研究方向
IL-12β蛋白,又称IL12 p40亚基或IL-12B,与IL-12 p35亚基(IL-12A)异二聚化形成IL-12,与IL23 p19亚基异二聚化形成IL-23,发挥不同的调节作用功能。
IL-12 和 IL23 属于 IL-12 家族,参与促炎反应,由活化的巨噬细胞表达,是 Th1 细胞发育的重要诱导剂。
IL-12 信号通过 p-STAT4 介导的 IL-12Rβ1 和 IL-12Rβ2 传递,而 IL-23 信号通过 p-STAT1 介导的 IL-12Rβ1 和 IL-23R 传递p-STAT3。
人IL-12β蛋白的氨基酸序列与小鼠(69.04%)和大鼠(69.04%)有很大差异。
白细胞介素 12 (IL-12) 家族已知是一种炎症因子,可诱导自身免疫性炎症,因此可能是自身免疫性炎症性疾病的原因,并且可能对肿瘤发生具有重要作用。
生物活性
Measured by its binding ability in a functional ELISA. When Recombinant Human IL‑12 R beta 1 Fc Chimera is immobilized at 1 µg/mL (100 µL/well), the concentration of Recombinant Human IL‑12/IL‑23 p40 Monomer that produces 50% of the optimal binding response is 1-6 ng/mL.
After reconstitution, the protein solution is stable at -20℃ for 3 months, at 2-8℃ for up to 1 week.未开盖的干粉蛋白在 -20°C至-80°C可保存12个月;
复溶之后,蛋白溶液在-20°C及以下可保存3个月,在2-8℃可保存1周。
背景信息
Interleukin 12, also known as natural killer cell stimulatory factor (NKSF) or cytotoxic lymphocyte maturation factor (CLMF), is a pleiotropic cytokine originally identified in the medium of activated human B lymphoblastoid cell lines. IL-12 is produced by macrophages and B lymphocytes and has multiple effects on T cells and NK cells, including stimulation of cytotoxic activity, proliferation, and promotion of Th1 development as well as IFN-gamma and TNF production. IL-12 is a disulfide-linked, 70 kDa (p70) heterodimeric glycoprotein composed of a 40 kDa (p40) subunit and a 35 kDa (p35) subunit. The p40 and p35 subunits by themselves have no IL-12 activity, the p40 dimer has been shown to bind the IL-12 receptor and to be an IL-12 antagonist. Free p35 has not been detected in supernatant solutions of cultured cells expressing only p35 or both p35 and p40 mRNAs. In contrast, p40 is secreted in excess of IL-12 in cells expressing both p35 and p40 mRNAs. The p40 subunit of IL-12 has been shown to have extensive amino acid sequence homology to the extracellular domain of the human IL-6 receptor while the p35 subunit shows distant but significant sequence similarity to IL-6, G-CSF, and chicken MGF. These observations have led to the suggestion that IL-12 might have evolved from a cytokine/soluble receptor complex. Human and mouse IL-12 share 70% and 60% amino acid sequence homology in their p40 and p35 subunits, respectively. IL-12 apparently shows species specificity with human IL-12 reportedly showing minimal activity in the murine system.