TNFRSF7/CD27 Extracellular Domain (human, recombinant)

TNFRSF7|Tp55|Tumor Necrosis Factor Receptor Superfamily Receptor 7

CD27, also known as tumor necrosis factor receptor superfamily receptor 7 (TNFRSF7), is a type I transmembrane glycoprotein with roles in T cell-mediated immunity.{59402,59403} It is comprised of an extracellular domain containing three cysteine-rich domains (CRDs), a transmembrane domain, and a short cytoplasmic domain that facilitates intracellular signaling.{59402} CD27 is expressed on a broad range of lymphocytes, including natural killer (NK), B, and T cells, with T cell CD27 expression increasing upon T cell receptor stimulation.{59405} Binding of homotrimeric CD70 to CD27 on antigen-primed T cells induces NF-kB 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.{54194,59406} Knockout of CD27 reduces thymic development of regulatory T cell (Treg) precursors and enhances apoptosis of mature Tregs in mice. Levels of CD27-expressing plasma cells are increased in the periphery and positively correlate with the disease activity index and serum levels of anti-dsDNA autoantibodies in patients with systemic lupus erythematosus (SLE).{59404} Cayman’s TNFRSF7/CD27 Extracellular Domain (human, recombinant) protein can be used for binding assay applications. This protein is a disulfide-linked homodimer. The reduced monomer, comprised of CD27 (amino acids 21-192) fused to His-tagged human IgG1 Fc at its C-terminus, consists of 420 amino acids, has a calculated molecular weight of 47.2 kDa, and a predicted N-terminus of Thr21 after signal peptide cleavage. As a result of glycosylation, the monomer migrates at approximately 65 kDa by SDS-PAGE under reducing conditions.

-80

-80

Lyophilized from sterile PBS, pH 7.4

365

≥95% estimated by SDS-page