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Safety Data Sheet (SDS) Alexa Fluor 647 Anti-mouse IL-27 P28 Antibody     Product Data Sheet (PDF)    
Alexa Fluor® 647 Anti-mouse IL-27 P28 Antibody
3184520 100 µg $290.00       
Clone: MM27-7B1
Isotype: Mouse IgG2a
Reactivity: Mouse
Immunogen: Mouse IL-27-OVA
Formulation: Phosphate-buffered solution, pH 7.2, containing 0.09% sodium azide.
Preparation: The antibody was purified by affinity chromatography, and conjugated with Alexa Fluor® 647 under optimal conditions.
Concentration: 0.5 mg/ml
Storage & Handling: The antibody solution should be stored undiluted between 2°C and 8°C, and protected from prolonged exposure to light. Do not freeze.
Application:

ICFC - Quality tested

Application Notes:

Clone MM27-7B1 specifically recognizes the p28 subunit of IL-27.1

ELISA Capture: To measure mouse IL-27 p28, this antibody can be used as a capture antibody in sandwich ELISA format and paired with the biotinylated B02P6E6 antibody as the detection antibody. Recombinant Mouse IL-27 (ELISA Std.) can be used as the protein standard.
Flow Cytometry: The fluorochrome-labeled MM27-7B1 antibody is useful for intracellular and membrane-bound immunofluorescent staining and flow cytometric analysis to identify granulysin-producing cells within mixed cell populations.
Note:
 For testing mouse IL-27 p28 heterodimer, plasma or cell culture supernatant, LEGEND MAX™ Mouse IL-27 Heterodimer ELISA Kit with Pre-coated Plates are specially developed and recommended.

Recommended Usage:

Each lot of this antibody is quality control tested by intracellular immunofluorescent staining with flow cytometric analysis. For flow cytometric staining, the suggested use of this reagent is ≤ 0.06 µg per million cells in 100 µl volume.  It is recommended that the reagent be titrated for optimal performance for each application.

* Alexa Fluor® 647 has a maximum emission of 668 nm when it is excited at 633 nm / 635 nm.

Application References:

1. Uyttenhove C, et al. 2011. J. Leuko. Biol. 89:1001.

Thioglycolate-elicited Balb/c peritoneal macrophages primed

Thioglycolate-elicited Balb/c peritoneal macrophages primed with IFN-γ for 2 hours, followed by overnight LPS-stimulation, then intracellularly stained with CD107b (Mac-3) PE and MM27-7B1 Alexa Fluor® 647 (top) or mouse IgG2a Alexa Fluor® 647 isotype control (bottom).





Description:

IL-27 is a heterodimeric cytokine consisting of EBV-induced gene-3 (EBI3, an IL-12 p40-related protein) and p28 (a newly discovered IL-12 P35-related protein). It is a member of the IL-6/IL-12 cytokine family and mainly produced by antigen-presenting cells, including macrophages and dendritic cells. IL-27 acts on T cells and NK cells. It has been reported that IL-27 drives rapid clonal expansion of naïve CD4+ T cells, and promotes Th1 polarization and IFN-γ production in synergy with IL-12. The IL-27-induced Th1 differentiation was mediated by rapid and marked upregulation of ICAM-1/LFA-1 interaction in a STAT1-dependent manner. IL-27 exhibits anti-inflammatory function by enhancing Th1 cell differentiation, a potent antitumor activity, through CD8+ T cell and NK cell activation. It also plays a potential therapeutic role in autoimmune disease by inhibiting Th-17 development. IL-27 mediates its biological effects through its receptor, WSX-1/T cell cytokine receptor (TCCR), which is homologous to the IL-12Rβ2 subunit. Protein gp130 serves as a functional signal-transducing molecule for IL-27.

Other Names: Interleukin-27 p28, IL-27-A, IL-27 subunit alpha
Structure: A heterodimeric cytokine consisting of EBV-induced gene-3 (EBI3, an IL-12 p40-related protein) and p28 (a newly discovered IL-12 p35-related protein).
Distribution: Produced by antigen-presenting cells, including macrophages and dendritic cells.
Function: Drives rapid clonal expansion of naïve CD4+ T cells, promotes Th1 polarization and IFN-γ production; plays a role in the anti-inflammatory and antitumor reponses, and has potential in autoimmune disease therapy.
Ligand Receptor: IL-27R (TCCR/WSX-1).
Interaction: T cells and NK cells.
Antigen References:

1. Salcedo R, et al. 2004. J. Immunol. 173:7170.
2. Owaki T, et al. 2005. J. Immunol. 175:2191.
3. Pflanz S, et al. 2002. Immunity 16:779.
4. Diveu C, et al. 2009. J. Immunol. 182:5748.
5. Morishima N, et al. 2005. J. Immunol. 175:1686.
6. Liu J, et al. 2007. J. Exp. Med. 204:141.


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