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1,8-Diaminonaphthalene
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1,8-Diaminonaphthalene
Catalog Number:
(89415-756)
Supplier:
Prosci
Description:
Avian Influenza Neuraminidase 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 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. Although it has been known that cleavage site and glycosylation patterns of the HA protein play important roles in determining the pathogenicity of H5 avian influenza viruses, it has only recently been shown that an additional glycosylation site within the globular head of the NA protein also contributes to the high virulence of the H5N1 virus.
Catalog Number:
(10285-006)
Supplier:
Bioss
Description:
When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection.
Catalog Number:
(10260-552)
Supplier:
Bioss
Description:
Receptor for TNFSF18. Seems to be involved in interactions between activated T-lymphocytes and endothelial cells and in the regulation of T-cell receptor-mediated cell death. Mediated NF-kappa-B activation via the TRAF2/NIK pathway (By similarity).
Supplier:
Spectrum Chemicals
Description:
Water, Reagent, ACS is used in many chemical reactions. Due to its ability to dissolve many ionic compounds, water is a common solvent in inorganic reactions. It is, however, rarely used as a reaction solvent since it is amphoteric and is not able to dissolve reactants very well. As an ACS grade Reagent, Spectrum Chemical manufactured water is used as the quality standard against which other substances are graded and has met the toughest regulatory standards for quality and pureness
Supplier:
Biotium
Description:
Mucosa associated lymphoid tissue lymphoma translocation gene 1 (MALT1) is found in extranodal low-grade B cell lymphomas. MALT1 encodes two Ig-like C2-type domains and fuses with an API2 gene, which is highly expressed in adult lymphoid tissue. The translocation of this MALT1 gene, which maps to human chromosome 18q21, and the apoptosis-inhibiting API2 gene results in an increased development of MALT lymphomas and apoptosis inhibition. Sites at which this API2-MALT1 (11;18)(q21;q21) translocation commonly occurs are within human lung and kidney tissue. MALT lymphoma expresses nuclear Bcl10, which mediates the oligomerization and activation of a MALT1 caspase-like domain. MALT1 mRNA is found in pre-B cells, mature B cells and plasma cells.
CF® dyes are Biotium's next-generation fluorescent dyes. CF®568 is a red fluorescent dye (Ex/Em 562/583 nm) with superior brightness and photostability. It also is compatible with super-resolution imaging by STORM and TIRF.
Catalog Number:
(10236-132)
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:
(10263-186)
Supplier:
Bioss
Description:
AT-motif binding factor 1 (ATBF1) binds to the AT-rich core sequence element in the human a-fetoprotein enhancer (1). Alternative splicing generates the ATBF1-A and ATBF1-B (2,3). While ATBF1-A contains a 920-amino acid extension at the N-terminus, both ATBF1-A and ATBF1-B contain 4 DNA-binding homeobox domains (2,3). Additionally, ATBF1-A contains 23 zinc finger motifs while ATBF1-B contains 18 zinc finger motifs (1–3). The N-terminal extension unique to ATBF1-A has transcriptional repressor activity (4). In the small intestine, ATBF1-A inhibits expression of the brushborder enzyme aminopeptidase-N through direct binding to the AT motif element (5). Besides functioning in transcription regulation, ATBF1 also functions in ATPase activity (6). ATPase activity associated with ATBF1-A is DNA/RNA-dependent and requires both homeobox domains and zinc finger motifs (6). ATBF1 is highly expressed in spleen and brain tissues (7). The gene encoding human ATBF1 maps to chromosome 16q22.3-q23.1 (8).
Catalog Number:
(10329-582)
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:
(10329-558)
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:
(46620-060)
Supplier:
Magid Glove
Description:
This clear vinyl sleeve is completely heat-sealed and great for food processing, meat packing, sanitation and maintenance.
Catalog Number:
(10288-360)
Supplier:
Bioss
Description:
When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection.
Catalog Number:
(10329-576)
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:
(10329-578)
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:
(103273-124)
Supplier:
Novus Biologicals
Description:
The TPGS2 Antibody from Novus Biologicals is a rabbit polyclonal antibody to TPGS2. This antibody reacts with human. The TPGS2 Antibody has been validated for the following applications: Western Blot, Immunohistochemistry, Immunohistochemistry-Paraffin.
Supplier:
Enzo Life Sciences
Description:
The small ubiquitin-related modifier SUMO-1 belongs to the growing family of ubiquitin-related proteins involved in post-translational protein modification. It is present in all eukaryotic kingdoms and is highly conserved from yeast to humans. Whereas invertebrates have only one SUMO gene, three members of the SUMO family have been described in vertebrates, SUMO-1 and the close homologues SUMO-2 and SUMO-3 with some 50% homology between SUMO-1 and SUMO-2/3. The SUMO family members have a short N-terminal extension that is absent in ubiquitin, and the function of which is unknown and the sequence of which varies between the three family members. Unlike ubiquitin, SUMO-1 does not appear to target proteins for degradation but seems to be involved in the modulation of protein-protein interactions. Although having only 18% amino acid sequence identity with ubiquitin, the overall structure closely resembles that of ubiquitin. Whereas the two C-terminal glycine residues required for isopeptide bond formation are conserved between the two molecules, Lys48 found in ubiquitin, and required to generate ubiquitin polymers, is substituted by Gln69in SUMO-1 thereby providing an explanation of why SUMO-1 has not been observed to form polymers. An increasing number of SUMO-1 substrates are being described but three major substrates for SUMO-1 modification are RanGAP1, PML and IκBα proteins.Â
Catalog Number:
(10260-558)
Supplier:
Bioss
Description:
Receptor for TNFSF18. Seems to be involved in interactions between activated T-lymphocytes and endothelial cells and in the regulation of T-cell receptor-mediated cell death. Mediated NF-kappa-B activation via the TRAF2/NIK pathway (By similarity).
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