1132 Results for: "viral rna"

Supplier: Prosci

VISA Antibody: Two distinct signaling pathways activate the host innate immunity against viral infection. One pathway is reliant on members of the Toll-like receptor (TLR) family while the other uses the RNA helicase RIG-I as a receptor for intracellular viral double-stranded RNA as a trigger for the immune response. VISA is a mitochondrial membrane protein that was identified as a critical component in the IFN-b signaling pathways that recruits IRF-3 to RIG-I, leading to its activation and that of NF-kappa B. VISA is also thought to interact with other components of the innate immune pathway such as the TLR adapter protein TRIF, TRAF2 and TRAF6. VISA also interacts with the IKK alpha , IKK beta and IKK epsilon kinases through its C-terminal region. Cleavage of this region by the Hepatitis C virus (HCV) protease allows HCV to escape the host immune system. At least three isoforms of VISA are known to exist.

Supplier: Proteintech

The process of mRNA splicing required assembly of pre-mRNA into a large, dynamic RNA-protein complex, in which 5 small nuclear RNAs and more than 50 protein components are incorporated into functional small nuclear ribonucleoproteins(snRNPs). SART3 interacts with U6 snRNA and functioned as a U6-specific recycling factor responsible for regeneration of base-paired U4/U6 snRNPs from post-spliceosomal free U4 and U6 snRNPs. Also it can interact and regulate Tat transactivation activity, and act as a cellular factor for HIV-1 gene expession and viral replicaiton.

Supplier: Rockland Immunochemical

Two distinct signaling pathways activate the host innate immunity against viral infection. One pathway is reliant on members of the Toll-like receptor (TLR) family while the other uses the RNA helicase RIG-I as a receptor for intracellular viral double-stranded RNA as a trigger for the immune response. VISA is a mitochondrial membrane protein that was identified as a critical component in the IFN-b signaling pathways that recruits IRF-3 to RIG-I, leading to its activation and that of NF-kB. VISA is also thought to interact with other components of the innate immune pathway such as the TLR adapter protein TRIF, TRAF2 and TRAF6. VISA also interacts with the IKKa, IKKb and IKKe kinases through its C-terminal region. Cleavage of this region by the Hepatitis C virus (HCV) protease allows HCV to escape the host immune system. At least three isoforms of VISA are known to exist.

Supplier: Bioss

Human immunodeficiency virus (HIV) is a retrovirus that can lead to a condition in which the immune system begins to fail, leading to opportunistic infections. HIV primarily infects vital cells in the human immune system such as helper T cells(specifically CD4+ T cells), macrophages and dendritic cells. HIV infection leads to low levels of CD4+ T cells through three main mechanisms: firstly, direct viral killing of infected cells; secondly, increased rates of apoptosis in infected cells; and thirdly, killing of infected CD4+ T cells by CD8 cytotoxic lymphocytes that recognize infected cells. When CD4+ T cell numbers decline below a critical level, cell-mediated immunity is lost, and the body becomes progressively more susceptible to opportunistic infections. HIV was classified as a member of the genus Lentivirus, part of the family of Retroviridae. Lentiviruses have many common morphologies and biological properties. Many species are infected by lentiviruses, which are characteristically responsible for long-duration illnesses with a long incubation period. Lentiviruses are transmitted as single-stranded, positive-sense, enveloped RNA viruses. Upon entry of the target cell, the viral RNA genome is converted to double-stranded DNA by a virally encoded reverse transcriptase that is present in the virus particle. This viral DNA is then integrated into the cellular DNA by a virally encoded integrase so that the genome can be transcribed. Once the virus has infected the cell, two pathways are possible: either the virus becomes latent and the infected cell continues to function, or the virus becomes active and replicates, and a large number of virus particles are liberated that can then infect other cells.

Supplier: Prosci

VISA Antibody: Two distinct signaling pathways activate the host innate immunity against viral infection. One pathway is reliant on members of the Toll-like receptor (TLR) family while the other uses the RNA helicase RIG-I as a receptor for intracellular viral double-stranded RNA as a trigger for the immune response. VISA is a mitochondrial membrane protein that was identified as a critical component in the IFN-b signaling pathways that recruits IRF-3 to RIG-I, leading to its activation and that of NF-kappa B. VISA is also thought to interact with other components of the innate immune pathway such as the TLR adapter protein TRIF, TRAF2 and TRAF6. VISA also interacts with the IKKalpha , IKKbeta ; and IKKepsilon kinases through its C-terminal region. Cleavage of this region by the Hepatitis C virus (HCV) protease allows HCV to escape the host immune system. At least three isoforms of VISA are known to exist.

Supplier: Prosci

VISA Antibody: Two distinct signaling pathways activate the host innate immunity against viral infection. One pathway is reliant on members of the Toll-like receptor (TLR) family while the other uses the RNA helicase RIG-I as a receptor for intracellular viral double-stranded RNA as a trigger for the immune response. VISA is a mitochondrial membrane protein that was identified as a critical component in the IFN-b signaling pathways that recruits IRF-3 to RIG-I, leading to its activation and that of NF-kappa B. VISA is also thought to interact with other components of the innate immune pathway such as the TLR adapter protein TRIF, TRAF2 and TRAF6. VISA also interacts with the IKK alpha , IKK beta and IKK epsilon kinases through its C-terminal region. Cleavage of this region by the Hepatitis C virus (HCV) protease allows HCV to escape the host immune system. At least three isoforms of VISA are known to exist.

Supplier: Rockland Immunochemical

Two distinct signaling pathways activate the host innate immunity against viral infection. One pathway is reliant on members of the Toll-like receptor (TLR) family while the other uses the RNA helicase RIG-I as a receptor for intracellular viral double-stranded RNA as a trigger for the immune response. VISA is a mitochondrial membrane protein that was identified as a critical component in the IFN-b signaling pathways that recruits IRF-3 to RIG-I, leading to its activation and that of NF-kB. VISA is also thought to interact with other components of the innate immune pathway such as the TLR adapter protein TRIF, TRAF2 and TRAF6. VISA also interacts with the IKKa, IKKb and IKKe kinases through its C-terminal region. Cleavage of this region by the Hepatitis C virus (HCV) protease allows HCV to escape the host immune system. At least three isoforms of VISA are known to exist.

Supplier: Prosci

VISA Antibody: Two distinct signaling pathways activate the host innate immunity against viral infection. One pathway is reliant on members of the Toll-like receptor (TLR) family while the other uses the RNA helicase RIG-I as a receptor for intracellular viral double-stranded RNA as a trigger for the immune response. VISA is a mitochondrial membrane protein that was identified as a critical component in the IFN-b signaling pathways that recruits IRF-3 to RIG-I, leading to its activation and that of NF-kappa B. VISA is also thought to interact with other components of the innate immune pathway such as the TLR adapter protein TRIF, TRAF2 and TRAF6. VISA also interacts with the IKK alpha , IKK beta ; and IKKepsilon kinases through its C-terminal region. Cleavage of this region by the Hepatitis C virus (HCV) protease allows HCV to escape the host immune system. At least three isoforms of VISA are known to exist.

Supplier: Rockland Immunochemical

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp, are putative RNA helicases implicated in several cellular processes involving modifications of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. DDX41, also known as Abstrakt, interacts with and regulates the expression of sorting nexin-2 (SNX2), a protein involved in protein sorting in the trans-Golgi network. Recent evidence suggests that DDX41 also plays a role in the innate immune response by sensing intracellular viral DNA, triggering TBK1 and IRF3 activation, leading to a type I interferon immune response.

Supplier: Rockland Immunochemical

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 (3).

Supplier: Bioss

SRPK2 belongs to the protein kinase superfamily. It phosphorylates RS domain-containing proteins, such as SFRS1 and SFRS2 on serine residues. It has a role in spliceosome assembly and in mediating the trafficking of splicing factors and appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids. SRPK2 highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney.

Supplier: Bioss

SRPK2 belongs to the protein kinase superfamily. It phosphorylates RS domain-containing proteins, such as SFRS1 and SFRS2 on serine residues. It has a role in spliceosome assembly and in mediating the trafficking of splicing factors and appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids. SRPK2 highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney.

Supplier: Bioss

SRPK2 belongs to the protein kinase superfamily. It phosphorylates RS domain-containing proteins, such as SFRS1 and SFRS2 on serine residues. It has a role in spliceosome assembly and in mediating the trafficking of splicing factors and appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids. SRPK2 highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney.

Supplier: Prosci

DDX41 Antibody: DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp, are putative RNA helicases implicated in several cellular processes involving modifications of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. DDX41, also known as Abstrakt, interacts with and regulates the expression of sorting nexin-2 (SNX2), a protein involved in protein sorting in the trans-Golgi network. Recent evidence suggests that DDX41 also plays a role in the innate immune response by sensing intracellular viral DNA, triggering TBK1 and IRF3 activation, leading to a type I interferon immune response.

Supplier: Bioss

SRPK2 belongs to the protein kinase superfamily. It phosphorylates RS domain-containing proteins, such as SFRS1 and SFRS2 on serine residues. It has a role in spliceosome assembly and in mediating the trafficking of splicing factors and appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids. SRPK2 highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney.

Supplier: AVANTOR PERFORMANCE MATERIAL LLC

J.T.Baker® Endonuclease Biotech Reagent meets the strictest cGMP standards and is designed for the degradation of both single stranded and double stranded DNA and RNA. J.T.Baker® Endonuclease Biotech Reagent is used to ensure host cell DNA impurities are removed; driving process efficiency by lowering viscosity and preventing aggregation. J.T.Baker® Endonuclease Biotech Reagent is an enzyme based upon the native endonuclease of Serratia marcescens, enabling rapid clearance of residual DNA and RNA during the production and purification of both recombinant proteins and viral vectors. Non-animal origin. Absence of proteolytic activity. The purity of materials in non-negotiable. J.T.Baker® Endonuclease Biotech Reagent acts to degrade and eliminate extraneous genetic material, ensuring the pristine quality of your final product.

Supplier: Prosci

DDX41 Antibody: DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp, are putative RNA helicases implicated in several cellular processes involving modifications of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. DDX41, also known as Abstrakt, interacts with and regulates the expression of sorting nexin-2 (SNX2), a protein involved in protein sorting in the trans-Golgi network. Recent evidence suggests that DDX41 also plays a role in the innate immune response by sensing intracellular viral DNA, triggering TBK1 and IRF3 activation, leading to a type I interferon immune response.

Supplier: Bioss

SRPK2 belongs to the protein kinase superfamily. It phosphorylates RS domain-containing proteins, such as SFRS1 and SFRS2 on serine residues. It has a role in spliceosome assembly and in mediating the trafficking of splicing factors and appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids. SRPK2 highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney.

Supplier: Bioss

SRPK2 belongs to the protein kinase superfamily. It phosphorylates RS domain-containing proteins, such as SFRS1 and SFRS2 on serine residues. It has a role in spliceosome assembly and in mediating the trafficking of splicing factors and appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids. SRPK2 highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney.

Supplier: Bioss

SRPK2 belongs to the protein kinase superfamily. It phosphorylates RS domain-containing proteins, such as SFRS1 and SFRS2 on serine residues. It has a role in spliceosome assembly and in mediating the trafficking of splicing factors and appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids. SRPK2 highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney.

Supplier: Rockland Immunochemical

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: Bioss

SRPK2 belongs to the protein kinase superfamily. It phosphorylates RS domain-containing proteins, such as SFRS1 and SFRS2 on serine residues. It has a role in spliceosome assembly and in mediating the trafficking of splicing factors and appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids. SRPK2 highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney.

Supplier: Bioss

SRPK2 belongs to the protein kinase superfamily. It phosphorylates RS domain-containing proteins, such as SFRS1 and SFRS2 on serine residues. It has a role in spliceosome assembly and in mediating the trafficking of splicing factors and appears to mediate HBV core protein phosphorylation which is a prerequisite for pregenomic RNA encapsidation into viral capsids. SRPK2 highly expressed in brain, moderately expressed in heart and skeletal muscle and at low levels in lung, liver, and kidney.

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: Rockland Immunochemical

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

Viral infection induces the interferon (IFN) response which triggers the production of an array of anti-viral proteins. Viperin (Virus inhibitory protein, endoplasmic reticulum-associated, interferon-inducible) is expressed in response to IFN-b binding to the IFN receptor, inducing the formation of the IFN-stimulated gene factor 3 complex which then binds to the Viperin promoter. It inhibits many DNA and RNA viruses through a diverse range of mechanisms and is involved in the PRR-mediated innate immune response. Viperin has been shown to be produced in response to TLR3 and TLR4 activation, but not TLR2 and TLR5. It may be involved in the TLR7 and TLR9-induced production of type I IFN by plasmacytoid dendritic cells (pDCs).

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. 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: Bioss

Component of the THO subcomplex of the TREX complex. The TREX complex specifically associates with spliced mRNA and not with unspliced pre-mRNA. It is recruited to spliced mRNAs by a transcription-independent mechanism. Binds to mRNA upstream of the exon-junction complex (EJC) and is recruited in a splicing- and cap-dependent manner to a region near the 5' end of the mRNA where it functions in mRNA export. The recruitment occurs via an interaction between ALYREF/THOC4 and the cap-binding protein NCBP1. DDX39B functions as a bridge between ALYREF/THOC4 and the THO complex. The TREX complex is essential for the export of Kaposi's sarcoma-associated herpesvirus (KSHV) intronless mRNAs and infectious virus production. The recruitment of the TREX complex to the intronless viral mRNA occurs via an interaction between KSHV ORF57 protein and ALYREF/THOC4. Splice factor that is required for the first ATP-dependent step in spliceosome assembly and for the interaction of U2 snRNP with the branchpoint. Has both RNA-stimulated ATP binding/hydrolysis activity and ATP-dependent RNA unwinding activity. Even with the stimulation of RNA, the ATPase activity is weak. Can only hydrolyze ATP but not other NTPs. The RNA stimulation of ATPase activity does not have a strong preference for the sequence and length of the RNA. However, ssRNA stimulates the ATPase activity much more strongly than dsRNA. Can unwind 5' or 3' overhangs or blunt end RNA duplexes in vitro. The ATPase and helicase activities are not influenced by U2AF2 and ALYREF/THOC4.

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: 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).