Recombinant Human IL-10 (mammalian expressed, carrier-free)

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Other Names
Cytokine synthesis inhibitory factor (CSIF)
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Human_IL-10_020711
Human IL-10 inhibits the production of IFNγ in PMA activated PBMC.
  • Human_IL-10_020711
    Human IL-10 inhibits the production of IFNγ in PMA activated PBMC.
Cat # Size Price Quantity Avail. Save
573202 10 µg 156€
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573204 25 µg 316€
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573206 100 µg 960€
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573208 500 µg 2.396€
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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.

Product Details
Technical Data Sheet (pdf)

Product Details

Reactivity
Human
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.
Concentration
10 and 25 µg sizes are bottled at 200 µg/mL. 100 µg size and larger sizes are lot-specific and bottled at the concentration indicated on the vial (please contact technical support for concentration, or use our Lookup tool if you have a lot number.)
Please note, new lots of the 100 µg size will be lot-specific and may differ from previous lots that had a fixed concentration.
Storage & Handling
Unopened vial can be stored between 2°C and 8°C for one month, at -20°C for six months, or at -70°C for one year. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored from -20°C to -70°C. Stock solutions can also be prepared at 50-100 µg/mL in sterile buffer (PBS, HPBS, DPBS, or EBSS) containing carrier protein such as 0.2-1% BSA or HSA and stored in working aliquots at -20°C to -70°C. 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.
Application

Bioassay

Application Notes

BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue-ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are validated in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at tech@biolegend.com.

Antigen Details

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.
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.
Ligand/Receptor
IL-10 binds to their receptors IL-10R1 and IL-10R2, and initiates a STAT3-dependent signaling cascade.
Biology Area
Cell Biology, Immunology
Molecular Family
Cytokines/Chemokines
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.

Gene ID
3586 View all products for this Gene ID
UniProt
View information about IL-10 on UniProt.org

Related FAQs

Does specific activity of a recombinant protein vary between lots?

Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.

Have your recombinants been tested for stability?

Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.

How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?
Use formula Specific activity (Units/mg) = 10e6/ ED50 (ng/mL)
How does the activity of your recombinant proteins compare to competitors?

We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!

What is the specific activity or ED50 of my recombinant protein?

The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.

Go To Top Version: 3    Revision Date: 08-19-2014

For research use only. Not for diagnostic use. Not for resale. BioLegend will not be held responsible for patent infringement or other violations that may occur with the use of our products.

 

*These products may be covered by one or more Limited Use Label Licenses (see the BioLegend Catalog or our website, www.biolegend.com/ordering#license). BioLegend products may not be transferred to third parties, resold, modified for resale, or used to manufacture commercial products, reverse engineer functionally similar materials, or to provide a service to third parties without written approval of BioLegend. By use of these products you accept the terms and conditions of all applicable Limited Use Label Licenses. Unless otherwise indicated, these products are for research use only and are not intended for human or animal diagnostic, therapeutic or commercial use.

 

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Toll-Free Phone: 1-877-Bio-Legend (246-5343) Phone: (858) 768-5800 Fax: (877) 455-9587

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