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      Purified NA/LE Mouse Anti-Mouse IL-27 p28

      BD Pharmingen™ Purified NA/LE Mouse Anti-Mouse IL-27 p28

      Clone MM27.7B1 (also known as MM27-7B1)

      (RUO)
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      BD Pharmingen™
      Il27; IL-27 alpha; Il27a; IL27-A; IL-27-A; IL-27α; IL-27 p28; Il30; IL-30
      Mouse (QC Testing)
      Mouse C57BL/6 IgG2a, κ
      Mouse IL-27
      Intracellular staining (flow cytometry) (Routinely Tested), Neutralization (Reported)
      1.0 mg/ml
      AB_2738115
      No azide/low endotoxin: Aqueous buffered solution containing no preservative, 0.2µm sterile filtered. Endotoxin level is ≤0.01 EU/µg (≤0.001 ng/µg) of protein as determined by the LAL assay.
      RUO


      Preparation And Storage

      Store undiluted at 4°C. This preparation contains no preservatives, thus it should be handled under aseptic conditions. The monoclonal antibody was purified from tissue culture supernatant or ascites by affinity chromatography.
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      Product Notices

      1. Since applications vary, each investigator should titrate the reagent to obtain optimal results.
      2. An isotype control should be used at the same concentration as the antibody of interest.
      3. Please refer to www.bdbiosciences.com/us/s/resources for technical protocols.
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      563284 Rev. 1
      Antibody Details
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      MM27.7B1

      The MM27.7B1 monoclonal antibody specifically binds to the p28 subunit of mouse Interleukin-27 (IL-27 p28) that is also known as IL-27 alpha (IL-27α) or Interleukin-30 (IL-30). IL-27 p28 is a member of the IL-6/IL-12 family of cytokines. The IL-27 p28 subunit binds to the EBI3 (Epstein-Barr virus induced gene 3) protein to form heterodimeric Interleukin-27. IL-27 p28 is produced by macrophages and dendritic cells stimulated by inflammatory cytokines and ligands for Toll-like receptors (TLR). IL-27 binds to and transduces signal through surface IL-27 receptors (IL-27R) that are expressed by B cells and naïve T cells and more highly expressed by NK cells and activated T cells. The IL-27R complex is comprised of gp130 (CD130) and WSX-1 (IL-27R alpha) subunits. IL-27 signals through IL-27R that activate the Jak/STAT signaling pathway resulting in the phosphorylation of Stat1 and Stat3. It acts in a proinflammatory manner to upregulate cellular T-bet transcription factor and surface IL-12R beta2 expression contributing to higher levels of IFN-γ and granzyme B expression. IL-27 exerts anti-inflammatory responses by suppressing the differentiation and proliferation of Th2 and Th17 cells. IL-27 p28 is reportedly produced and secreted independently of EBI3. It may inhibit the actions of IL-17 and other proinflammatory cytokines like IL-6. The MM27/7B1 antibody has been reported to neutralize IL-27 activity in vitro. Routine quality testing of mAb MM27.7B1 is performed via flow cytometry of intracellularly stained IL-27 p28-transfected cells.

      563284 Rev. 1
      Format Details
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      NA/LE
      NA/LE refers to the culture and purification methods and buffer used to produce purified antibodies with no azide and low endotoxin: Aqueous buffered solution containing no preservative, 0.2µm sterile filtered. Endotoxin level is ≤0.01 EU/µg (≤0.001 ng/µg) of protein as determined by the LAL assay.NA/LE are perfectly suited to be used in culture or in vivo (for nonhuman studies) for functional assays — blocking, neutralizing, activation or depletion — where the presence of azide may damage cells or exogenous endotoxin may signal or activate cells.
      NA/LE
      563284 Rev.1
      Citations & References
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      View product citations for antibody "563284" on CiteAb

      Development References (9)

      1. Hall AO, Silver JS, Hunter CA. The immunobiology of IL-27. Adv Immunol. 2012; 115:1-44. (Biology). View Reference
      2. Hibbert L, Pflanz S, De Waal Malefyt R, Kastelein RA. IL-27 and IFN-alpha signal via Stat1 and Stat3 and induce T-Bet and IL-12Rbeta2 in naive T cells. J Interferon Cytokine Res. 2003; 23(9):513-522. (Biology). View Reference
      3. Morishima N, Owaki T, Asakawa M, Kamiya S, Mizuguchi J, Yoshimoto T. Augmentation of effector CD8+ T cell generation with enhanced granzyme B expression by IL-27. J Immunol. 2005; 175(3):1686-1693. (Biology). View Reference
      4. Pflanz S, Timans JC, Cheung J, et al. IL-27, a heterodimeric cytokine composed of EBI3 and p28 protein, induces proliferation of naive CD4(+) T cells. Immunity. 2002; 16(6):779-790. (Biology). View Reference
      5. Stumhofer JS, Hunter CA. Advances in understanding the anti-inflammatory properties of IL-27. Immunol Lett. 2008; 117(2):123-130. (Biology). View Reference
      6. Stumhofer JS, Tait ED, Quinn WJ, 3rd, et al. A role for IL-27p28 as an antagonist of gp130-mediated signaling. Nat Immunol. 2010; 11(12):1119-1126. (Biology). View Reference
      7. Uyttenhove C, Marillier RG, Tacchini-Cottier F, et al. Amine-reactive OVA multimers for auto-vaccination against cytokines and other mediators: perspectives illustrated for GCP-2 in L. major infection. J Leukoc Biol. 2011; 89(6):1001-1007. (Immunogen: Neutralization). View Reference
      8. Yoshimoto T, Okada K, Morishima N, et al. Induction of IgG2a class switching in B cells by IL-27. J Immunol. 2004; 173(4):2479-2485. (Biology). View Reference
      9. Yoshimura T, Takeda A, Hamano S, et al. Two-sided roles of IL-27: induction of Th1 differentiation on naive CD4+ T cells versus suppression of proinflammatory cytokine production including IL-23-induced IL-17 on activated CD4+ T cells partially through STAT3-dependent mechanism. J Immunol. 2006; 177(8):5377-5385. (Biology). View Reference
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      563284 Rev. 1

      Please refer to Support Documents for Quality Certificates


      Global - Refer to manufacturer's instructions for use and related User Manuals and Technical data sheets before using this products as described


      Comparisons, where applicable, are made against older BD Technology, manual methods or are general performance claims.  Comparisons are not made against non-BD technologies, unless otherwise noted.

      For Research Use Only. Not for use in diagnostic or therapeutic procedures.