nuclear factor kappa light chain enhancer of activated B cells
Pipoxolan suppresses the inflammatory factors of NF-κB, AP-1, and STATs, but activates the antioxidative factor Nrf2 in LPS-stimulated RAW 264.7 murine macrophage cells
Although pipoxolan (PIPO) is a smooth muscle relaxant, anti-inflammatory abilities have not been studied. Therefore, we investigated the molecular mechanism of anti-inflammatory PIPO in lipopolysaccharide (LPS) -induced RAW 264.7 macrophages. In this study, we used the MTT assay to evaluate cytotoxicity of the applied enzyme-linked immunosorbent assay to determine the inflammatory cytokines, and performed Western blotting to assess protein expression.
The results showed that PIPO significantly inhibited the production of cytokines, including nitric oxide, prostaglandin E2, tumor necrosis factor-α and interleukin-6. PIPO also suppresses pro-inflammatory mediator expression with inducible nitric oxide synthase and cyclooxygenase-2. Additionally, PIPO forbidden lane transcription factor of inflammatory several, including the inhibitor of kappa B / nuclear factor of κ chain enhancer light B cells (NF-kB), mitogen-activated protein kinase / activator protein-1 (AP-1),
Janus kinase / signal transducer and activator of transcription (STAT), and pulses like receptor 4 (TLR4) / serine / threonine kinase (Akt). In addition, effective PIPO activated nuclear factor erythroid 2-related factor 2 (Nrf2) / heme oxygenase-1 antioxidant pathway. Collectively, PIPO may attenuate the inflammatory effects through affecting LPS / TLR4 receptor binding; suppress the expression of anti-inflammatory transcription factor NF-kB, AP-1 and STAT; and activate the transcription factor Nrf2 antioxidant in LPS-stimulated RAW 264.7 mouse cells.
Pipoxolan suppresses the inflammatory factors of NF-κB, AP-1, and STATs, but activates the antioxidative factor Nrf2 in LPS-stimulated RAW 264.7 murine macrophage cells
Rhaponticin the effects of oxidative stress and inflammation in the diabetic retina through NRF2 / HO-1 / NF-kB signaling
Oxidative stress and inflammation has long been considered responsible for the development and progression of diabetic retinopathy. On the other hand, rhaponticin (RN) has received scientific attention for its wide range of pharmacological properties. Keeping all this in view, this study was conducted to investigate the potential protective effect of RN to the retina in diabetic rats. Rats were randomly divided into three groups: a control group of mice, rats diabetic groups, diabetes + RN (20 mg / kg body weight for 28 days via the oral route) mice groups. RN supplementation to significantly prevent diabetic mice lose weight reduction end, weekly fasting reduced blood glucose levels and HbA1c levels with a significant increase in serum levels of insulin.
Quantitative polymerase chain reaction and immunohistochemical analysis found increased regulation of Nrf2, NQO-1, HO-1 and upregulation of genes Keap1 and distribution of protein along with a significant level reduces malondialdehyde and increased activity of superoxide dismutase, catalase, and glutathione peroxidase in diabetes RN-treated mice compared to diabetic rats. In addition, treatment of diabetic mice with RN showed downregulated the expression of tumor necrosis factor-α, matrix metalloproteinase-2 and upregulated the expression of interleukin-10 (IL-10) and TIMP-1 in the retina. RN treatment decreased nuclear factor kappa-light-chain-enhancer of activated B cells and increased distribution of IL-10 protein distribution in the retina of diabetic rats. In addition, the RN treatment improved morphological changes were observed in the retina of diabetic rats.
Description: A Monoclonal antibody against Human NF-κB p65. The antibodies are raised in Mouse and are from clone 6H7. This antibody is applicable in WB, E
Human Nuclear Factor Kappa B p65 (NF-κB p65) CLIA Kit
Description: The NF-κB Reporter kit is designed for monitoring the activity of the NF-κB signaling pathway in the cultured cells. The kit contains transfection-ready NF-κB luciferase reporter vector. This reporter contains a firefly luciferase gene under the control of multimerized NF-κB responsive element located upstream of a minimal promoter. The NF-κB reporter is premixed with constitutively-expressing Renilla (sea pansy) luciferase vector, which serves as an internal control for transfection efficiency. The kit also includes a non-inducible firefly luciferase vector premixed with constitutively-expressing Renilla luciferase vector as a negative control. The non-inducible luciferase vector contains a firefly luciferase gene under the control of a minimal promoter, without any additional response elements. The negative control is critical to determining pathway specific effects and background luciferase activity.
Description: The p65 (RELA) heterodimer is the most abundant form of NF-KB. This gene is located on 11q13, which consists of 10 exons and spans about 8.1 kb of DNA. In rat sciatic nerves, the expression of the activated p65 subunit of NFKB was high in the nuclei of premyelinating Schwann cells and then progressively declined until it was nearly absent in adults. The transcriptional activity of NF-kappa-B is stimulated upon phosphorylation of its p65 subunit on serine-276 by protein kinase A(PKA). The transcriptional coactivator CBP/p300 associates with NF-kappa-B through 2 sites, an N-terminal domain that interacts with the C-terminal region of the unphosphorylated protein, and a second domain that only interacts with p65 phosphorylated on serine-276.
Description: RELA, also called NFKB3 or NFKB, p65 subunit is part of the NF-kB complex. The complex is inhibited by I-kappa-B proteins, which inactivates NFkB by trapping it in the cytoplasm. The p65 heterodimer is the most abundant form of NF-kB. It is a nonhistone substrate of HDAC3 and that IKBA-dependent nuclear export of the HDAC3-deacetylated RELA replenishes the depleted cytoplasmic pool of latent NFKB-IKBA complexes for subsequent NF-kB responses. Its nucleocytoplasmic redistribution coincided with export of PPARG, and immunoprecipitation analysis indicated that PPARG-RELA association was dependent on the PPARG C-terminal ligand-binding domain. IKK-dependent phosphorylation of RELA on Ser468 enhanced binding of GCN5 to RELA and its ubiquitination.
Description: Transcription factor p65, also known as NFKB3 or NF-kB p65, is a protein that in humans is encoded by the RELA gene. It is mapped to 11q13.1. NFKB is an essential transcription factor complex involved in all types of cellular processes, including cellular metabolism, chemotaxis, etc, and it may play a role in inflammatory conditions of the peripheral nervous system. Phosphorylation and acetylation of NFKB3 are crucial post-translational modifications required for NFKB activation. It has also been shown to modulate immune responses, and activation of NFKB3 is positively associated with multiple types of cancer. In addition to that, NFKB3 antagonizes TNFR1-JNK proliferative signals in epidermis and plays a nonredundant role in restraining epidermal growth.
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: The NF-κB Transient Pack is designed to provide the tools necessary for transiently transfecting and monitoring the activity of the NF-κB signaling pathway in cultured HEK293 cells. The kit contains transfection-ready vectors containing firefly luciferase as a NF-κB pathway-responsive reporter and constitutively expressing Renilla luciferase as a transfection control. It also includes the Dual Luciferase detection reagents to detect both luciferase activities and specialized medium for growing and assaying HEK293 cells._x000D_The key to the NF-κB Transient Pack is the NF-κB luciferase reporter vector. This reporter contains a firefly luciferase gene under the control of multimerized NF-κB responsive element located upstream of a minimal promoter. The NF-κB reporter is premixed with constitutively-expressing Renilla luciferase vector, which serves as an internal control for transfection efficiency._x000D_The pack also includes a non-inducible firefly luciferase vector premixed with constitutively-expressing Renilla luciferase vector as a negative control. The non-inducible luciferase vector contains a firefly luciferase gene under the control of a minimal promoter, without any additional response elements. The negative control is critical to determining pathway specific effects and background luciferase activity._x000D_Additionally, the pack includes cell culture medium (BPS Medium 1) that has been optimized for use with HEK293 cells*. BPS Medium 1 includes MEM medium, 10% fetal bovine serum, 1% non-essential amino acids, sodium pyruvate, and 1% Pen/Strep. Finally, the pack provides the Dual Luciferase (Firefly-Renilla) Assay System. These reagents provide highly sensitive, stable detection of firefly luciferase activity and Renilla luciferase activity. The dual luciferase reagents can be used directly in cells in growth medium, and can be detected with any luminometer; automated injectors are not required._x000D_*Note: the kit may be used with other cell lines than HEK293, but an alternate cell culture medium may be required for optimal cell growth.
Description: The NF-κB Luciferase Reporter Lentivirus are replication incompetent, HIV-based, VSV-G pseudotyped lentiviral particles that are ready to be transduced into almost all types of mammalian cells, including primary and non-dividing cells. The particles contain a firefly luciferase gene driven by four copies of the NF-κB response element located upstream of the minimal TATA promoter. After transduction, activation of the NF-κB signaling pathway in the target cells can be monitored by measuring the luciferase activity.
Description: The NF-κB eGFP Reporter Lentivirus are replication incompetent, HIV-based, VSV-G pseudotyped lentiviral particles that are ready to infect almost all types of mammalian cells, including primary and non-dividing cells. The particles contain an enhanced GFP gene driven by the NF-κB response element located upstream of the minimal TATA promoter. After transduction, activation of the NF-κB signaling pathway in the target cells can be monitored by examining eGFP expression.
Description: Transcription factor p65, also known as NFKB3 or NF-kB p65, is a protein that in humans is encoded by the RELA gene. It is mapped to 11q13.1. RELA is an essential transcription factor complex involved in all types of cellular processes, including cellular metabolism, chemotaxis, etc, and it may play a role in inflammatory conditions of the peripheral nervous system. Phosphorylation and acetylation of RELA are crucial post-translational modifications required for NFkB activation. It has also been shown to modulate immune responses, and activation of the protein is positively associated with multiple types of cancer. In addition, RELA antagonizes TNFR1-JNK proliferative signals in epidermis and plays a nonredundant role in restraining epidermal growth.
Description: NF-kappa-B 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-kappa-B 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 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively. NF-kappa-B is controlled by various mechanisms of post-translational modification and subcellular compartmentalization as well as by interactions with other cofactors or corepressors. NF-kappa-B complexes are held in the cytoplasm in an inactive state complexed with members of the NF-kappa-B inhibitor (I-kappa-B) family. In a conventional activation pathway, I-kappa-B is phosphorylated by I-kappa-B kinases (IKKs) in response to different activators, subsequently degraded thus liberating the active NF-kappa-B complex which translocates to the nucleus. NF-kappa-B heterodimeric p65-p50 and p65-c-Rel complexes are transcriptional activators. The NF-kappa-B p65-p65 complex appears to be involved in invasin-mediated activation of IL-8 expression. The inhibitory effect of I-kappa-B upon NF-kappa-B the cytoplasm is exerted primarily through the interaction with p65. p65 shows a weak DNA-binding site which could contribute directly to DNA binding in the NF-kappa-B complex. Associates with chromatin at the NF-kappa-B promoter region via association with DDX1. Essential for cytokine gene expression in T-cells. [UniProt]
Description: A polyclonal antibody for detection of NF-?B p65 from Human, Mouse, Rat. This NF-?B p65 antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthetic peptide of NF-?B p65
Description: A polyclonal antibody for detection of NF-?B p65 from Human, Mouse, Rat. This NF-?B p65 antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthetic peptide of NF-?B p65
Description: A polyclonal antibody for detection of NF-?B p65 from Human, Mouse, Rat. This NF-?B p65 antibody is for WB, ELISA. It is affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogenand is unconjugated. The antibody is produced in rabbit by using as an immunogen synthetic peptide of NF-?B p65
Overall, these results provide clear evidence that treatment of diabetic rats with diabetic retinal changes RN attenuated through hypoglycemic, antioxidant and anti-inflammatory effects. Prolonged inflammatory response can lead to the development of from some chronic diseases, such as autoimmune disorders and the development of from natural therapeutic agent needed. A murine model was used to assess the effects of anti-inflammatory from the glucoside megastigmane, icariside B 2 (ICS B ), and the assessment was carried out in vitro , and in vivo.
