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Recombinant Human IL-10 (mammalian expressed, carrier-free)
Recombinant Human IL-10 (mammalian expressed, carrier-free)
573202
10 µg
$195.00
573204
25 µg
$395.00
573206
100 µg
$1,200.00
Product Details
Source:
Human IL-10, amino acids Ser19-Asn178 (Accession # NM_000572), was expressed in 293E cells, using human IL-2 signal peptide.
Molecular Mass:
The 160 amino acid recombinant protein has a predicted molecular mass of 18,647 Da. The DTT-reduced protein migrates at approximately 18 kD and the non-reduced protein migrates slightly with faster mobility by SDS-PAGE. The N-terminal amino acid is Serine.
Purity:
>95%, as determined by Coomassie stained SDS-PAGE.
Formulation:
0.22 µm filtered protein solution is in PBS
Endotoxin Level:
Less than 0.01 ng per µg cytokine as determined by the LAL method.
Preparation:
10-100 µg sizes are bottled at 200 µg/mL.
Storage & Handling:
Unopened vial can be stored at 4°C for three months, at -20°C for six months, or at -70°C for one year. For maximum results, quick spin vial prior to opening. Stock solutions should be prepared at no less than 10 µg/mL in buffer containing carrier protein such as 1% BSA or HSA or 10% FBS. After dilution, the cytokine can be stored at 4°C for one month or at -20°C to -70°C for up to 3 months. Avoid repeated freeze/thaw cycles.
Activity:
ED50 = 0.1 - 0.3 ng/ml corresponding to a specific activity of 3.3 - 10 x 106 units/mg, as determined by the dose dependent inhibition of IFNg production by PHA activated PBMC.
Human IL-10 inhibits the production of IFNγ in PMA activated PBMC.
Description:
IL-10 was first described as a cytokine that is produced by T helper 2 (Th2) cell clones. It inhibits interferon (IFN)-g synthesis in Th1 cell, and therefore it was initially called ‘cytokine synthesis inhibiting factor’ (CSIF). Macrophages are the main source of IL-10 and its secretion can be stimulated by endotoxin (via Toll-like receptor 4, NF-kB dependent), tumor necrosis factor TNF-a (via TNF receptor p55, NF-kB-dependent), catecholamines, and IL-1. IL-10 controls inflammatory processes by suppressing the expression of proinflammatory cytokines, chemokines, adhesion molecules, as well as antigen-presenting and costimulatory molecules in monocytes/macrophages, neutrophils, and T cells. IL-10 inhibits the production of proinflammatory mediators by monocytes and macrophages such as endotoxin- and IFNg-induced release of IL-1a, IL-6, IL-8, G-CSF, GM-CSF, and TNF-a. In addition, it enhances the production of anti-inflammatory mediators such as IL-1RA and soluble TNFa receptors. IL-10 inhibits the capacity of monocytes and macrophages to present antigen to T cells. This is realized by down-regulation of constitutive and IFNg-induced cell surface levels of MHC class II, of costimulatory molecules such as CD86 and of some adhesion molecules such as CD58. IL-10 belongs to a family of nine members: IL-10, IL-19, IL-20, IL-22, IL-24, IL-26, and the more distantly related IL-28A, IL-28B, and IL-29. This family of cytokines emerged before the adaptive immune response.
Other Names:
Cytokine synthesis inhibitory factor (CSIF)
Distribution:
IL-10 is produce by Th2 cells, macrophages, DCs, B cells, CD8+ T cells, regulatory T cells (Tregs), Th1 cells and Th17 cells. In addition, IL-10 is expressed by monocytes, B cells, eosinophils, and mast cells.
Function:
IL-10 is an immunoregulatory cytokine. Its main function is the limitation and termination of inflammatory responses and the regulation of differentiation and proliferation of several immune cells such as T cells, B cells, natural killer cells, antigen-presenting cells, mast cells, and granulocytes.
Ligand Receptor:
IL-10 binds to their receptors IL-10R1 and IL-10R2, and initiates a STAT3-dependent signaling cascade.
Interaction:
IL-10R is expressed in monocytes, NK, B and T cells. In addition, Langerhans cells, dermal dendritic cells, eosinophils, mast cells, and endothelial cells can respond to IL-10.
Antigen References:
1. Fiorentino DF, et al. 1989. J. Exp. Med. 170:2081. 2. Ho AS, et al.P. Natl. Acad. Sci. 1993. 90:11267. 3. Hart PH, et al. 1996. J. Immunol. 157:3672. 4. Asadullah K, et al. 2003. Pharmacol. Rev. 55:241. 5. Mosser DM and Zhang X. 2008. Immunol. Rev. 226:205. 6. Maynard CL and Weaver CT. 2008. Immunol. Rev. 226:219. 7. Ouyang W, et al. 2010. Annu. Rev. Immunol. 30:559.
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