Glycoprotein 130 Extracellular Domain (human, recombinant)

Glycoprotein 130 (gp130), also known as IL-6 signal transducer (IL6ST), is a single-pass type I membrane protein and shared signal transducing receptor for the IL-6 cytokine family.¹ It is composed of an N-terminal immunoglobulin-like domain, two cytokine-binding domains, three fibronectin type III-like domains, a transmembrane domain, and a cytoplasmic domain, which contains JAK and STAT binding sites.^2,3,4 Soluble forms of gp130 are formed via alternative splicing of the extracellular domain.³ gp130 is ubiquitously expressed and its membrane-bound form associates with membrane-bound cytokine-cytokine receptor complexes via the classical signaling pathway to induce JAK/STAT signaling.^4,1,5 In contrast, in the trans-signaling pathway, membrane-bound cytokines and soluble cytokine receptors form a complex that can associate with either membrane-bound or soluble gp130, and high concentrations of soluble gp130 lead to signaling inhibition.^5,3 Due to the variety of cytokines that utilize it for signaling, gp130 is involved in many biological processes, including immune signaling, organ and neural development, and bone homeostasis.⁴ Loss-of-function mutations in IL6ST are associated with hyper-IgE syndrome, extended Stüve-Wiedemann syndrome, or craniosynostosis, while a gain-of-function mutation is associated with inflammatory hepatocellular adenoma. Cayman’s Glycoprotein 130 Extracellular Domain (human, recombinant) protein can be used for cell-based assays. This protein is a disulfide-linked homodimer. The reduced monomer, composed of gp130 (amino acids 23-618) fused to His-tagged human IgG1 Fc at its C-terminus, consists of 844 amino acids and has a calculated molecular weight of 96 kDa. As a result of glycosylation, the monomer migrates at approximately 125-140 kDa by SDS-PAGE under reducing conditions.

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1. Minegishi, Y. Hyper-IgE syndrome, 2021 update. Allergol. Int. 70(4), 407-414 (2021).

2. Moritz, R.L., Hall, N.E., Connolly, L.M., et al. Determination of the disulfide structure and N-glycosylation sites of the extracellular domain of the human signal transducer gp130. The Journal of Biological Chemisty 276(11), 8244-8253 (2001).

3. Martínez-Pérez, C., Kay, C., Meehan, J., et al. The IL6-like cytokine family: Role and biomarker potential in breast cancer. J. Pers. Med. 11(11), 1073 (2021).

4. Chen, Y.-H., van Zon, S., Adams, A., et al. The human GP130 cytokine receptor and its expression-an atlas and functional taxonomy of genetic variants. J. Clin. Immunol. 44(1), 30 (2023).

5. Rose-John, S., Jenkins, B.J., Garbers, C., et al. Targeting IL-6 trans-signalling: Past, present and future prospects. Nat. Rev. Immunol. 23(10), 666-681 (2023).