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Description: Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). RNF25 (RING finger protein 25), also known as AO7, is a 459 amino acid protein that contains one RWD domain and one RING-type zinc finger. Via its RING-type zinc finger (a common domain that contains a conserved cysteine-rich region and is found in a number of viral and eukaryotic proteins), RNF25 is thought to exhibit E2-dependent E3 ubiquitin-protein ligase activity. Specifically, the RING finger of RNF25 interacts with an E2 ligase and, through this interaction, facilitates the ubiquitination of target proteins. RNF25 may also regulate the transcriptional activity of NF-kappa-B, a protein that plays important roles in cell survival, inflammation response, host defense and proliferation.
Catalog Number: 10669-790
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.
Catalog Number: 10668-032
Supplier: Bioss


Description: Avian Influenza Hemagglutinin 1 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.
Catalog Number: 89416-120
Supplier: Prosci


Description: Avian Influenza Hemagglutinin 1 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.
Catalog Number: 10748-646
Supplier: Prosci


Description: Avian Influenza Hemagglutinin 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.
Catalog Number: 10749-974
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.
Catalog Number: 10748-648
Supplier: Prosci


Description: Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). RNF25 (RING finger protein 25), also known as AO7, is a 459 amino acid protein that contains one RWD domain and one RING-type zinc finger. Via its RING-type zinc finger (a common domain that contains a conserved cysteine-rich region and is found in a number of viral and eukaryotic proteins), RNF25 is thought to exhibit E2-dependent E3 ubiquitin-protein ligase activity. Specifically, the RING finger of RNF25 interacts with an E2 ligase and, through this interaction, facilitates the ubiquitination of target proteins. RNF25 may also regulate the transcriptional activity of NF-kappa-B, a protein that plays important roles in cell survival, inflammation response, host defense and proliferation.
Catalog Number: 10669-788
Supplier: Bioss


Description: Avian Influenza Hemagglutinin 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.
Catalog Number: 89415-762
Supplier: Prosci


Description: Avian Influenza Hemagglutinin 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.
Catalog Number: 89415-760
Supplier: Prosci


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: 10471-798
Supplier: Bioss


Description: Bst2 Antibody: Bst2 was first identified as a novel terminal B-cell-restricted antigen termed HM1.24 that is expressed on certain bone marrow cells as well as other tissues. The surface expression of Bst2 on fibroblast cell lines facilitated the stromal cell-dependent growth of DW34, a pre-B-cell line, suggesting that this protein is involved in pre-B-cell growth. Later experiments also showed it to be upregulated in several myeloma cells. More recently, Bst2 was identified an inhibitor of retroviral release from human cells whose activity is antagonized by the HIV-1 accessory protein Vpu. While Bst2 caused retention of virions on cell surfaces or endocytosis into Bst2-positive compartments, its depletion abolished the viral requirement for Vpu for virus release. This activity may represent a potential therapeutic strategy for the treatment of HIV/AIDS.
Catalog Number: 89416-634
Supplier: Prosci


Description: The Jumonji / JARID2 Antibody [DyLight 405] from Novus Biologicals is a rabbit polyclonal antibody to Jumonji / JARID2. This antibody reacts with human, mouse, rabbit. The Jumonji / JARID2 Antibody [DyLight 405] has been validated for the following applications: Western Blot, Immunohistochemistry, Immunocytochemistry / Immunofluorescence, Immunohistochemistry-Paraffin.
Catalog Number: 103368-968
Supplier: Novus Biologicals


Description: Transmembrane adapter protein which associates with KLRK1 to form an activation receptor KLRK1-HCST in lymphoid and myeloid cells; this receptor plays a major role in triggering cytotoxicity against target cells expressing cell surface ligands such as MHC class I chain-related MICA and MICB, and UL16-binding proteins (ULBPs); these ligands are up-regulated by stress conditions and pathological state such as viral infection and tumor transformation. Functions as docking site for PI3-kinase PIK3R1 and GRB2. Interaction of ULBPs with KLRK1-HCST triggers calcium mobilization and activation of the PIK3R1, MAP2K/ERK, and JAK2/STAT5 signaling pathways. Both PIK3R1 and GRB2 are required for full KLRK1-HCST-mediated activation and ultimate killing of target cells. In NK cells, KLRK1-HCST signaling directly induces cytotoxicity and enhances cytokine production initiated via DAP12/TYROBP-associated receptors. In T-cells, it provides primarily costimulation for TCR-induced signals. KLRK1-HCST receptor plays a role in immune surveillance against tumors and is required for cytolysis of tumors cells; indeed, melanoma cells that do not express KLRK1 ligands escape from immune surveillance mediated by NK cells.
Catalog Number: 76099-834
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.
Catalog Number: 10668-030
Supplier: Bioss


Description: Ubiquitination is an important mechanism through which three classes of enzymes act in concert to target short-lived or abnormal proteins for destruction. The three classes of enzymes involved in ubiquitination are the ubiquitin-activating enzymes (E1s), the ubiquitin-conjugating enzymes (E2s) and the ubiquitin-protein ligases (E3s). RNF25 (RING finger protein 25), also known as AO7, is a 459 amino acid protein that contains one RWD domain and one RING-type zinc finger. Via its RING-type zinc finger (a common domain that contains a conserved cysteine-rich region and is found in a number of viral and eukaryotic proteins), RNF25 is thought to exhibit E2-dependent E3 ubiquitin-protein ligase activity. Specifically, the RING finger of RNF25 interacts with an E2 ligase and, through this interaction, facilitates the ubiquitination of target proteins. RNF25 may also regulate the transcriptional activity of NF-kappa-B, a protein that plays important roles in cell survival, inflammation response, host defense and proliferation.
Catalog Number: 10669-794
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: 10669-650
Supplier: Bioss


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