Recombinant Human CD27/TNFRSF7 Fc Avi-tag Protein, CF Summary
Accession # P26842.2
|IEGRMD||Human IgG1 Fc|
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
2 μg/lane of Biotinylated Recombinant Human CD27/TNFRSF7 Fc Chimera Avi-tag Protein (Catalog # AVI11027) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 57-69 kDa and 110-140 kDa, respectively.
CD27, also known as TNFRSF7, is an approximately 55 kDa transmembrane protein in the TNF receptor superfamily. It functions as a co‑stimulatory molecule that supports lymphocyte activation and survival (1). Mature human CD27 consists of a 172 amino acid (aa) extracellular domain (ECD) with three TNFR cysteine‑rich repeats, a 21 aa transmembrane segment, and a 48 aa cytoplasmic domain (2). Within the ECD, human CD27 shares 63% and 66% aa sequence identity with mouse and rat CD27, respectively. CD27 is expressed as a disulfide‑linked homodimer that carries N‑linked and O‑linked glycosylation (3, 4). Proteolytic cleavage of CD27 results in the shedding of a 28‑32 kDa fragment of the ECD (4). CD27 is weakly expressed on naïve T cells and NK cells and is up‑regulated upon cell activation (4, 5). It is also up‑regulated on activated germinal center B cells, plasma cells, and a subset of memory B cells (6, 7). CD27 binds to the transmembrane glycoprotein CD27 Ligand/CD70 which is expressed on activated B cells, activated T cells, and dendritic cells (1, 8, 9). This interaction contributes to the activation and survival of CD4+ helper T cells (8‑11), CD8+ effector T cells (12, 13), memory T cells (10), and NK cells (5, 14). Ligation of CD27 on B cells promotes germinal center formation and the expansion and affinity maturation of memory B cell responses (6, 15). Our Avi-tag Biotinylated CD27/TNFRSF7 Fc Chimeria features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
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