisting of four B55 isoforms (Alpha,Beta, Gamma and Delta) encoded by four distinct genes.

Supplier: Bioss

ATF2 is a member of the ATF/CREB family of basic region leucine zipper DNA binding proteins that regulates transcription by binding to a consensus cAMP response element (CRE) in the promoter of various viral and cellular genes. Many of these genes are important in cell growth and differentiation, and in stress and immune responses. ATF2 is a nuclear protein that binds DNA as a dimer and can form dimers with members of the ATF/CREB and Jun/Fos families. It is a stronger activator as a heterodimer with cJun than as a homodimer. Several isoforms of ATF2 arise by differential splicing. The stable native full length ATF2 is transcriptionally inactive as a result of an inhibitory direct intramolecular interaction of its carboxy terminal DNA binding domain with the amino terminal transactivation domain. Following dimerization ATF2 becomes a short lived protein that undergoes ubiquitination and proteolysis, seemingly in a protein phosphatase-dependent mechanism. Stimulation of the transcriptional activity of ATF2 occurs following cellular stress induced by several genotoxic agents, inflammatory cytokines, and UV irradiation. This activation requires phosphorylation of two threonine residues in ATF2 by both JNK/SAP kinase and p38 MAP kinase. ATF2 is abundantly expressed in brain.

Supplier: Bioss

The sense of taste provides animals with valuable information about the quality and nutritional value of food. A family of G protein-coupled receptors are involved in taste perception and include T1R, which is involved in sweet and umami taste perception, and T2R, which is involved in bitter taste perception. Both types of taste receptors couple to various G proteins to initiate signal transduction cascades. Single taste receptor cells express a variety of T2Rs, suggesting that each cell is capable of recognizing multiple tastants. T2R6 (also designatedT2R30, mt2r42, STC 7-4 or taste receptor, type 2, member 130) is an integral membrane receptor protein in mice that may play a role in the perception of bitterness and in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate Alpha-gustducin, mediate PLC-Beta-2 activation and lead to the gating of TRPM5. T2R6 is expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin-positive cells. The human homolog of T2R6, designated T2R7 (TAS2R7, TRB4 or taste receptor, type 2, member 7) is a G protein-coupled receptor expressed in taste receptor cells of the tongue and palate epithelia.

Supplier: Bioss

The sense of taste provides animals with valuable information about the quality and nutritional value of food. A family of G protein-coupled receptors are involved in taste perception and include T1R, which is involved in sweet and umami taste perception, and T2R, which is involved in bitter taste perception. Both types of taste receptors couple to various G proteins to initiate signal transduction cascades. Single taste receptor cells express a variety of T2Rs, suggesting that each cell is capable of recognizing multiple tastants. T2R6 (also designatedT2R30, mt2r42, STC 7-4 or taste receptor, type 2, member 130) is an integral membrane receptor protein in mice that may play a role in the perception of bitterness and in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate Alpha-gustducin, mediate PLC-Beta-2 activation and lead to the gating of TRPM5. T2R6 is expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin-positive cells. The human homolog of T2R6, designated T2R7 (TAS2R7, TRB4 or taste receptor, type 2, member 7) is a G protein-coupled receptor expressed in taste receptor cells of the tongue and palate epithelia.

Supplier: Bioss

Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and 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 IFN-stimulated genes (ISG), 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. Becomes activated in response to KITLG/SCF and KIT signaling. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4.

Supplier: Bioss

Signal transducer and transcription activator that mediates cellular responses to interferons (IFNs), cytokine KITLG/SCF and other cytokines and other growth factors. Following type I IFN (IFN-alpha and IFN-beta) binding to cell surface receptors, signaling via protein kinases leads to activation of Jak kinases (TYK2 and JAK1) and to tyrosine phosphorylation of STAT1 and STAT2. The phosphorylated STATs dimerize and 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 IFN-stimulated genes (ISG), 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. Becomes activated in response to KITLG/SCF and KIT signaling. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4.

Supplier: Bioss

Glutamic acid rich protein (GARP) is a soluble protein localized to the outer segments of the rod photoreceptor. It forms a subunit of cyclic nucleotide-gated (CNG) channels, nonselective cation channels, which play important roles in both visual and olfactory signal transduction. When associated with CNGA1, it is involved in the regulation of ion flow into the rod photoreceptor outer segment (ROS), in response to light-induced alteration of the levels of intracellular cGMP. There are 3 isoforms produced by alternative splicing. Isoform GARP2 is a high affinity rod photoreceptor phosphodiesterase (PDE6)-binding protein that modulates its catalytic properties; it is a regulator of spontaneous activation of rod PDE6, thereby serving to lower rod photoreceptor 'dark noise' and allowing these sensory cells to operate at the single photon detection limit. Defects in GARP are the cause of retinitis pigmentosa type 25 (RP25). RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.

Supplier: Bioss

Glutamic acid rich protein (GARP) is a soluble protein localized to the outer segments of the rod photoreceptor. It forms a subunit of cyclic nucleotide-gated (CNG) channels, nonselective cation channels, which play important roles in both visual and olfactory signal transduction. When associated with CNGA1, it is involved in the regulation of ion flow into the rod photoreceptor outer segment (ROS), in response to light-induced alteration of the levels of intracellular cGMP. There are 3 isoforms produced by alternative splicing. Isoform GARP2 is a high affinity rod photoreceptor phosphodiesterase (PDE6)-binding protein that modulates its catalytic properties; it is a regulator of spontaneous activation of rod PDE6, thereby serving to lower rod photoreceptor 'dark noise' and allowing these sensory cells to operate at the single photon detection limit. Defects in GARP are the cause of retinitis pigmentosa type 25 (RP25). RP leads to degeneration of retinal photoreceptor cells. Patients typically have night vision blindness and loss of midperipheral visual field. As their condition progresses, they lose their far peripheral visual field and eventually central vision as well.

Supplier: Bioss

Chk2 is a serine/threonine kinase involved in the control of cell cycle checkpoints, and may also participate in transduction of the DNA damage and replicational stress signals. Chk2 is the mammalian ortholog of the budding yeast Rad53 and fission yeast Cds1 checkpoint kinases. The amino-terminal domain of Chk2 contains a series of seven serine and threonine residues (Ser19, Thr26, Ser28, Ser33, Ser35, Ser50 and Thr68) followed by glutamine (SQ or TQ motif). These are known to be preferred sites for phosphorylation by ATM/ATR kinases. Indeed, after DNA damage by ionizing radiation (IR), UV irradiation or hydroxyurea treatment, Thr68 and other sites in this region become phosphorylated by ATM/ATR. The SQ/TQ cluster domain, therefore, seems to have a regulatory function. Phosphorylation at Thr68 is a prerequisite for the subsequent activation step, which is attributable to autophosphorylation of Chk2 on residues Thr383 and Thr387 in the activation loop of the kinase domain. Chk2 inhibits CDC25C phosphatase by phosphorylating it on Ser-216, preventing the entry into mitosis. This kinase may have a role in meiosis as well. Kinase activity is up regulated by autophosphorylation and the protein is rapidly phosphorylated in response to DNA damage and to replication block.

Supplier: Bioss

MOZ (monocytic leukemia zinc finger protein) is a chromatin-associated histone acetyltransferase (HAT) that regulates chromatin remodeling and transcription. The MOZ gene was initially isolated as a consequence of two variant translocations that were identified in a distinct subtype of acute myeloid leukemias and resulted in the formation of MOZ fusion proteins. These fusions involve the HAT domain of MOZ with the activation domain of either transcriptional coactivator protein TIF2/GRIP1 or CBP, and lead to enhanced transcriptional activation by a mechanism involving aberrant histone acetylation. Additional MOZ related proteins, including MORF (MOZ related factor) and TIP60 (TAT interacting proteins 60), share significant similarities with MOZ including the putuative HAT domain. MORF also contains a strong transcriptional repression domain at its N terminus and a highly potent activation domain at the C terminus, suggesting that MORF has both HAT activity and contributes to the regulation of transcriptional activation. TIP60 was originally identified as a coactivator for the HIV TAT protein and also functions as a nuclear hormone receptor coactivator that enhances ligand dependent steroid receptor-mediated transactivation involving the androgen, estrogen and progesterone receptors.

Supplier: Bioss

Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation. Association with MYD88 leads to IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates the interferon regulatory factor 7 (IRF7) to induce its activation and translocation to the nucleus, resulting in transcriptional activation of type I IFN genes, which drive the cell in an antiviral state. When sumoylated, translocates to the nucleus and phosphorylates STAT3.