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Phosphate-buffered solution, pH 7.2, containing no preservative. 0.2 μm filter sterilized. Endotoxin level is < 0.1 EU/μg of the protein (< 0.01 ng/μg of the protein) as determined by the LAL test.
Preparation:
The LEAF™ (Low Endotoxin, Azide-Free) antibody was Purified by affinity chromatography.
Concentration:
1.0 mg/ml
Storage & Handling:
The antibody solution should be stored undiluted at 4°C. This LEAF™ solution contains no preservative; handle under aseptic conditions.
Each lot of this antibody is quality control tested by ELISA assay. For ELISA and ELISPOT capture applications, a concentration range of 4-8 µg/ml is recommended. To obtain a linear standard curve, serial dilutions of IL-10 recombinant protein ranging from 2000 to 15 pg/ml are recommended for each ELISA plate. It is recommended that the reagent be titrated for optimal performance for each application. * For ELISA/ELISPOT capture, it is very critical to use 0.2 M Sodium Phosphate Buffer, pH 6.5 (11.8g Na2HPO4, 16.1g NaH2PO4; q.s. to 1.0 L) as coating buffer. Note: Carbonate buffer, pH 9.5 should not be used as coating buffer for JES5-2A5. It may cause high background and lower sensitivity.
COA:
Enter Lot#:
Application Notes:
ELISA or ELISPOT Detection1,9,11: The biotinylated JES5-16E3 antibody is useful as a detection antibody for a sandwich ELISA or ELISPOT assay, when used in conjunction with purified JES5-2A5 antibody (Cat. No. 504902/504904) as the capture antibody.
Neutralization: The JES5-16E3 antibody can neutralize the bioactivity of natural or recombinant IL-10.
Application References:
1. Simkin G, et al. 2000. J. Immunol. 164:2457. 2. Kitagaki K, et al. 2002. Clin. Diagn. Lab Immunol. 9:1260. 3. Khanna A, et al. 2000. J. Immunol. 164:1346. 4. Sander B, et al. 1993. J. Immunol. Methods 166:201. 5. Litton M, et al. 1994. J. Immunol. Methods 175:47. 6. Andersson U, et al. 1999. Detection and qunatification of gene expression. New York:Springer-Verlag. 7. Finkelman F, et al. 2003. Curr. Prot. Immunol. John Wiley & Sons New York. Unit 6.28. 8. Wang W, et al. 2004. FASEB J. 18:1043. 9. Brummel R and Lenert P. 2005. J. Immunol. 174:2429. 10. Lawson BR, et al. 2007. J. Immunol. 178:5366. 11. Xu G, et al. 2007. J. Immunol. 179:5358. PubMed 12. Brummel R, et al. 2005. J. Immunol.174:2429. PubMed 13. Kang YJ, et al. 2007. Stem Cells 25:1814. PubMed
Description:
IL-10 was originally described as Cytokine Synthesis Inhibitory Factor (CSIF) by virtue of its ability to inhibit cytokine production by Th1 clones. IL-10 shares over 80% sequence homology with the Epstein-Barr virus protein BCRFI. IL-10 inhibits IFN-γ, TNF-β, and IL-2 production by Th1 clones; inhibits macrophage-mediated IL-1, IL-6, and TNF-α synthesis; suppresses the delayed type hypersensitivity response; stimulates Th2 cell response (which results in elevated antibody production); and promotes mast cell proliferation in combination with IL-4.
Other Names:
Interleukin-10, Cytokine synthesis inhibitory factor (CSIF), B cell derived T cell growth factor (B-TCGF), T cell growth inhibitory factor (TGIF)
Structure:
Acid-labile cytokine, dimer, 17-21 kD (Mammalian)
Regulation:
Downregulated by IL-4, IL-10
Cellular Sources:
Activated CD8+ T cells, Th0, Th2 subset of CD4+ T cells, Ly-1+ B cells, monocytes, macrophages, keratinocytes
Cellular Targets:
T cells, B cells, mast cells, macrophages
Receptors:
IL-10R (CDw210)
Antigen References:
1. Fitzgerald K, et al. Eds. 2001. The Cytokine FactsBook. Academic Press San Diego. 2. de Waal-Malefy R, et al. 1992. Curr. Opin. Immunol. 4:314. 3. Howard M, et al. 1992. Immunol. Today 13:198. 4. Quesniaux V. 1992. Res. Immunol. 143:385. 5. Norton SK, et al. 2008. J. Immunol. 180:2848.
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