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- Table of Contents
160 Citations 11 Q&As
266 Citations 6 Q&As
159 Citations 10 Q&As
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1 Citations 15 Q&As
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Facts about Interleukin-10.
Inhibits the synthesis of a number of cytokines, Such as IFN-gamma, IL-2, IL-3, TNF and GM-CSF produced by activated macrophages and by helper T-cells.
.Human | |
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Gene Name: | IL10 |
Uniprot: | P22301 |
Entrez: | 3586 |
Belongs to: |
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IL-10 family |
CSIF; CSIFMGC126450; Cytokine synthesis inhibitory factor; GVHDS; IL10; IL-10; IL10A; IL-10MGC126451; interleukin 10; interleukin-10; TGIF
Mass (kDA):
20.517 kDA
Human | |
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Location: | 1q32.1 |
Sequence: | 1; NC_000001.11 (206767602..206772494, complement) |
Produced by a variety of cell lines, including T-cells, macrophages, mast cells and other cell types.
Secreted.
If you're in search of an excellent antibody for the IL10 marker look at Boster Bio. Boster Bio tests all of their antibodies with negative and positive samples to ensure that they are highly specific and have high affinity. Boster Bio also rewards the first reviewers by awarding product credits. This is a way of recognizing the most innovative scientists around the world. Continue reading for more details. The most effective use for IL10 is in research into the immunoregulatory process.
Il-10 is a pleiotropic cytokine that is renowned for its powerful anti-inflammatory and immunosuppressive properties. It reduces the production of proinflammatory mediators by monocytes and macrophages, and it also restricts the growth of T cells. It plays an important role in maintaining good health. This article will discuss the mechanisms behind its action and how it may be used to fight infections.
IL-10 binds to its receptor (IL-10R) with high affinity. Its binding is a species-specific phenomenon and mouse IL-10 blocked human IL-10 from binding to mice, whereas human IL-10 did not. The dimer of IL-10, which is not covalent, is unstable under acidic conditions and at low protein concentrations. These conditions include hemoatomas caused by fractures, as well as inflammatory skin.
The anti-inflammatory properties of IL-10 are believed to result from its interaction with the IL-10 receptor, that is expressed most frequently on monocytes. It also activates JAK1-TYK2-STAT3 pathway which regulates genes that limit the inflammatory response. Interestingly, IL-10 also inhibits the production of pro-inflammatory cytokines, but this effect is not entirely dependent on the presence of IL-10.
Il-10 can be used to treat diabetes. However, if it is not controlled properly, it could increase the risk of acquiring clinical melioidosis. Patients with DM may benefit from IL-10 which can help regulate the production of IL-6, and TNF-a. If diabetes is not managed properly, people with diabetes are at greatest risk of developing clinical melioidosis.
It is not clear what role it plays in regulation of the immune response to infection. However, it may inhibit the production of pro-inflammatory cytokines and reduce the number of B. pseudomallei-infected monocytes. It may also inhibit the activity of NK and T cells and increase susceptibility to other bacteria-related infections. It is important to study the role of the IL-10 gene in COVID-19 and how it may be affected by it.
The IL-10 cytokine is an immunoregulatory anti-inflammatory cytokine, which plays a important role in GVHD. This cytokine can also have other effects on the immune system. The IL-10 cytokine can also alter or delay the kinetics for T cell reconstitution after xenogeneic GVHD has been inducible. It also reduces the production of proinflammatory cytokines in antigen-presenting cells. Exogenous IL-10 treatment for xenogeneic GVHD significantly increased survival rates in mice. Combining IL-2 and IL-10 treatment decreased the incidence of GVHD in mice by 20%.
The serum samples of Hu/PBL NSG mice were used to determine IL-10 levels. In the same study, serum from IL-10/ mice was administered intravenously with increasing amounts of STm and Nm. Both groups underwent LPS-induced TNF synthesis. Additionally the serum samples were taken at the times indicated. The samples of serum were analysed using ELISA to determine the levels of IL-10 in serum.
Interleukin 10, also known as IL10, is a pro-inflammatory cytokine which promotes phosphorylation STAT3 transcription factor. It is a member of STAT family. This protein binds to DNA and polymerizes to activated transcription activator. STAT3 triggers transcription and stimulates the production of inflammatory genes and cytokine. This process also involves IL10 and other cytokines.
The AhR-associated Src activity activates STAT3 which in turn increases IL-10 expression. Moreover, AhR-expressing macrophages protect mice from LPS-induced peritonitis, which suggests that this pathway is vital. Additionally, AhR may also be an effective therapeutic target. It is a proinflammatory cytokine, which promotes the production of IL-10.
The cell culture method of chromatin immunoprecipitation was used to incubate rBMECs with untreated or septic serum. The septic serum enhanced apoptosis, and p-JAK2 mediated STAT3 activation in rBMECs.
Cell Signaling Technology and Enzo Life provided the anti-AhR antibodies used in this study. The primary antibody was a monoclonal rabbit anti-mouse antibody (HRP labeled), and the secondary antibodies were goat IgG (1,20,000).
Boster Bio IL10 promotes tyrosine phosphorylation of transcription factor STAT3. The NF-kB pathway regulates activation of STAT3 via IL-10. AhR is also crucial in the immune system and regulates STAT3 transcription. In LPS-induced AhR macrophages, IL-10 can be involved in activation of the STAT3 pathway.
LPS treatment of RAW/NC cells for 2 hours increased the production of cytokines. The levels of nuclear extract protein were then compared with DNA-binding site probes or AhR-containing vectors. The cytokine levels were determined in both cell lines using EMSA. In the third and final test, Boster Bio IL10 promoted the phosphorylation process of transcription factor STAT3 in THP-1 cells.
It also increased the expression of inflammatory cytokines within macrophages and airway cells in the human. LPS also increased NFKB-dependent levels of STAT3 phosphorylation, and increased the production of inflammatory cytokines inside THP-1 cells. These results suggest that Boster Bio's IL10 could be therapeutically useful in inflammatory disease treatment.
The activation of the JAK/STAT signaling pathway has been connected to inflammatory mediators cytokines, as well as the immune response in sepsis. In addition, the expression of miR-30a and miR-155 was also increased in blood cells that are sepsis-infected. Anti-miR-181b may be the best therapy for sepsis.
IL-10 is a factor in metabolic disorders associated with obesity, such as insulin resistance. In childhood the cytokine was found to be expressed in less than one percent of the adipose tissue. It has been linked with obesity, which is associated with low prognosis. This cytokine has also been linked to the JAK-STAT3 pathway.
Although IL10 increases phosphorylation in the brain, it has yet to be shown that it enhances the activity of this protein at the blood brain border. These results suggest that IL10 is involved in the progression and development of sepsis-associated encephalopathy. It also enhances the transcription factor's phosphorylation STAT3.
IL-10 is an anti-inflammatory cytokine with multiple functions in the field of immunoregulation. IL-10 inhibits the production of pro-inflammatory cytokines like as IL-6 and IFN-g, blocks the secretion of IL-1b and TNF-a and reduces expression of MHC II and CD80 on the surface of macrophages as well as dendritic cells.
The IL-10 M2Mu was evaluated for its ability to block the activity of luciferase. The IL-10 M2Mu dose inhibited the activity of luciferase by a ratio of 1.5. The greatest level of suppression was attained at 50 ng/mL. This suggests that the dimerization of IL-10 protein may represent its maximum activity.
In addition, the IL-10-mRNA that was cloned transformed into the Bifidobacterium bifidum BLN4 phage. Bioassay testing, Western Blot, and ELISA confirmed the successfulness of the transformation. The IL-10 marker blocks the production of inflammatory cytokines in various models of inflammation.
Boster Bio's IL10 made mRNA with the His-tagged pCEPV19 expression vector. Under reducing conditions, Nm and STm were stained using Coomassie Blue. Recombinant IL-10 can be detected by Nm and STm peptides by Western Blot and ELISA. A peptide linker between the Nm and STm proteins is illustrated in red.
IL-10 inhibits inflammation by limiting the production of pro-inflammatory cytokines. The inability to regulate IL-10 production can cause neuronal stress and reactive microgliosis. The IL-10 MRNA can be utilized to identify drug targets by inhibiting IL-10 production. It is currently the only human mRNA to inhibit the production of pro-inflammatory cytokines.
The IL-10 molecular RNA (mRNA) is a polypeptide that is not co which binds to IL-10R. Its receptor-binding domain is required to bind to IL-10R. Janus kinase STAT signaling is activated to aid in the binding process. Its binding to IL-10R is a multi-step process involving several steps.
Multiple MS (MS) is an inflammatory disease that results in demyelination in the central nervous system (CNS). While the nature of MS remains a mystery but it is believed that the increased production and use of cytokines play a major role in the pathogenesis. Therefore, it is essential to understand IL-10's biochemical mechanisms and determine if it can be beneficial.
The IL10M2Mu protein is a stable version of IL-10. It has four point mutations in the p65 and STm receptors. The protein can be identified using the ELISA technique or 1/2-dilution. Purified IL-10Mu can also be detected by luciferase activity on a reporter mice model expressing Nm and STm.
Human IL-10 was cloned into the Bifidobacterium spp. shuttle vector pBES2. The human IL-10 gene was expressed in these bacterial cells via the gap promoter. This marker may be a useful therapeutic agent for inflammatory cytokines, including interferon-alpha.
PMID: 1847510 by Vieira P., et al. Isolation and expression of human cytokine synthesis inhibitory factor cDNA clones: homology to Epstein-Barr virus open reading frame BCRFI.
PMID: 9405662 by Gesser B., et al. Identification of functional domains on human interleukin 10.
*Showing only the more recent 20. More publications can be found for each product on its corresponding product page