||Recombinant Human CD27 Molecule, Fc-Tagged expressed in human cells is a disulfide-linked homodimeric protein. The reduced monomer comprises 420 amino acids and has a calculated molecular mass of 47.2 kDa. As a result of glycosylation, the monomer migrates as an approximately 65 kDa band in SDS-PAGE under reducing conditions.
||Human CD27 is a lymphocyte-specific member of the TNF receptor superfamily. CD27 is expressed on a subset of human thymocytes and on the majority of mature T cells. CD27 expression is up-regulated after TCR stimulation. Within the CD4+ compartment, it is preferentially expressed on CD45RA+ cells. In contrast, it is preferentially expressed on CD45RO+ cells in the CD8+ compartment. CD27 also appeaars to be a potential marker for memory B cells. It exists as both a disulfide-linked dimer on the cell surface and as a soluble protein found in serum. Human CD27 is a 260 amino acid (aa) protein with a 20 aa signal, a 173 aa extracellular domain, a 20 aa transmembrane domain, and a 47 aa cytoplasmic domain. A DNA sequence encoding the extracellular domain (Met 1- Ile 192) of human CD27 (NP_001233.1) was fused with the C-terminal polyhistidine-tagged Fc region of human IgG1 at the carboxy-terminus.
||> 95%, as determined by SDS-PAGE and SEC-HPLC Analysis
|Predicted N terminal:
||Supplied as a 0.2μm filtered solution of 100mM Glycine, 10mM NaCl,50 mM Tris, pH 7.5
||< 1.0 EU per 1 μg of the cytokine as determined by the LAL method
||Follow the instructions on the vial. Centrifuge the vial at 4°Cbefore opening to recover the entire contents.
||Samples are stable for up to twelve months from date of receipt -70C
||Store at –70°C; Avoid repeated freeze-thaw cycles