Cayman 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). 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.^,, CD70 forms homotrimers and binds to its receptor, CD27 (Item No. ), 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.^, CD70 is overexpressed in various hematological malignancies and is associated with accelerated tumor cell proliferation. 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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