CD27L/CD70 Extracellular Domain (human, recombinant)

CD70, also known as CD27 ligand (CD27L), is a type II transmembrane glycoprotein and member of the tumor necrosis factor (TNF) ligand superfamily (TNFSF).¹ It is comprised of an N-terminal extracellular domain, a transmembrane domain, a stalk region, and a C-terminal TNF homology domain and is exclusively expressed on activated T and B cells and mature dendritic cells.^1,2,3 CD70 forms homotrimers and binds to its receptor, CD27 (Item No. 31828), on antigen-primed T cells, which induces NF-κB and MAPK signaling through TNF receptor-associated factors (TRAFs) and, when the T cell is stimulated by other factors, induces PI3K signaling to induce the co-stimulation and expansion of naïve CD4⁺ and CD8⁺ T cells.^4,1 CD70 is overexpressed in various hematological malignancies and is associated with accelerated tumor cell proliferation.³ CD70 expression is negatively correlated with overall survival in patients with diffuse malignant mesothelioma of the pleura. Cayman’s CD27L/CD70 Extracellular Domain (human, recombinant) protein can be used for binding assay applications. This protein is a disulfide-linked homodimer. The reduced monomer, comprised of CD70 (amino acids 39-193) fused to human IgG Fc at its N-terminus, consists of 413 amino acids and has a calculated molecular weight of 45.5 kDa. As a result of glycosylation, the monomer migrates at approximately 55-60, 110-120, and 160-170 kDa, corresponding to the monomeric, dimeric and trimeric forms, respectively, by SDS-PAGE under reducing conditions.

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1. Wajant, H. Therapeutic targeting of CD70 and CD27. Expert Opin. Ther. Targets 20(8), 959-973 (2016).

2. Prasad, K.V.S., Ao, Z., Yoon, Y., et al. CD27, a member of the tumor necrosis factor receptor family, induces apoptosis and binds to Siva, a proapoptotic protein. Proc. Natl. Acad. Sci. USA 94(12), 6346-6351 (1997).

3. Inaguma, S., Lasota, J., Czapiewski, P., et al. CD70 expression correlates with a worse prognosis in malignant pleural mesothelioma patients via immune evasion and enhanced invasiveness. J. Pathol. 250(2), 205-216 (2020).

4. Wyzgol, A., Müller, N., Fick, A., et al. Trimer stabilization, oligomerization, and antibody-mediated cell surface immobilization improve the activity of soluble trimers of CD27L, CD40L, 41BBL, and glucocorticoid-induced TNF receptor ligand. J. Immunol. 183(3), 1851-1861 (2009).