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EBI3 antibody

The Mouse Monoclonal anti-EBI3 antibody has been validated for ELISA, IP and Neut. It is suitable to detect EBI3 in samples from Mouse. There are 179+ publications available.
Rockland
Catalog No. ABIN1043813
Supplier Product No.: 210-301-b66

Quick Overview for EBI3 antibody (ABIN1043813)

Target

See all EBI3 (IL-27b) Antibodies
EBI3 (IL-27b) (Interleukin-27 subunit beta (IL-27b))

Reactivity

  • 64
  • 32
  • 5
  • 1
  • 1
Mouse

Host

  • 61
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  • 8
  • 1
Mouse

Clonality

  • 61
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Monoclonal

Conjugate

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  • 1
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This EBI3 antibody is un-conjugated

Application

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ELISA, Immunoprecipitation (IP), Neutralization (Neut)

Clone

V1-4C4-22
  • Supplier Product No.

    210-301-b66

    Supplier

    Rockland

    Specificity

    Anti-Mouse EBI-3 (MOUSE) Monoclonal Antibody was purified from mouse ascites by Protein A chromatography followed by extensive dialysis against the buffer stated above. This antibody is specific for mouse EBI3 protein. A BLAST analysis was used to suggest cross-reactivity with EBI3 from mouse sources based on 100% homology with the immunizing sequence. Cross-reactivity with EBI-3 from other sources has not been determined.

    Characteristics

    The cytokine Interleukin 27 (IL-27) is produced in response to inflammation. It is made by activated antigen presenting cells including monocytes, endothelial cells, and dendritic cells. IL-27 consists of a heterodimeric combination of Epstein-Barr virus-induced molecule 3 (EBI3, or IL-27B) non-covalently linked with IL-27 p28 (or IL-27A). It is a regulator of T helper cell development and suppressor of T-cell proliferation. IL-27 has both pro- and anti-inflammatory properties. It can stimulate cytotoxic T cell activity and induce isotype switching in B-cells. It has diverse effects on innate immune cells. It induces monocytes and mast cells to secrete pro-inflammatory cytokines. When infection is present, IL-27 induces naive CD4+ T cells to proliferate and develop Th1 cell responses. As an anti-inflammatory regulator, IL-27 can inhibit Th1 or Th2 responses and restrict the strength and duration of adaptive immune responses. The IL-27 p28 subunit, a 28 kDa glycoprotein belonging to the type I cytokine family, is homologous to IL-12 p35, IL-23 p19, and IL-6. The EBI3 (Epstein-Barr virus-induced molecule 3, or IL-27B) subunit is a 34 kDa glycoprotein containing two fibronectin type III domains, and belongs to the type I cytokine receptor family. It can exist as a homodimer and can also heterodimerize with IL-27 p28 or IL-12 p35 subunit. It is homologous to the p40 subunit of IL-12 and IL-23 and to the extracellular domain of IL-6 R.

    Sterility

    Sterile filtered

    Immunogen

    Anti-EBI-3 (MOUSE) Monoclonal Antibody was produced in mouse by repeated immunizations with mature full length recombinant mouse EBI-3 produced in E.coli followed by hybridoma development.
    Immunogen Type: RecombinantProtein

    Isotype

    IgG2b
  • Application Notes

    Anti-Mouse EBI-3 antibody has been tested for use in ELISA, IP, and Neutralization. Specific conditions for reactivity should be optimized by the end user.

    Comment

    Gene Name: EBI3

    Restrictions

    For Research Use only
  • Format

    Liquid

    Concentration

    1.0 mg/mL

    Buffer

    0.02 M Potassium Phosphate, 0.15 M Sodium Chloride, pH 7.2

    Preservative

    Sodium azide

    Precaution of Use

    This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.

    Storage

    4 °C/-20 °C

    Storage Comment

    Store vial at 4 °C prior to restoration. For extended storage aliquot contents and freeze at -20 °C or below. Avoid cycles of freezing and thawing. Centrifuge product if not completely clear after standing at room temperature. This product is stable for several weeks at 4 °C as an undiluted liquid. Dilute only prior to immediate use. Expiration date is one (1) year from date of opening.

    Expiry Date

    12 months
  • Liu, Su, Zhang, Ge, Li, Wang, Gravel, Roulston, Song, Xu, Liang, Shore, Wang, Liang: "Improvement of Pharmacokinetic Profile of TRAIL via Trimer-Tag Enhances its Antitumor Activity in vivo." in: Scientific reports, Vol. 7, Issue 1, pp. 8953, (2019) (PubMed).

    Surolia, Li, Wang, Li, Liu, Zhou, Luckhardt, Bae, Liu, Rangarajan, de Andrade, Thannickal, Antony: "3D pulmospheres serve as a personalized and predictive multicellular model for assessment of antifibrotic drugs." in: JCI insight, Vol. 2, Issue 2, pp. e91377, (2019) (PubMed).

    Haapalainen, Karjalainen, Daddali, Ohlmeier, Anttonen, Määttä, Salminen, Mahlman, Bergmann, Mäkikallio, Ojaniemi, Hallman, Rämet: "Expression of CPPED1 in human trophoblasts is associated with timing of term birth." in: Journal of cellular and molecular medicine, Vol. 22, Issue 2, pp. 968-981, (2019) (PubMed).

    Turchinovich, Surowy, Tonevitsky, Burwinkel: "Interference in transcription of overexpressed genes by promoter-proximal downstream sequences." in: Scientific reports, Vol. 6, pp. 30735, (2018) (PubMed).

    Scholefield, Henriques, Savulescu, Fontan, Boucharlat, Laplantine, Smahi, Israël, Agou, Mhlanga: "Super-resolution microscopy reveals a preformed NEMO lattice structure that is collapsed in incontinentia pigmenti." in: Nature communications, Vol. 7, pp. 12629, (2018) (PubMed).

    Huang, Ku, Chen, Chang, Chu: "Dual mechanisms regulate the nucleocytoplasmic localization of human DDX6." in: Scientific reports, Vol. 7, pp. 42853, (2018) (PubMed).

    Jarrett, Lee, Yeh, Hsu, Gupta, Zhang, Rodriguez, Lee, Gillard, Bissig, Pownall, Martin, Bao, Lagor: "Somatic genome editing with CRISPR/Cas9 generates and corrects a metabolic disease." in: Scientific reports, Vol. 7, pp. 44624, (2018) (PubMed).

    Joachim, Razi, Judith, Wirth, Calamita, Encheva, Dynlacht, Snijders, OReilly, Jefferies, Tooze: "Centriolar Satellites Control GABARAP Ubiquitination and GABARAP-Mediated Autophagy." in: Current biology : CB, Vol. 27, Issue 14, pp. 2123-2136.e7, (2018) (PubMed).

    He, Liu, Luo, Liu, Liu, Liu, Wang, Zhang, Zhang, Liu, Cao, Zhou: "Repair of osteochondral defects with in vitro engineered cartilage based on autologous bone marrow stromal cells in a swine model." in: Scientific reports, Vol. 7, pp. 40489, (2018) (PubMed).

    Roselló-Díez, Stephen, Joyner: "Altered paracrine signaling from the injured knee joint impairs postnatal long bone growth." in: eLife, Vol. 6, (2018) (PubMed).

    Yamauchi, Takeuchi, Chihara, Honjoh, Kato, Yoshiki, Hotta, Sada: "STAT1 is essential for the inhibition of hepatitis C virus replication by interferon-λ but not by interferon-α." in: Scientific reports, Vol. 6, pp. 38336, (2018) (PubMed).

    OBrien, Guo, Bahrami-Samani, Park, Hasso, Lee, Fang, Kim, Guo, Hong, Peterson, Lozanoff, Raviram, Ren, Fogelgren, Smith, Valouev, McMahon: "Transcriptional regulatory control of mammalian nephron progenitors revealed by multi-factor cistromic analysis and genetic studies." in: PLoS genetics, Vol. 14, Issue 1, pp. e1007181, (2018) (PubMed).

    Girnius, Davis: "JNK Promotes Epithelial Cell Anoikis by Transcriptional and Post-translational Regulation of BH3-Only Proteins." in: Cell reports, Vol. 21, Issue 7, pp. 1910-1921, (2018) (PubMed).

    Wyatt, Xiao, Americo, Earl, Moss: "Novel Nonreplicating Vaccinia Virus Vector Enhances Expression of Heterologous Genes and Suppresses Synthesis of Endogenous Viral Proteins." in: mBio, Vol. 8, Issue 3, (2018) (PubMed).

    Hagemeyer, Kierdorf, Frenzel, Xue, Ringelhan, Abdullah, Godin, Wieghofer, Costa Jordão, Ulas, Yorgancioglu, Rosenbauer, Knolle, Heikenwalder, Schultze, Prinz: "Transcriptome-based profiling of yolk sac-derived macrophages reveals a role for Irf8 in macrophage maturation." in: The EMBO journal, Vol. 35, Issue 16, pp. 1730-44, (2017) (PubMed).

    Granados-Durán, López-Ávalos, Hughes, Johnson, Morgan, Tamburini, Fernández-Llebrez, Grondona: "Complement system activation contributes to the ependymal damage induced by microbial neuraminidase." in: Journal of neuroinflammation, Vol. 13, Issue 1, pp. 115, (2017) (PubMed).

    Komatsu, Ibi, Chosa, Kyakumoto, Kamo, Shibata, Sugiyama, Ishisaki: "Zoledronic acid suppresses transforming growth factor-β-induced fibrogenesis by human gingival fibroblasts." in: International journal of molecular medicine, Vol. 38, Issue 1, pp. 139-47, (2017) (PubMed).

    Boareto, Jolly, Goldman, Pietilä, Mani, Sengupta, Ben-Jacob, Levine, Onuchic: "Notch-Jagged signalling can give rise to clusters of cells exhibiting a hybrid epithelial/mesenchymal phenotype." in: Journal of the Royal Society, Interface, Vol. 13, Issue 118, (2017) (PubMed).

    Feng, Cook, Tsai, Zhou, LaFlamme, Evans, Chen: "Discovery of a Small-Molecule BMP Sensitizer for Human Embryonic Stem Cell Differentiation." in: Cell reports, Vol. 15, Issue 9, pp. 2063-75, (2017) (PubMed).

    Weaver, Limzerwala, Naylor, Jeganathan, Baker, van Deursen: "BubR1 alterations that reinforce mitotic surveillance act against aneuploidy and cancer." in: eLife, Vol. 5, (2017) (PubMed).

  • Target

    EBI3 (IL-27b) (Interleukin-27 subunit beta (IL-27b))

    Alternative Name

    EBI-3

    Background

    The cytokine Interleukin 27 (IL-27) is produced in response to inflammation. It is made by activated antigen presenting cells including monocytes, endothelial cells, and dendritic cells. IL-27 consists of a heterodimeric combination of Epstein-Barr virus-induced molecule 3 (EBI3, or IL-27B) non-covalently linked with IL-27 p28 (or IL-27A). It is a regulator of T helper cell development and suppressor of T-cell proliferation. IL-27 has both pro- and anti-inflammatory properties. It can stimulate cytotoxic T cell activity and induce isotype switching in B-cells. It has diverse effects on innate immune cells. It induces monocytes and mast cells to secrete pro-inflammatory cytokines. When infection is present, IL-27 induces naive CD4+ T cells to proliferate and develop Th1 cell responses. As an anti-inflammatory regulator, IL-27 can inhibit Th1 or Th2 responses and restrict the strength and duration of adaptive immune responses. The IL-27 p28 subunit, a 28 kDa glycoprotein belonging to the type I cytokine family, is homologous to IL-12 p35, IL-23 p19, and IL-6. The EBI3 (Epstein-Barr virus-induced molecule 3, or IL-27B) subunit is a 34 kDa glycoprotein containing two fibronectin type III domains, and belongs to the type I cytokine receptor family. It can exist as a homodimer and can also heterodimerize with IL-27 p28 or IL-12 p35 subunit. It is homologous to the p40 subunit of IL-12 and IL-23 and to the extracellular domain of IL-6 R.
    Synonyms: Interleukin-27 subunit beta, IL-27 subunit beta, IL-27B, Epstein-Barr virus-induced gene 3 protein, EBV-induced gene 3 protein

    Gene ID

    50498

    NCBI Accession

    NP_056581

    UniProt

    O35228
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