You Searched For: viral+rna

Catalog Number: (103396-942)

Supplier: Novus Biologicals

Description: The Calicivirus Antibody (FCV1-43) [DyLight 650] from Novus Biologicals is a mouse monoclonal antibody to Calicivirus. This antibody reacts with virus. The Calicivirus Antibody (FCV1-43) [DyLight 650] has been validated for the following applications: Western Blot, ELISA, Immunohistochemistry, Immunohistochemistry-Paraffin.

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Catalog Number: (103395-784)

Supplier: Novus Biologicals

Description: The Canine Distemper Virus Antibody (DV2-12) [DyLight 755] from Novus Biologicals is a mouse monoclonal antibody to Canine Distemper Virus. This antibody reacts with canine, virus. The Canine Distemper Virus Antibody (DV2-12) [DyLight 755] has been validated for the following applications: Western Blot, ELISA, Immunohistochemistry-Paraffin, Immunohistochemistry-Frozen.

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Catalog Number: (10471-802)

Supplier: Bioss

Description: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes. Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes. Promotes ubiquitination of RAPGEF2. According to PubMed:18562292 the direct link between NEDD4 and PTEN regulation through polyubiquitination described in PubMed:17218260 is questionable. Involved in ubiquitination of ERBB4 intracellular domain E4ICD. Involved in the budding of many viruses. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. Ubiquitinates TNK2 and regulates EGF-induced degradation of EGFR and TNF2. Involved in the ubiquitination of ebola virus VP40 protein and this ubiquitination plays a role in facilitating viral budding.

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Catalog Number: (76116-914)

Supplier: Bioss

Description: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Involved in the pathway leading to the degradation of VEGFR-2/KDFR, independently of its ubiquitin-ligase activity. Monoubiquitinates IGF1R at multiple sites, thus leading to receptor internalization and degradation in lysosomes. Ubiquitinates FGFR1, leading to receptor internalization and degradation in lysosomes. Promotes ubiquitination of RAPGEF2. According to PubMed:18562292 the direct link between NEDD4 and PTEN regulation through polyubiquitination described in PubMed:17218260 is questionable. Involved in ubiquitination of ERBB4 intracellular domain E4ICD. Involved in the budding of many viruses. Part of a signaling complex composed of NEDD4, RAP2A and TNIK which regulates neuronal dendrite extension and arborization during development. Ubiquitinates TNK2 and regulates EGF-induced degradation of EGFR and TNF2. Involved in the ubiquitination of ebola virus VP40 protein and this ubiquitination plays a role in facilitating viral budding.

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Catalog Number: (103357-540)

Supplier: Novus Biologicals

Description: The Polyoma Virus, Large T Antigen Antibody (PyLT) [DyLight 680] from Novus Biologicals is a mouse monoclonal antibody to Polyoma Virus, Large T Antigen. This antibody reacts with human, virus. The Polyoma Virus, Large T Antigen Antibody (PyLT) [DyLight 680] has been validated for the following applications: Western Blot, Immunocytochemistry / Immunofluorescence.

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Catalog Number: (89416-110)

Supplier: Prosci

Description: Avian Influenza Hemagglutinin 2 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 can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. There was some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species-jumping ability.

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Catalog Number: (10668-034)

Supplier: Bioss

Description: E3 ubiquitin-protein ligase that promotes the degradation of insoluble ubiquitinated proteins, including insoluble PAX6, poly-Gln repeat expanded HTT and poly-Ala repeat expanded ARX. Mediates PAX6 ubiquitination leading to proteasomal degradation, thereby modulating cortical neurogenesis. May also inhibit PAX6 transcriptional activity, possibly in part by preventing the binding of PAX6 to its consensus sequences. May contribute to the regulation of the intracellular level of HN (humanin) or HN-containing proteins through the proteasomal degradation pathway. Mediates MED15 ubiquitination leading to proteasomal degradation. May contribute to the innate restriction of retroviruses. Upon overexpression, reduces HIV-1 and murine leukemia virus infectivity, by suppressing viral gene expression. Antiviral activity depends on a functional E3 ubiquitin-protein ligase domain. May regulate TRIM5 turnover via the proteasome pathway, thus counteracting the TRIM5-mediated cross-species restriction of retroviral infection at early stages of the retroviral life cycle.

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Catalog Number: (10800-262)

Supplier: Rockland Immunochemical

Description: 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 can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. There was some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species-jumping ability.

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Catalog Number: (10284-654)

Supplier: Bioss

Description: The adenovirus E1B protein is a viral homolog of the Bcl-2 family of proteins that are involved in regulating cell death. A family of interacting proteins, which are designated Nip or Bnip and include BNIP-1, BNIP-2, BNIP-3 and Nix, associate with both the E1B protein and Bcl-2 proteins to mediate apoptotic signaling. BNIP-1 contains a hydrophobic transmembrane domain, which enables its localization to the nuclear envelope, endoplasmic recticulum and mitochondria. BNIP-2, (previously designated Nip2 and Nip21 in human and mouse respectively), shares homology with the non-catalytic domain of Cdc42 GTPase-activating protein (Cdc42GAP). Through binding to Cdc42GAP, BNIP-2 enhances the GTPase activity of Cdc42GAP, facilitating the hydrolysis of GTP bound to Cdc42 and thereby, mediating the signaling pathways involving receptor kinases, small GTPases and apoptotic proteins. Nix, which is also designated Nip3L or Bnip3L, is highly related to BNIP-3, and both proteins localize to the mitochondria where they associate with Bcl-2 proteins. BNIP-3 preferentially binds to Bcl-xL and induces apoptosis by suppressing the anti-apoptosis activity of Bcl-xL.

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Catalog Number: (102981-684)

Supplier: Adipogen

Description: The TIM (T cell/transmembrane, immunoglobulin and mucin) family plays a critical role in regulating immune responses, including allergy, asthma, transplant tolerance, autoimmunity and the response to viral infections. The unique structure of TIM immunoglobulin variable region domains allows highly specific recognition of phosphatidylserine (PtdSer), exposed on the surface of apoptotic cells. Tim-3, a type I transmembrane protein, contains an immunoglobulin and a mucin-like domain in its extracellular portion and a tyrosine phosphorylation motif in its cytoplasmic portion. TIM-3 is preferentially expressed on Th1 and Tc1 cells, and generates an inhibitory signal resulting in apoptosis of Th1 and Tc1 cells. TIM-3 is also expressed on some dendritic cells and can mediate phagocytosis of apoptotic cells and cross-presentation of antigen. Tim-3 functions to inhibit aggressive Th1-mediated auto- and alloimmune responses. Tim-3 pathway blockade by administration of Tim-3:Fc fusion protein accelerates diabetes in nonobese diabetic mice, causes hyperproliferation of Th1 cells and Th1 cytokine release in an experimental autoimmune encephalomyelitis (EAE) model and prevents acquisition of transplantation tolerance induced by costimulation blockade.

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Supplier: Shenandoah Biotechnology

Description: Interferon gamma (IFNγ) is a type II interferon that is critical during adaptive and innate immune responses to infection. IFNγ is produced by T cells and natural killer cells following antigen-specific activation. IFNγ binds IFNγ receptors (IFNγR1 and IFNγR2), which are expressed on most immune cells, to activate the JAK-STAT pathway. IFNγ-induced signaling increases the expression of class 1 major histocompatibility complex (MHC) molecules. Human IFNγ is not cross-reactive with mouse IFNγ.

Catalog Number: (10320-554)

Supplier: Bioss

Description: Hepatitis B Virus (HBV) infection induces a disease state characterised by liver damage, inflammation and viral persistence. Infection also increases the risk of hepatocellular carcinoma. HBV belongs to the Hepadnaviridae family of viruses. Its genome consists of partially double stranded circular DNA. The DNA is enclosed in a nucleocapsid, or core antigen (HBcAg), which is surrounded by a spherical envelope (surface antigen or HBsAg). The core antigen shares its sequences with the e antigen (HBeAg) but no cross reactivity between the two proteins has been observed. The HBV genome also encodes a DNA polymerase that also acts as a reverse transcriptase. Hepatitis B infection is normally diagnosed from serological tests that detect HBsAg but as the disease progresses this antigen may no longer be present in the blood and tests for HBcAg are used. If HBsAg can be detected in the blood for longer than six months, chronic hepatitis B is diagnosed. The antigenic determinant of the protein moiety of the HBsAg determines specific characteristics of different serotypes and provides the basis of immunodetection. HBsAg has antigenic heterogeneity, specifically, two pairs of sub specific determinants, d/y and w/r allow the following combinations: adw, ayw, adr, ayr.

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Catalog Number: (103395-768)

Supplier: Novus Biologicals

Description: The Canine Distemper Virus Antibody (DV2-12) [Biotin] from Novus Biologicals is a mouse monoclonal antibody to Canine Distemper Virus. This antibody reacts with canine, virus. The Canine Distemper Virus Antibody (DV2-12) [Biotin] has been validated for the following applications: Western Blot, ELISA, Immunohistochemistry-Paraffin, Immunohistochemistry-Frozen.

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Catalog Number: (10283-766)

Supplier: Bioss

Description: 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.

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Catalog Number: (10410-078)

Supplier: Bioss

Description: 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.

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Catalog Number: (10282-728)

Supplier: Bioss

Description: 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.

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