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Supplier: Greiner Bio-One
Description: Tubes are designed for routine use in immunohematology testing and viral marker testing in screening and clinical laboratories.
Supplier: VWR International
Description: VWR® One-Step RT-qPCR Kit is designed to facilitate rapid, sensitive, and precise detection and quantification of various RNA sequences via dye-based qPCR. It features a distinctive universal passive reference dye that is compatible with ROX-dependent and ROX-independent qPCR instruments.
Supplier: VWR International
Description: VWR® Probe One-Step RT-qPCR Master Mix with UDG is designed for the detection and quantitation of RNA targets and is an ideal choice for multiplex applications. It features a distinctive universal passive reference dye that is compatible with ROX-dependent and ROX-independent qPCR instruments.
Catalog Number: (103395-782)
Supplier: Novus Biologicals
Description: The Canine Distemper Virus Antibody (DV2-12) [DyLight 680] 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 680] has been validated for the following applications: Western Blot, ELISA, Immunohistochemistry-Paraffin, Immunohistochemistry-Frozen.


Catalog Number: (103357-544)
Supplier: Novus Biologicals
Description: The Polyoma Virus, Large T Antigen Antibody (PyLT) [DyLight 755] 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 755] has been validated for the following applications: Western Blot, Immunocytochemistry / Immunofluorescence.


Catalog Number: (76101-670)
Supplier: Bioss
Description: Multifunctional protein that may modulate protein degradation pathways, apoptosis, transcription, signal transduction, cell cycle progress, and genetic stability by directly or indirectly interacting with hosts factors. Does not seem to be essential for HBV infection. May be directly involved in development of cirrhosis and liver cancer (hepatocellular carcinoma). Most of cytosolic activities involve modulation of cytosolic calcium. The effect on apoptosis is controversial depending on the cell types in which the studies have been conducted. By binding to human DDB1, may affect cell viability and stimulate genome replication. May induce apoptosis by localizing in mitochondria and causing loss of mitochondrial membrane potential. May also modulate apoptosis by binding human CFLAR, a key regulator of the death-inducing signaling complex (DISC). Moderately stimulates transcription of many different viral and cellular transcription elements. Promoters and enhancers stimulated by HBx contain DNA binding sites for NF-kappa-B, AP-1, AP-2, c-EBP, ATF/CREB, or the calcium-activated factor NF-AT. May bind bZIP transcription factors like CREB1 (By similarity).


Catalog Number: (102980-148)
Supplier: Adipogen
Description: IL-36alpha (IL-1F6), IL-36beta (IL-1F8) and IL-36gamma (IL-1F9) bind to IL-36R (IL-1Rrp2) and IL-1RAcP, activating similar intracellular signals as IL-1 and are inhibited by IL-36Ra. The expression of IL-36 cytokines has been shown to occur at different sites including the lung and skin and can be derived from diverse cell types including keratinocytes, bronchial epithelium as well as macrophages, monocytes and different T cell subsets. IL-36 family members induce the production of proinflammatory cytokines, including IL-12, IL-1beta, IL-6, TNF-alpha and IL-23 in BMDC and CD4 T cells, thus promoting neutrophil influx, dendritic cell (DC) activation, polarization of T helper type 1 (Th1) and IL-17-producing T cells (alphabeta T cells and gammadelta T cells) and keratinocyte proliferation. These cytokines may represent potential targets for immune-mediated inflammatory conditions or, alternatively, could be used as adjuvants in vaccination. IL-36gamma is also induced in the lung in various models of asthma and can be produced by bronchial epithelial cells in response to viral infection, smoke or inflammatory cytokines.


Catalog Number: (10322-284)
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.


Catalog Number: (10282-716)
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.


Catalog Number: (10354-664)
Supplier: Bioss
Description: Serine kinase that plays an essential role in the NF-kappa-B signaling pathway which is activated by multiple stimuli such as inflammatory cytokines, bacterial or viral products, DNA damages or other cellular stresses. Acts as part of the canonical IKK complex in the conventional pathway of NF-kappa-B activation and phosphorylates inhibitors of NF-kappa-B on 2 critical serine residues. These modifications allow polyubiquitination of the inhibitors and subsequent degradation by the proteasome. In turn, free NF-kappa-B is translocated into the nucleus and activates the transcription of hundreds of genes involved in immune response, growth control, or protection against apoptosis. In addition to the NF-kappa-B inhibitors, phosphorylates several other components of the signaling pathway including NEMO/IKBKG, NF-kappa-B subunits RELA and NFKB1, as well as IKK-related kinases TBK1 and IKBKE. IKK-related kinase phosphorylations may prevent the overproduction of inflammatory mediators since they exert a negative regulation on canonical IKKs. Also phosphorylates other substrates including NCOA3, BCL10 and IRS1. Within the nucleus, acts as an adapter protein for NFKBIA degradation in UV-induced NF-kappa-B activation.


Catalog Number: (75790-932)
Supplier: Prosci
Description: Ubiquitin-Like Protein ISG15 (ISG15) is a ubiquitin-like protein that becomes conjugated to many cellular proteins upon activation by interferon-alpha and -beta. Several functions have been ascribed to the encoded protein, including chemotactic activity towards neutrophils, direction of ligated target proteins to intermediate filaments, cell-to-cell signaling, and antiviral activity during viral infections. While conjugates of this protein have been found to be noncovalently attached to intermediate filaments, this protein is sometimes secreted. ISG15 becomes conjugated to a diverse set of proteins after IFN-alpha/beta stimulation or microbial challenge. The functions or biochemical consequences ISG15 conjugation to proteins are not yet known, but it appears that this modification does not target proteins for proteasomal degradation. ISG15 shows specific chemotactic activity towards neutrophils and activates them to induce release of eosinophil chemotactic factors. Upon interferon treatment, ISG15 can be detected in both free and conjugated forms, and is secreted from monocytes and lymphocytes where it can function as a cytokine. In the cell, ISG15 co-localizes with intermediate filaments and ISGylation may modulate the JAK-STAT pathway or certain aspects of neurological disease.


Catalog Number: (10410-052)
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.


Catalog Number: (10283-786)
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.


Catalog Number: (76079-874)
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.


Catalog Number: (10329-580)
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 Hemagglutinin recognize the influenza hemagglutinin epitope, which has been used extensively as a general epitope tag in expression vectors. The extreme specificity of this antibody allows for unambiguous identification and quantitative analysis of the tagged protein.


Catalog Number: (10281-020)
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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