Human IL-10 ELISA Kit

Detection Principle:

This kit uses double antibody sandwich enzyme-linked immunosorbent assay technology. The specific anti human il-10antibody was pre coated on a high affinity microplate. The standard, sample to be tested and biotinylated detection antibody are added into the wells of the enzyme plate. After incubation, the il-10present in the sample combines with the solid-phase antibody and detection antibody to form an immune complex. After washing to remove unbound material, horseradish peroxidase labeled streptavidin (streptavidin HRP) was added. After washing, the chromogenic substrate was added to avoid light for color development. Stop the reaction by adding stop solution, and determine the absorbance value at 450 nmwavelength (reference correction wavelength 540nmor 570nm).

Test Type: Double antibody sandwich method

Form: pre coated 96orifice plate

Test Sample Type: cell supernatant, Serum, plasma

Sample Loading: 100ul

Kit Components:

Precoated 96well plates, standards, il-10detection antibody, dilution buffer, chromogenic solution (a, b)One copy of washing solution, termination solution, sa-hrp, plate sealing membrane and instructions.

Sensitivity: 3.9pg/ml

Detection Range: 31.2 - 2000 pg/ml

Recovery Range: 88-110%

Saving Method: 2-8℃

Standard Curve

Background:

Interleukin 10 (IL - 10), also known as cell growth factor synthesis inhibitory factor (CSIF), IL - 10 & alpha; Spiral members of the family, the family also includes IL - 19, 20, IL - IL - 24 and 22, IL - IL - 26 / ak155. IL - 10 can be made of a variety of activation of hematopoietic cells, hepatic stellate cells, cutin formation and placenta nourish cells. The human IL - 10 cells in mice activity, and IL - 10 cannot act on human cells in mice. Mature human IL-10 shares 86% amino acid sequence identity with equine IL-10 and between 72 and 80% identity with bovine, canine, cat, guinea pig, mouse, sheep, pig, and rat IL-10. It contains two disulfide bond within the chain, in the form of non covalent bonding homologous dimers expression, molecular weight 36 kda.

IL-10 is mediated by the type II cytokine IL-10 receptor subunit α And β Heterologous dimer complex mediates its biological activity. IL - 10 receptor & alpha; Sub is a 110 kda transmembrane glycoprotein, is mainly expressed in lymphocytes, NK cells, macrophages and monocytes, astrocytes, intestinal epithelial cells, trophoblastic cells and the activation of hepatic stellate cells, and 75 kda transmembrane receptor & beta; Is widely expressed. IL - 10 dimers in combination with two IL - 10 Rα Chain, two IL - 10 Rβ The addition of chains. IL-10 Rβ Not directly combined with IL - 10, but the need for signal transduction. IL-10 Rβ It also interacted with IL-20 Rα IL-22 Rα 1 and IL - 28 Rα IL - 22, IL - 26, 28 and IL - IL - 29 receptor complexes.

IL - 10 in immune regulation including inhibition and stimulation. It by inhibiting the amplification and activation of Th1 cells and Th17 cells, promote the M2 macrophages play a role of anti-inflammatory. The regulation of IL-10 expression by immune regulatory T cells (Treg) and regulatory B cells is important for Treg proliferation. In the tumor environment, however, IL - 10 Treg and pulp source sex inhibition of cell proliferation. IL-10 induces the accumulation and activation of CD8 T cells in tumors. IL-10 plays a protective role by limiting tissue damage in arthritis and promoting muscle regeneration after injury, but it may contribute to the persistence of viral infection. IL-10 levels are elevated in Sjogren's syndrome (saliva), primary central nervous system lymphoma (cerebrospinal fluid), and ovarian cancer (serum and ascites). Its level in patients with heart disease recurrence or child refined early lower serum and semen in male infertility patients.

IL-1α And IL-1β They are structurally related peptides that share approximately 25% identity at the amino acid level. Both are synthetic precursor for 31 kDa first, and then cracking for mature about 17.5 kDa protein. The effect of Caspase-1/ICE on IL-1β The precursor to the cutting is the key step in the inflammatory response. Although IL - 1 & alpha; And IL - 1 & beta; Does not contain a typical hydrophobic signal peptide, but there is evidence that they can through the classical secreted to the outside of the cell. Untreated IL-1α Part can display on the cell membrane, and may retain biological activity. And IL - 1 & beta; Different precursors, IL-1β Precursor and mature IL-1β In contrast, it has little or no biological activity. IL-1β Precursor and mature IL-1β Are shipped to the extracellular.

IL-1α And IL - 1 & beta; It exerts its effects by binding to IL-1RA through the immunoglobulin superfamily receptor. 80 kda type I transmembrane receptors (IL - 1 ri) expressed in various cells, including T cells, fibroblasts, horniness cells, endothelial cells, synovial lining cells, cartilage cells and liver cells. 68 kda type II transmembrane receptors (IL - 1 rii) in B cells, neutrophils and bone marrow cells. The extracellular regions of IL-1RI and IL-1RII share 28% identity. But other regions are significantly different: the intracellular domain of the type II receptor is only 29 amino acids, compared with 213 amino acids for the type I receptor. IL-1RII does not appear to respond to IL-1 signaling and functions as a decoy receptor thereby impairing the effects of IL-1. IL - 1 receptor ligands protein (IL - 1 racp) interact with IL - 1 ri ri is IL - 1 essential for signal transduction. Secretion of IL - 1 ra is molecule, is the competitive inhibitor of IL - 1. Soluble IL-1RI and IL-1RII are present in human plasma, synovial fluid, and conditioned media of several cell lines. In addition, vaccinia virus code is similar to the soluble binding protein of rii IL IL - 1-1.