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Catalog Number: (10314-246)
Supplier: Bioss
Description: Transcriptional activator. Binds the cAMP response element (CRE) (consensus: 5'-GTGACGT[AC][AG]-3'), a sequence present in many viral and cellular promoters. Cooperates with FOXO1 in osteoblasts to regulate glucose homeostasis through suppression of beta-cell production and decrease in insulin production (By similarity). It binds to a Tax-responsive enhancer element in the long terminal repeat of HTLV-I. Regulates the induction of DDIT3/CHOP and asparagine synthetase (ASNS) in response to ER stress. In concert with DDIT3/CHOP, activates the transcription of TRIB3 and promotes ER stress-induced neuronal apoptosis by regulating the transcriptional induction of BBC3/PUMA. Activates transcription of SIRT4. Regulates the circadian expression of the core clock component PER2 and the serotonin transporter SLC6A4. Binds in a circadian time-dependent manner to the cAMP response elements (CRE) in the SLC6A4 and PER2 promoters and periodically activates the transcription of these genes.


Catalog Number: (89416-448)
Supplier: Prosci
Description: ATG12 Antibody: Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components. This process is negatively regulated by TOR (Target of rapamycin) through phosphorylation of autophagy protein APG1. ATG12, another member of the autophagy protein family, forms a conjugate with ATG5; this conjugate has a ubiquitin-protein ligase (E3)-like activity for protein lipidation in autophagy. This conjugate also associates with innate immune response proteins such as RIG-I and VISA (also known as IPS-1), inhibiting type I interferon production and permitting viral replication in host cells. ATG12 has also been shown to interact with ATG10 in human embryonic kidney cells in the presence of ATG7. At least two isoforms of ATG12 are known to exist.


Catalog Number: (75789-564)
Supplier: Prosci
Description: Nectin-1 is a type I transmembrane glycoprotein belonging to the Ig superfamily. Nectin-1 promotes cell-cell contacts by forming homophilic or heterophilic trans-dimers. Heterophilic interactions have been detected between Nectin-1 and Nectin-3 and between Nectin-1 and Nectin-4. Nectin ECDs contain three Ig like domains: an N terminal V type that mediates ligand binding, and two C2 type. Nectin-1 binds viral Glycoprotein D to mediate Herpesvirus (but not Poxvirus) entry into vaginal mucosa, sensory neurons and fibroblasts. In forming adherens junctions and synapses, Nectin-1 and Nectin-3 initiate cell-cell interactions, recruiting alphav beta 3 integrin extracellularly and cadherins intracellularly through afadin and other junctional proteins. These interactions organize the cytoskeleton, strengthen attachment to basement membrane and promote further cell-cell connections. Nectin-1 and Nectin-3 have been found to localize assymetrically along the chemical synapse, with Nectin-1 primarily on the axonal side and Nectin-3 on the dendritic side. Deficiency of Nectin-1 can result in cleft lip/palate ectodermal dysplasia. Nectin-1 downregulation in epithelial cancers is mediated in part by ectodomain shedding, but it may contribute to invasiveness.


Catalog Number: (10483-218)
Supplier: Bioss
Description: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro, in the presence or in the absence of BRCA1-BARD1 E3 ubiquitin-protein ligase complex, catalyzes the synthesis of 'Lys-48'-linked polyubiquitin chains. Does not transfer ubiquitin directly to but elongates monoubiquitinated substrate protein. Mediates the selective degradation of short-lived and abnormal proteins, such as the endoplasmic reticulum-associated degradation (ERAD) of misfolded lumenal proteins. Ubiquitinates huntingtin. May mediate foam cell formation by the suppression of apoptosis of lipid-bearing macrophages through ubiquitination and subsequence degradation of p53/TP53. Proposed to be involved in ubiquitination and proteolytic processing of NF-kappa-B; in vitro supports ubiquitination of NFKB1. In case of infection by cytomegaloviruses may be involved in the US11-dependent degradation of MHC class I heavy chains following their export from the ER to the cytosol. In case of viral infections may be involved in the HPV E7 protein-dependent degradation of RB1.


Catalog Number: (10334-980)
Supplier: Bioss
Description: Influenza A virus is a major public health threat. 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.Influenza A Virus [A/California/04/2009(H1N1)]


Catalog Number: (75789-658)
Supplier: Prosci
Description: Surfactant Pulmonary-Associated Protein D (SP-D) is a 43 kDa member of the collectin family of innate immune modulators. Its principal components consist of a collagen-like region and a C-terminal carbohydrate recognition domain (CRD), a structure that places it in a subset of pattern recognition proteins termed defense collagens. SP-D is constitutively secreted by alveolar lining cells and epithelium associated with tubular structures and induced in cardiac smooth muscle and endothelial cells. It binds both secreted and transmembrane proteins that transduce its function. It binds human neutrophil defensins, modulating influenza anti-viral defense. It binds MD-2/LY96, a secreted protein that cooperates with Toll-like receptors (TLRs) in the response of macrophages to bacterial lipopolysaccharides (LPS) or cell wall components. It also binds macrophage CD14 and TLRs directly, blocking binding of LPS and down-regulating TNF- alpha secretion. SP-D binding of both SIRP alpha and the calreticulin/CD91 complex on macrophages allows for a graded response to environmental challenge.


Catalog Number: (76195-052)
Supplier: Prosci
Description: Recognizes a protein of 55kDa, which is identified as fascin-1. Its actin binding ability is regulated by phosphorylation. Antibody to fascin-1 is a very sensitive marker for Reed-Sternberg cells and variants in nodular sclerosis, mixed cellularity, and lymphocyte depletion Hodgkin's disease. It is uniformly negative in lymphoid cells, plasma cells, and myeloid cells. Fascin-1 is also expressed in dendritic cells. This marker may be helpful to distinguish between Hodgkin lymphoma and non-Hodgkin lymphoma in difficult cases. Also, the lack of expression of fascin-1 in the neoplastic follicles in follicular lymphoma may be helpful in distinguishing these lymphomas from reactive follicular hyperplasia in which the number of follicular dendritic cells is normal or increased. Antibody to fascin-1 has been suggested as a prognostic marker in neuroendocrine neoplasms of the lung as well as in ovarian cancer. Fascin-1 expression may be induced by Epstein-Barr virus (EBV) infection of B cells with the possibility that viral induction of fascin in lymphoid or other cell types must also be considered in EBV-positive cases.


Catalog Number: (10335-198)
Supplier: Bioss
Description: Influenza A virus is a major public health threat. 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.Influenza A Virus [A/California/04/2009(H1N1)]


Catalog Number: (10236-134)
Supplier: Bioss
Description: Influenza A virus is a major public health threat. 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.


Catalog Number: (10801-110)
Supplier: Rockland Immunochemical
Description: DC-SIGN Monoclonal antibody detects human DC-SIGN. Dendritic cells (DCs) that control immune responses were recently found to capture and transport HIV from the mucosal area to remote lymph nodes , where DCs hand over HIV to CD4+ T lymphocytes. DCs also amplify the amount of virus and extend the duration of viral infectivity. Multiple strains of HIV-1, HIV-2 and SIV bind to DCs via DC-SIGN. ICAM-3 is the natural ligand for DC-SIGN. A DC-SIGN homologue (termed DC-SIGNR, L-SIGN, and DC-SIGN2) was identified recently. DC-SIGN forms a novel gene family with DC-SIGNR and many alternatively spliced isoforms of DC-SIGN and DC-SIGNR. The expression of DC-SIGN was found in mucosal tissues including placenta, small intestine, and rectum. Anti-DC-SIGN Monoclonal antibodies are ideal for investigators involved in infectious disease research.


Catalog Number: (89416-680)
Supplier: Prosci
Description: TRIM30 Antibody: TRIM30 belongs to a family of the tripartite motif (TRIM) proteins involved in the regulation of cell proliferation, differentiation, development, oncogenesis, apoptosis and antiviral responses. The TRIM protein family is an expanding family of RING ('really interesting new gene') proteins, also known as RBCC proteins as they contain an RBCC motif, which comprises a RING domain, one or two B-boxes and a predicted coiled-coil region. Studies have shown that some TRIM family members are critical to innate immunity; TRIM5, TRIM19 and TRIM25, for example, have been shown to restrict viral infection. A recent study shows that TRIM30 functions as a negative modulator of the TLR signaling pathway, by targeting TAB2 and TAB3, and contributes to the inhibition of TLR-mediated NF-kappa B activation. The importance of TRIM30 in the attenuation or termination of NF-kappa B activation suggests that targeting of TAB2 and TAB3 by TRIM30 alpha may be a mechanism for modulating many types of immune responses.


Catalog Number: (10669-642)
Supplier: Bioss
Description: The RING-type zinc finger motif is present in a number of viral and eukaryotic proteins and is made of a conserved cysteine-rich domain that is able to bind two zinc atoms. Proteins that contain this conserved domain are generally involved in the ubiquitination pathway of protein degradation. RNF180 (ring finger protein 180), also known as Rines, is a 592 single-pass membrane protein that contains a single RING-type zinc finger. Expressed as three alternatively spliced isoforms, RNF180 is well conserved among vertebrates. RNF180 is expressed in brain, kidney, testis and uterus and localizes to the endoplasmic reticulum. RNF180 is an E3 ubiquitin ligase involved in the ubiquitin-proteasome pathway. RNF180 is encoded by a gene located on human chromosome 5, which contains 181 million base pairs and comprises nearly 6% of the human genome. Deletion of the p arm of chromosome 5 leads to Cri du chat syndrome, while deletion of the q arm, or of chromosome 5 altogether, is common in therapy-related acute myelogenous leukemias and myelodysplastic syndrome.


Catalog Number: (103396-932)
Supplier: Novus Biologicals
Description: The Calicivirus Antibody (FCV1-43) [DyLight 350] from Novus Biologicals is a mouse monoclonal antibody to Calicivirus. This antibody reacts with virus. The Calicivirus Antibody (FCV1-43) [DyLight 350] has been validated for the following applications: Western Blot, ELISA, Immunohistochemistry, Immunohistochemistry-Paraffin.


Catalog Number: (76194-128)
Supplier: Prosci
Description: Recognizes a protein of 16-27kDa, identified as human interferon-II) (IFN-(II). Its epitope maps between aa112-148 of IFN-II) (total aa172). This mAb is specific for IFN-(II) and does not cross-react with IFN-(I). The site recognized by this mAb is called "site I" and is responsible for the antiviral and anti-proliferative activities of IFN-(II). Epitopes of N27 and N39 mAbs are different and represent a good combination of antibodies to set up an ELISA assay for the quantitation of IFN-(II) after viral infections. The IFN- family consists of 24 or more genes or pseudo-genes. IFN-II) is one of the two distinct families (I and II) of human IFN-. The -interferon are mainly produced by lymphocytes, monocytes, macrophages, and cell lines such as Namalwa and KG1 following induction by viruses, nucleic acids, and glucocorticoid hormones. They are involved in virus resistance on target cells, inhibition of cell proliferation, induction of cytokines and regulation of expression of MHC class I antigens.


Catalog Number: (10471-796)
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.


Catalog Number: (10471-804)
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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