You Searched For: viral+rna

Catalog Number: (76083-640)

Supplier: Bioss

Description: Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages.

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Catalog Number: (76119-358)

Supplier: Bioss

Description: The 2'- 5'- oligoadenylate synthetase (OAS) family is comprised of four members: OAS1, OAS2, OAS3 and OASL. These proteins are induced by interferons and function to convert ATP into 2'- 5'- linked oligomers of adenosine in the presence of double-stranded RNA and magnesium ions. Copper, iron and zinc ions strongly inhibit the OAS enzymatic activity, while manganese ions can replace magnesium ions as an activator. The OAS family plays a significant role in the inhibition of cellular protein synthesis, apoptosis and growth, and its members are important factors in viral infection resistance. OAS3, also referred to as p100, contains three adjacent OAS1-like domains and maps to the human chromosome 12q24.2

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Catalog Number: (10107-430)

Supplier: Prosci

Description: ILF3 may facilitate double-stranded RNA-regulated gene expression at the level of post-transcription. ILF3 can act as a translation inhibitory protein which binds to coding sequences of acid beta-glucosidase (GCase) and other mRNAs and functions at the initiation phase of GCase mRNA translation, probably by inhibiting its binding to polysomes. ILF3 can regulate protein arginine N-methyltransferase 1 activity. ILF3 may regulate transcription of the IL2 gene during T-cell activation. It can promote the formation of stable DNA-dependent protein kinase holoenzyme complexes on DNA.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.

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Catalog Number: (10367-570)

Supplier: Bioss

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

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Catalog Number: (10108-130)

Supplier: Prosci

Description: Inhibition of the nuclear export of poly (A)-containing mRNAs caused by the influenza A virus NS1 protein requires its effector domain. The NS1 effector domain functionally interacts with the cellular 30 kDa subunit of cleavage and polyadenylation specific factor 4, an essential component of the 3' end processing machinery of cellular pre-mRNAs. In influenza virus-infected cells, the NS1 protein is physically associated with cleavage and polyadenylation specific factor 4, 30kD subunit. Binding of the NS1 protein to the 30 kDa protein in vitro prevents CPSF binding to the RNA substrate and inhibits 3' end cleavage and polyadenylation of host pre-mRNAs. Thus the NS1 protein selectively inhibits the nuclear export of cellular, and not viral, mRNAs.

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Catalog Number: (10073-034)

Supplier: Prosci

Description: Lin28 is a RNA-binding protein that belongs to a diverse family of structurally-related transcription factors. Lin28 is found abundantly in embryonic stem cells (ESCs), and to a lesser extent in placenta and testis. Lin28 has been shown to block let-7 microRNA processing and maturation, a necessary step in the differentiation of stem cells and certain cancer cell lines. Together with Sox2, Oct4, and Nanog, Lin28 can induce the reprogramming of primary human fibroblasts to a pluripotent state. Lin28 and other regulatory proteins can be introduced into cells by DNA transfection, viral infection, or microinjection. Protein transduction using TAT fusion proteins represents an alternative methodology for introducing proteins into primary as well as transformed cells. Recombinant human Lin28-TAT is a 24.4 kDa protein containing 222 amino acid residues, including 13- residue C-terminal TAT peptide.

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Catalog Number: (76120-274)

Supplier: Bioss

Description: ELYS is a protein of the nuclear matrix that contains one AT hook DNA-binding domain. ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division. Nuclear pores span the nuclear envelope and act as gated aqueous channels to regulate the transport of macromolecules between the nucleus and cytoplasm, from individual proteins and RNAs to entire viral genomes. The A.T. hook near the C-terminus of likely indicates ELYS can function as a transcription factor which may play a specific role in hematopoietic tissues. It also may play a role in early embryo development, as ELYS is critical for the survival of inner cells of the blastocyst.

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Catalog Number: (76120-276)

Supplier: Bioss

Description: ELYS is a protein of the nuclear matrix that contains one AT hook DNA-binding domain. ELYS is a dual nucleoporin/kinetochore protein required for nuclear pore assembly and proper cell division. Nuclear pores span the nuclear envelope and act as gated aqueous channels to regulate the transport of macromolecules between the nucleus and cytoplasm, from individual proteins and RNAs to entire viral genomes. The A.T. hook near the C-terminus of likely indicates ELYS can function as a transcription factor which may play a specific role in hematopoietic tissues. It also may play a role in early embryo development, as ELYS is critical for the survival of inner cells of the blastocyst.

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Catalog Number: (10749-200)

Supplier: Prosci

Description: Swine H1N1 Nucleocapsid Protein Antibody: 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. The influenza A virus polymerase transcribes and replicates eight virion RNA (vRNA) segments, among which the nucleocapsid protein (NP), thought to control whether mRNA or cRNA is produced. The nucleoprotein (NP), which has multiple functions during the virus life cycle, possesses regions that are highly conserved among influenza A, B, and C viruses. It was recently found several NP mutations that affected the efficient incorporation of multiple viral-RNA (vRNA) segments into progeny virions even though a single vRNA segment was incorporated efficiently. This indicates that the respective conserved amino acids in NP may be critical for the assembly and/or incorporation of sets of eight vRNA segments.

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Catalog Number: (10349-670)

Supplier: Bioss

Description: Key transcriptional regulator of type I interferon (IFN)-dependent immune responses which plays a critical role in the innate immune response against DNA and RNA viruses. Regulates the transcription of type I IFN genes (IFN-alpha and IFN-beta) and IFN-stimulated genes (ISG) by binding to an interferon-stimulated response element (ISRE) in their promoters. Acts as a more potent activator of the IFN-beta (IFNB) gene than the IFN-alpha (IFNA) gene and plays a critical role in both the early and late phases of the IFNA/B gene induction. Found in an inactive form in the cytoplasm of uninfected cells and following viral infection, double-stranded RNA (dsRNA), or toll-like receptor (TLR) signaling, is phosphorylated by IKBKE and TBK1 kinases. This induces a conformational change, leading to its dimerization and nuclear localization and association with CREB binding protein (CREBBP) to form dsRNA-activated factor 1 (DRAF1), a complex which activates the transcription of the type I IFN and ISG genes. Can activate distinct gene expression programs in macrophages and can induce significant apoptosis in primary macrophages.

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Catalog Number: (76082-300)

Supplier: Bioss

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

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Catalog Number: (102514-260)

Supplier: Adipogen

Description: RIG-I (retinoic acid-inducible gene I; Ddx58) and MDA5 (melanoma differentiation-associated gene 5, also known as Ifih1 or Helicard) are proteins that sense viral replication intermediates, such as double-stranded RNA and triggers the host antiviral programs. These molecules signal the downstream activation of NF-kappaB and IFN regulatory factor (IRF) -3, which coordinately regulate the expression of type-I interferons. Cardif (also called VISA/IPS-1/MAVS) is a new CARD (caspase activation and recruitment domain)-containing adaptor protein that interacts with the CARD domain of RIG-I and MDA5, leading to the activation of NF-kappaB and IRF3. Cardif is located to the mitochondrial outer membrane. Removal of the mitochondrial-targeting domain of cardif abolishes its ability to induce IFNs. Cardif is cleaved and inactivated by NS3-4A, a serine protease from hepatitis C virus known to block interferon-beta production.

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Catalog Number: (10050-166)

Supplier: Enzo Life Sciences

Description: EIF-2α, also known as eukaryotic translation initiation factor 2α, promotes the binding of the initiator tRNA to the 40S ribosomal subunits and controls translational rates via phosphorylation/dephosphorylation mechanisms. The double-stranded RNA (dsRNA)-activated protein kinase (PKR) provides an important control in the regulation of protein synthesis initiation through the phosphorylation of eIF-2α. Phosphorylated eIF-2α inhibits cell growth and induces apoptosis. Phosphorylation of eIF-2α occurs under a variety of conditions including viral infection, apoptosis, nutrient deprivation, heme-deprivation, and certain stresses. EIF-2 exists as a heterotrimeric protein composed of 3 nonidentical subunits, alpha (36 kDa), beta (38 kDa), and gamma (52 kDa).

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Catalog Number: (10751-878)

Supplier: Prosci

Description: CCNT1 Antibody: Cyclins function as regulators of CDK kinases and exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. The cyclin-T1 protein (CCNT1) belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. CCNT1 tightly associates with CDK9 kinase, and was found to be a major subunit of the transcription elongation factor p-TEFb. The kinase complex containing CCNT1 and the elongation factor can interact with, and act as a cofactor of human immunodeficiency virus type 1 (HIV-1) Tat protein, and was shown to be both necessary and sufficient for full activation of viral transcription. CCNT1 and its kinase partner were also found to be involved in the phosphorylation and regulation of the carboxy-terminal domain (CTD) of the largest RNA polymerase II subunit.

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Catalog Number: (10367-588)

Supplier: Bioss

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

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Catalog Number: (10367-586)

Supplier: Bioss

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

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