Human IL-23 alpha & Mouse IL-12 beta Heterodimer Protein (HEK293, His-Avi)
IL-23 alpha and IL-12 beta are the IL-23p19 and IL-12p40 subunits, respectively, composing IL-23 via heterodimerization manner. IL-23 binds to a heterodimeric receptor composed of IL-12RB1 and IL-23R, activates the Jak-Stat signaling cascade, acts on memory CD4(+) T cells preferentially. IL-23 also involves in activation of several pathways including p38 MAPK or NF-κB and promotes the production of pro-inflammatory cytokines such as interleukin-17A/IL17A. Human IL-23 alpha & Mouse IL-12 beta Heterodimer Protein is produced in HEK293 cells, with a C-Terminal Avi and His-tag.
- Species: Human; Mouse
- Source: HEK293
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Storage:Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
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Biological Activity
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Technical Parameters
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Product Properties
- Documentation
- References
- Help & FAQs
Biological Activity
Description
IL-23 alpha and IL-12 beta are the IL-23p19 and IL-12p40 subunits, respectively, composing IL-23 via heterodimerization manner. IL-23 binds to a heterodimeric receptor composed of IL-12RB1 and IL-23R, activates the Jak-Stat signaling cascade, acts on memory CD4(+) T cells preferentially[1]. IL-23 also involves in activation of several pathways including p38 MAPK or NF-κB and promotes the production of pro-inflammatory cytokines such as interleukin-17A/IL17A[2]. Human IL-23 alpha & Mouse IL-12 beta Heterodimer Protein is produced in HEK293 cells, with a C-Terminal Avi and His-tag.
Background
IL-23 alpha and IL-12 beta, also known as IL23p19 and IL12p40, respectively, and composing IL-23 in a heterodimerization manner, exerts proinflammatory effects and promotes angiogenesis[1][5].
IL-23 belongs to the IL-12 cytokine family together with IL-12 p35/p40, IL-27 EBI3/p28 and IL-35 EBI3/p35, and is produced by various immune cells such as dendritic cells and macrophages upon Toll-like receptor signaling in tissues[3].
IL-23 has a preference expression on memory CD4(+) T cells, and activates the Jak-Stat signaling cascade. IL-23 leads to IL-23 receptor phosphorylation and forms a docking site to trigger phosphorylation signal of STAT3 and STAT4[1].
IL-23 is a key factor perpetuating Th17 cell activation and cytokine production by binding IL-23 receptor to produce Th17 cytokines such as IL17 A, IL-17 F and IL-22[2].
IL-23 also acts function on natural killer cells, results interferon-γ secretion increasing and enhances antibody-dependent cellular cytotoxicity[4].
The sequence of amino acids in IL-23 alpha proteins of mouse shows moderately high similarity with rat (87.76%) and is very different from human (74.60%) or cynomolgus (74.60%), while the sequence of IL-12 beta proteins of human is very different from human (69.04%) and shows high similarity with rat (92.24%).
IL-23 facilitates development of inflammation in numerous other models of immune pathology where IL-12 had previously been implicated, including models of arthritis,intestinal inflammation, and psoriasis[6][7][8].
Technical Parameters
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Species Human; Mouse
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Source HEK293
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Tag C-Avi;C-8*His
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Synonyms
IL23A; Interleukin 23, Alpha Subunit P19; Interleukin 23 Subunit Alpha; Interleukin-23 Subunit Alpha; SGRF; Interleukin-23 Subunit P19; IL23P19; IL-23 Subunit Alpha; IL-23A; IL-23p19; IL-23; IL-23-A; P19; JKA3 Induced Upon T-Cell Activation; Interleukin-S
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Predicted Molecular Mass
21.7 kDa (Human IL-23 alpha) & 35.8 kDa (Mouse IL-12 beta)
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Molecular Weight
Approximately 22 kDa (Human IL-23 alpha) & 45-60 kDa (Mouse IL-12 beta), based on SDS-PAGE under reducing conditions, due to the glycosylation.
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Purity
≥ 95%, as determined by Bis-Tris PAGE.
Product Properties
Lyophilized powder.
<1 EU/μg, determined by LAL method.
It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH2O.
Stored at -20°C for 2 years from date of receipt. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.
Room temperature in continental US; may vary elsewhere.
Documentation
References
[1]. Oppmann B, et al. Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with biological activities similar as well as distinct from IL-12. Immunity. 2000 Nov;13(5):715-25. [Content Brief]
[2]. Parham C, et al. A receptor for the heterodimeric cytokine IL-23 is composed of IL-12Rbeta1 and a novel cytokine receptor subunit, IL-23R. J Immunol. 2002 Jun 1;168(11):5699-708. [Content Brief]
[3]. Neurath MF. IL-23 in inflammatory bowel diseases and colon cancer. Cytokine Growth Factor Rev. 2019 Feb;45:1-8. [Content Brief]
[4]. Teng MW, et al. IL-12 and IL-23 cytokines: from discovery to targeted therapies for immune-mediated inflammatory diseases. Nat Med. 2015 Jul;21(7):719-29. [Content Brief]
[5]. Li Y, et al. Regulation of Memory T Cells by Interleukin-23. Int Arch Allergy Immunol. 2016;169(3):157-62. [Content Brief]
[6]. Langowski JL, et al. IL-23 promotes tumour incidence and growth. Nature. 2006 Jul 27;442(7101):461-5. [Content Brief]
[7]. Murphy CA, et al. Divergent pro- and antiinflammatory roles for IL-23 and IL-12 in joint autoimmune inflammation. J Exp Med. 2003 Dec 15;198(12):1951-7. [Content Brief]
[8]. Yen D, et al. IL-23 is essential for T cell-mediated colitis and promotes inflammation via IL-17 and IL-6. J Clin Invest. 2006 May;116(5):1310-6. [Content Brief]
[9]. Chan JR, et al. IL-23 stimulates epidermal hyperplasia via TNF and IL-20R2-dependent mechanisms with implications for psoriasis pathogenesis. J Exp Med. 2006 Nov 27;203(12):2577-87. [Content Brief]
[10]. Yago T, et al. IL-23 induces human osteoclastogenesis via IL-17 in vitro, and anti-IL-23 antibody attenuates collagen-induced arthritis in rats. Arthritis Res Ther. 2007;9(5):R96. [Content Brief]
Calculators
Concentration (start) × Volume (start) = Concentration (final) × Volume (final)
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