Multidrug-resistant enterococci are main causes of hospital-acquired infections. Immunotherapy with monoclonal antibodies (MAbs) concentrating on bacterial antigens could be a worthwhile remedy choice on this setting.
Here, we describe the event of two MAbs by way of hybridoma expertise that concentrate on antigens from essentially the most clinically related enterococcal species.
Diheteroglycan (DHG), a well-characterized capsular polysaccharide of Enterococcus faecalis, and the secreted antigen A (SagA), an immunogenic protein from Enterococcus faecium, are each immunogens which were confirmed to boost opsonic and cross-reactive antibodies against enterococcal strains.
Development of Opsonic Mouse Monoclonal Antibodies against Multidrug-Resistant Enterococci.
For this objective, a conjugated type of the native DHG with SagA was used to boost the antibodies in mice, whereas enzyme-linked immunosorbent assay and opsonophagocytic assay had been mixed within the choice course of of hybridoma cells producing immunoreactive and opsonic antibodies concentrating on the chosen antigens.
Description: Proteins encoded by the v-Rel viral oncogene and its cellular homolog, c-Rel, are members of a family of transcription factors that include the two subunits of the transcription factor N B (p50 and p65) and the Drosophila maternal morphogen, dorsal. Both proteins specifically bind to DNA sequences that are the same or slight variations of the 10 bp B sequence in the immunoglobulin light chain enhancer. This same sequence is also present in a number of other cellular and viral enhancers. The DNA binding activity of NF B is activated and NF B is subsequently transported from the cytoplasm to the nucleus in cells exposed to mitogens or growth factors. cDNAs encoding precursors for two distinct proteins of the same size have been described, designated p105 and p100. The p105 precursor contains p50 at its N-terminus and a C-terminal region that when expressed as a separate molecule, designated pdI, binds to p50 and regulates its activity.
Description: Proteins encoded by the v-Rel viral oncogene and its cellular homolog, c-Rel, are members of a family of transcription factors that include the two subunits of the transcription factor N B (p50 and p65) and the Drosophila maternal morphogen, dorsal. Both proteins specifically bind to DNA sequences that are the same or slight variations of the 10 bp B sequence in the immunoglobulin light chain enhancer. This same sequence is also present in a number of other cellular and viral enhancers. The DNA binding activity of NF B is activated and NF B is subsequently transported from the cytoplasm to the nucleus in cells exposed to mitogens or growth factors. cDNAs encoding precursors for two distinct proteins of the same size have been described, designated p105 and p100. The p105 precursor contains p50 at its N-terminus and a C-terminal region that when expressed as a separate molecule, designated pdI, binds to p50 and regulates its activity.
Description: Proteins encoded by the v-Rel viral oncogene and its cellular homolog, c-Rel, are members of a family of transcription factors that include the two subunits of the transcription factor N B (p50 and p65) and the Drosophila maternal morphogen, dorsal. Both proteins specifically bind to DNA sequences that are the same or slight variations of the 10 bp B sequence in the immunoglobulin light chain enhancer. This same sequence is also present in a number of other cellular and viral enhancers. The DNA binding activity of NF B is activated and NF B is subsequently transported from the cytoplasm to the nucleus in cells exposed to mitogens or growth factors. cDNAs encoding precursors for two distinct proteins of the same size have been described, designated p105 and p100. The p105 precursor contains p50 at its N-terminus and a C-terminal region that when expressed as a separate molecule, designated pdI, binds to p50 and regulates its activity.
Description: Proteins encoded by the v-Rel viral oncogene and its cellular homolog, c-Rel, are members of a family of transcription factors that include the two subunits of the transcription factor N B (p50 and p65) and the Drosophila maternal morphogen, dorsal. Both proteins specifically bind to DNA sequences that are the same or slight variations of the 10 bp B sequence in the immunoglobulin light chain enhancer. This same sequence is also present in a number of other cellular and viral enhancers. The DNA binding activity of NF B is activated and NF B is subsequently transported from the cytoplasm to the nucleus in cells exposed to mitogens or growth factors. cDNAs encoding precursors for two distinct proteins of the same size have been described, designated p105 and p100. The p105 precursor contains p50 at its N-terminus and a C-terminal region that when expressed as a separate molecule, designated pdI, binds to p50 and regulates its activity.
Description: Proteins encoded by the v-Rel viral oncogene and its cellular homolog, c-Rel, are members of a family of transcription factors that include the two subunits of the transcription factor N B (p50 and p65) and the Drosophila maternal morphogen, dorsal. Both proteins specifically bind to DNA sequences that are the same or slight variations of the 10 bp B sequence in the immunoglobulin light chain enhancer. This same sequence is also present in a number of other cellular and viral enhancers. The DNA binding activity of NF B is activated and NF B is subsequently transported from the cytoplasm to the nucleus in cells exposed to mitogens or growth factors. cDNAs encoding precursors for two distinct proteins of the same size have been described, designated p105 and p100. The p105 precursor contains p50 at its N-terminus and a C-terminal region that when expressed as a separate molecule, designated pdI, binds to p50 and regulates its activity.
Description: Proteins encoded by the v-Rel viral oncogene and its cellular homolog, c-Rel, are members of a family of transcription factors that include the two subunits of the transcription factor N B (p50 and p65) and the Drosophila maternal morphogen, dorsal. Both proteins specifically bind to DNA sequences that are the same or slight variations of the 10 bp B sequence in the immunoglobulin light chain enhancer. This same sequence is also present in a number of other cellular and viral enhancers. The DNA binding activity of NF B is activated and NF B is subsequently transported from the cytoplasm to the nucleus in cells exposed to mitogens or growth factors. cDNAs encoding precursors for two distinct proteins of the same size have been described, designated p105 and p100. The p105 precursor contains p50 at its N-terminus and a C-terminal region that when expressed as a separate molecule, designated pdI, binds to p50 and regulates its activity.
Description: Quantitative sandwich ELISA for measuring Human Nuclear factor-KB p65 (NF-KB p65) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
ELISA kit for Human Nuclear factor-KB p65 (NF-KB p65)
Description: Quantitative sandwich ELISA for measuring Human Nuclear factor-KB p65 (NF-KB p65) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
ELISA kit for Human Nuclear factor-KB p65 (NF-KB p65)
Description: Quantitative sandwich ELISA for measuring Human Nuclear factor-KB p65 (NF-KB p65) in samples from cell culture supernatants, serum, whole blood, plasma and other biological fluids.
ELISA kit for Mouse Nuclear factor-KB p65 (NF-KB p65)
Description: NF-kappaB is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappaB is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The heterodimeric p65-p50 complex is the most abundant complex. The dimers bind at kappaB sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappaB sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappaB complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappaB inhibitor (I-kappaB) family. In a conventional activation pathway, I-kappaB is phosphorylated by I-kappaB kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappaB complex which translocates to the nucleus. NF-kappaB heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappaB p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappaB complex.
Description: NF-kappaB is a pleiotropic transcription factor present in almost all cell types and is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli related to many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappaB is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52. The heterodimeric p65-p50 complex is the most abundant complex. The dimers bind at kappaB sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappaB sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappaB complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappaB inhibitor (I-kappaB) family. In a conventional activation pathway, I-kappaB is phosphorylated by I-kappaB kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappaB complex which translocates to the nucleus. NF-kappaB heterodimeric p65-p50 and RelB-p50 complexes are transcriptional activators. The NF-kappaB p50-p50 homodimer is a transcriptional repressor, but can act as a transcriptional activator when associated with BCL3.
Description: A polyclonal antibody raised in Rabbit that recognizes and binds to Human NF-KB p100 (Ab-869). This antibody is tested and proven to work in the following applications:
From this course of, two extremely particular IgG1(κ) MAbs had been obtained, one against the polysaccharide (DHG.01) and one against the protein (SagA.01). Both MAbs exhibited good opsonic killing against the goal bacterial strains: DHG.01 confirmed 90% killing against E. faecalis kind 2, and SagA.01 confirmed 40% killing against E. faecium 11231/6.
In addition, each MAbs confirmed cross-reactivity towards different E. faecalis and E. faecium strains. The sequences from the variable areas of the heavy and light-weight chains had been reconstructed in expression vectors, and the exercise of the MAbs upon expression in eukaryotic cells was confirmed with the identical immunological assays. In abstract, we recognized two opsonic MAbs against enterococci which may very well be used for therapeutic or prophylactic approaches against enterococcal infections.
