1132 Results for: "viral rna"

Supplier: Prosci

NCBP1 Antibody: NCBP1, also known as CBP80, is a component of the nuclear cap-binding protein complex (CBC), which binds to the monomethylated 5' cap of nascent pre-mRNA in the nucleoplasm. NCBP1 promotes high-affinity mRNA-cap binding and associates with the CTD of RNA polymerase II. The CBC promotes pre-mRNA splicing, 3'-end processing, RNA nuclear export, and nonsense-mediated mRNA decay (1,2). Recent evidence has shown that cellular-cap-binding proteins such as NCBP1 associate with influenza virus mRNAs, suggesting that these viral mRNAs may follow the normal cellular pathways for splicing, nuclear export, and translation.

Supplier: G-Biosciences

Favipiravir is an inhibitor of Influenza viruses A, B, and C (IC50s: A = 0.03-0.20 µg/mL H1N1, 0.01-0.30 H2N2, 0.08-0.48 H3N2, 0.14-0.15 H4N2, 0.24-1.60 H7N2, 0.20-0.82 H5N1, 0.35 H1N2; B = 0.04-0.09 µg/mL; C = 0.03-0.06 µg/mL) as well as strains resistant to adamantane-type antivirals, oseltamivir, and zanamivir1-3. It displayed no cytotoxicity in a variety of cells. Favipiravir selectively inhibits viral RNA-dependent RNA polymerase4. Favipiravir has also shown activity against other viruses including arena, phlebo, hanta, flavi, entero, alpha, respiratory syncytial, and noroviruses5. In clinical trials for treatment of SARS-CoV-26,7.

Supplier: Bioss

Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response (By similarity).

Supplier: Bioss

Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response (By similarity).

Supplier: Bioss

Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response (By similarity).

Supplier: Bioss

Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response (By similarity).

Supplier: Prosci

Nuclear factor of activated T-cells (NFAT) is a transcription factor required for T-cell expression of interleukin 2. NFAT binds to a sequence in the IL2 enhancer known as the antigen receptor response element 2. In addition, NFAT can bind RNA and is an essential component for encapsidation and protein priming of hepatitis B viral polymerase. NFAT is a heterodimer of 45 kDa and 90 kDa proteins, the larger of which is the product of ILF3.Nuclear factor of activated T-cells (NFAT) is a transcription factor required for T-cell expression of interleukin 2. NFAT binds to a sequence in the IL2 enhancer known as the antigen receptor response element 2. In addition, NFAT can bind RNA and is an essential component for encapsidation and protein priming of hepatitis B viral polymerase. NFAT is a heterodimer of 45 kDa and 90 kDa proteins, the larger of which is the product of this gene. The encoded protein, which is primarily localized to ribosomes, probably regulates transcription at the level of mRNA elongation. At least three transcript variants encoding three different isoforms have been found for this gene.

Supplier: Bioss

Key component of innate and adaptive immunity. TLRs (Toll-like receptors) control host immune response against pathogens through recognition of molecular patterns specific to microorganisms. TLR3 is a nucleotide-sensing TLR which is activated by double-stranded RNA, a sign of viral infection. Acts via the adapter TRIF/TICAM1, leading to NF-kappa-B activation, IRF3 nuclear translocation, cytokine secretion and the inflammatory response (By similarity).

Supplier: Rockland Immunochemical

STAU1 is a member of a family of double-stranded RNA (dsRNA)-binding proteins involved in the transport and/or localization of mRNAs to different subcellular compartments and/or organelles. These proteins are characterized by the presence of multiple dsRNA-binding domains which are required to bind RNAs having double-stranded secondary structures. The human STAU1 also contains a microtubule- binding domain similar to that of microtubule-associated protein 1B, and binds tubulin. STAU1 has been shown to be present in the cytoplasm in association with the rough endoplasmic reticulum (RER), implicating this protein in the transport of mRNA via the microtubule network to the RER. STAU1 is also known to interact with influenza ribonucleoproteins NS1, NP, and PA and is required for efficient viral replication.

Supplier: Prosci

TLR3 Antibody: Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules resembling the toll proteins that mediate antimicrobial responses in Drosophila. These proteins recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. The TLRs act through adaptor molecules such as MyD88 and TIRAP to activate various kinases and transcription factors so the organism can respond to potential infection. TLR3 is known to recognize viral double-stranded (ds) RNA, a molecular pattern associated with viral infection. Recently it has been shown to recognize viruses such as Influenza A and West Nile Virus and can mediate entry of at least West Nile Virus.

Supplier: Prosci

TLR3 Antibody: Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules resembling the toll proteins that mediate antimicrobial responses in Drosophila. These proteins recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. The TLRs act through adaptor molecules such as MyD88 and TIRAP to activate various kinases and transcription factors so the organism can respond to potential infection. TLR3 is known to recognize viral double-stranded (ds) RNA, a molecular pattern associated with viral infection. Recently it has been shown to recognize viruses such as Influenza A and West Nile Virus and can mediate entry of at least West Nile Virus.

Supplier: Abcam

Daclatasvir a potent, direct acting, small molecule inhbitor of HCV NS5A protein. It inhbibits replicons expressing a wide range of HCV genotypes with EC₅₀ values in the pM range (9 and 71 pM against the 1b and 2a genotypes, respectively). It also inhibits infection by the JFH-1 genotype 2a virus in cultured cells. Daclatasvir is thought to inhibit relication of the HCV viral genome by affecting the subcellular localization of HCV NS5A and preventing its incorporation into relication complexes. In HCV-infected Huh7 cells, Daclatasvir (1 nM) inhibits viral RNA synthesis and viron assembly. Daclatasvir displays moderate activity against the OAT1B1 (IC₅₀ = 1.5 μM) and OAT1B3 (IC₅₀ = 3.27 μM) organic anion transporters.

Supplier: Bioss

Encapsidates the negative strand viral RNA, protecting it from nucleases. The encapsidated genomic RNA is termed the ribonucleoprotein (RNP) and serves as template for transcription and replication. The RNP needs to be localized in the nucleus to start an infectious cycle, but is too large to diffuse through the nuclear pore complex. NP comprises at least 2 nuclear localization signals and is responsible of the active RNP import into the nucleus through the cellular importin alpha/beta pathway. Later in the infection, nucleus export of RNP are mediated through viral proteins NEP interacting with M1 which binds nucleoproteins. It is possible that the nucleoprotein binds directly exportin-1 (XPO1) and plays an active role in RNP nuclear export. M1 interaction with RNP seems to hide nucleoprotein's nuclear localization signals. Soon after a virion infects a new cell, M1 dissociates from the RNP under acidification of the virion driven by M2 protein. Dissociation of M1 from RNP unmask nucleoprotein's nuclear localization signals, targeting the RNP to the nucleus.

Supplier: Rockland Immunochemical

Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus (S-OIV) was identified in specimens obtained from patients in Mexico and the United States. One of the less studied proteins encoded by, but not incorporated in, the influenza virus is the nonstructural protein (NS) 1. NS1 counters cellular antiviral activities and acts as a virulence factor. It can bind to double-stranded RNA and sequester it from 2'-5'OAS, preventing the activation of the RNAse L, which normally acts to degrade RNA and prevent virus replication. NS1 also binds to and inhibits the anti-viral protein kinase PKR.

Supplier: Rockland Immunochemical

Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. In early 2009, a novel swine-origin influenza A (H1N1) virus (S-OIV) was identified in specimens obtained from patients in Mexico and the United States. One of the less studied proteins encoded by, but not incorporated in, the influenza virus is the nonstructural protein (NS) 1. NS1 counters cellular antiviral activities and acts as a virulence factor. It can bind to double-stranded RNA and sequester it from 2'-5'OAS, preventing the activation of the RNAse L, which normally acts to degrade RNA and prevent virus replication. NS1 also binds to and inhibits the anti-viral protein kinase PKR.

Supplier: Prosci

TLR3 Antibody: Toll-like receptors (TLRs) are evolutionarily conserved pattern-recognition molecules resembling the toll proteins that mediate antimicrobial responses in Drosophila. These proteins recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. The TLRs act through adaptor molecules such as MyD88 and TIRAP to activate various kinases and transcription factors so the organism can respond to potential infection. TLR3 is known to recognize viral double-stranded (ds) RNA, a molecular pattern associated with viral infection. Recently it has been shown to recognize viruses such as Influenza A and West Nile Virus and can mediate entry of at least West Nile Virus.

Supplier: Aladdin Scientific

Reactant for preparation of: . Indole derivatives as antitumor agents . Endothelin-1 antagonists . Oncrasin-1 derivatives as inhibitors of the C-terminal domain of RNA polymerase II with antitumor activities . Inhibitors of hepatitis C NS3/4A serine protease . Antibacterial agens against MDR Staphylococcus aureus strains . Antimalarial agents . Anti-bovine viral diarrhea virus (BVDV) agents . HIV-1 integrase inhibitors . Inhibitors of NF-κB transcription regulation related to TNF-α cytokine release

Supplier: Bioss

Innate immune receptor which acts as a cytoplasmic sensor of viral nucleic acids and plays a major role in sensing viral infection and in the activation of a cascade of antiviral responses including the induction of type I interferons and proinflammatory cytokines. Its ligands include: 5'-triphosphorylated ssRNA and dsRNA and short dsRNA (<1 kb in length). In addition to the 5'-triphosphate moiety, blunt-end base pairing at the 5'-end of the RNA is very essential. Overhangs at the non-triphosphorylated end of the dsRNA RNA have no major impact on its activity. A 3'overhang at the 5'triphosphate end decreases and any 5'overhang at the 5' triphosphate end abolishes its activity. Upon ligand binding it associates with mitochondria antiviral signaling protein (MAVS/IPS1) which activates the IKK-related kinases: TBK1 and IKBKE which phosphorylate interferon regulatory factors: IRF3 and IRF7 which in turn activate transcription of antiviral immunological genes, including interferons (IFNs); IFN-alpha and IFN-beta. Detects both positive and negative strand RNA viruses including members of the families Paramyxoviridae: Human respiratory syncytial virus and measles virus (MeV), Rhabdoviridae: vesicular stomatitis virus (VSV), Orthomyxoviridae: influenza A and B virus, Flaviviridae: Japanese encephalitis virus (JEV), hepatitis C virus (HCV), dengue virus (DENV) and west Nile virus (WNV). It also detects rotavirus and reovirus. Also involved in antiviral signaling in response to viruses containing a dsDNA genome such as Epstein-Barr virus (EBV). Detects dsRNA produced from non-self dsDNA by RNA polymerase III, such as Epstein-Barr virus-encoded RNAs (EBERs). May play important roles in granulocyte production and differentiation, bacterial phagocytosis and in the regulation of cell migration.

Supplier: Prosci

Avian Influenza Nonstructural Protein 1 Antibody: Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however, it is in birds that all subtypes, including the so-called "avian flu" or H5N1, can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. One of the less studied proteins encoded by, but not incorporated in, the influenza virus is the nonstructural protein (NS) 1. NS1 counters cellular antiviral activities and acts as a virulence factor. It can bind to double-stranded RNA and sequester it from 2'-5'OAS, preventing the activation of the RNAse L, which normally acts to degrade RNA and prevent virus replication. NS1 also binds to and inhibits the anti-viral protein kinase PKR.

Supplier: Prosci

SART3 is an RNA-binding nuclear protein that is a tumor-rejection antigen. This antigen possesses tumor epitopes capable of inducing HLA-A24-restricted and tumor-specific cytotoxic T lymphocytes in cancer patients and may be useful for specific immunotherapy. SART3 is found to be an important cellular factor for HIV-1 gene expression and viral replication. It also associates transiently with U6 and U4/U6 snRNPs during the recycling phase of the spliceosome cycle. This protein is thought to be involved in the regulation of mRNA splicing.

Supplier: Prosci

STAU1 Antibody: STAU1 is a member of a family of double-stranded RNA (dsRNA)-binding proteins involved in the transport and/or localization of mRNAs to different subcellular compartments and/or organelles. These proteins are characterized by the presence of multiple dsRNA-binding domains which are required to bind RNAs having double-stranded secondary structures. The human STAU1 also contains a microtubule- binding domain similar to that of microtubule-associated protein 1B, and binds tubulin. STAU1 has been shown to be present in the cytoplasm in association with the rough endoplasmic reticulum (RER), implicating this protein in the transport of mRNA via the microtubule network to the RER. STAU1 is also known to interact with influenza ribonucleoproteins NS1, NP, and PA and is required for efficient viral replication.

Supplier: Prosci

Avian Influenza Nonstructural Protein 1 Antibody: Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however, it is in birds that all subtypes, including the so-called "avian flu" or H5N1, can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. One of the less studied proteins encoded by, but not incorporated in, the influenza virus is the nonstructural protein (NS) 1. NS1 counters cellular antiviral activities and acts as a virulence factor. It can bind to double-stranded RNA and sequester it from 2'-5'OAS, preventing the activation of the RNAse L, which normally acts to degrade RNA and prevent virus replication. NS1 also binds to and inhibits the anti-viral protein kinase PKR.

Supplier: Prosci

STAU1 Antibody: STAU1 is a member of a family of double-stranded RNA (dsRNA)-binding proteins involved in the transport and/or localization of mRNAs to different subcellular compartments and/or organelles. These proteins are characterized by the presence of multiple dsRNA-binding domains which are required to bind RNAs having double-stranded secondary structures. The human STAU1 also contains a microtubule- binding domain similar to that of microtubule-associated protein 1B, and binds tubulin. STAU1 has been shown to be present in the cytoplasm in association with the rough endoplasmic reticulum (RER), implicating this protein in the transport of mRNA via the microtubule network to the RER. STAU1 is also known to interact with influenza ribonucleoproteins NS1, NP, and PA and is required for efficient viral replication.

Supplier: Bioss

Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Hyperphosphorylates RS domain-containing proteins such as SFRS1, SFRS2 and ZRSR2 on serine residues during metaphase but at lower levels during interphase. Locks onto SFRS1 to form a stable complex and processively phosphorylates the RS domain. Appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids.

Supplier: Bioss

Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Hyperphosphorylates RS domain-containing proteins such as SFRS1, SFRS2 and ZRSR2 on serine residues during metaphase but at lower levels during interphase. Locks onto SFRS1 to form a stable complex and processively phosphorylates the RS domain. Appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids.

Supplier: Prosci

The interferon-induced protein with tetratricopeptide repeats 3 (IFIT3) protein is a member of a family of tetratricopeptide repeat-containing proteins whose transcription is upregulated by interferons, virus infection, and molecular patterns such as dsRNA or lipopolysaccharides. These proteins have been suggested to induce anti-viral cellular activities in response to infection. IFIT3 has been shown to interact with TBK1 following RNA virus infection, thereby bridging TBK1 to VISA on the mitochondrion and activating IRF3 and thus the immune response.

Supplier: Bioss

Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Hyperphosphorylates RS domain-containing proteins such as SFRS1, SFRS2 and ZRSR2 on serine residues during metaphase but at lower levels during interphase. Locks onto SFRS1 to form a stable complex and processively phosphorylates the RS domain. Appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids.

Supplier: Bioss

Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Hyperphosphorylates RS domain-containing proteins such as SFRS1, SFRS2 and ZRSR2 on serine residues during metaphase but at lower levels during interphase. Locks onto SFRS1 to form a stable complex and processively phosphorylates the RS domain. Appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids.

Supplier: Bioss

Plays a central role in the regulatory network for splicing, controlling the intranuclear distribution of splicing factors in interphase cells and the reorganization of nuclear speckles during mitosis. Hyperphosphorylates RS domain-containing proteins such as SFRS1, SFRS2 and ZRSR2 on serine residues during metaphase but at lower levels during interphase. Locks onto SFRS1 to form a stable complex and processively phosphorylates the RS domain. Appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids.

Supplier: Bioss

Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. ZNF426 (Zinc finger protein 426), also known as MGC2663, is a 554 amino acid protein that is thought to be involved in transcriptional regulation. Localized to the nucleus, ZNF426 contains one KRAB domain and 12 C2H2-type zinc fingers through which it may convey DNA, RNA and protein binding capabilities. Specifically, ZNF426 may interact with the viral protein KSHV ORF 50 and, through this interaction, may activate viral gene transcription.