Recombinant Human IL-22BP Fc Chimera Avi-tag Protein, CF Summary
Accession # NP_851826.1
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||Supplied as a 0.2 μm filtered solution in PBS with Trehalose.|
|Shipping||The product is shipped with dry ice or equivalent. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Measured by its binding ability in a functional ELISA. When Recombinant Human IL-22 Protein (782-IL) is coated at 0.500 µg/mL (100 µL/well), Biotinylated Recombinant Human IL‑22BP Fc Chimera Avi-tag (Catalog # AVI1087) binds with an ED50 of 50.0-400 ng/mL.
2 μg/lane of Recombinant Human IL-22BP Fc Chimera Avi-tag Protein (Catalog # AVI1087) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 73-82 kDa and 146-164 kDa, respectively.
Interleukin 22 binding protein (IL-22BP), also known as CRF210, CRF2X, and IL-22 RA2, is a 35-45 kDa secreted glycoprotein in the type II cytokine receptor family (CRF). IL-22 signals through a receptor complex consisting of IL-22 R and IL-10Rb. IL-10Rb is also a component of the receptor complexes for IL-10, IL-26, IL-28, and IL-29 (1, 2). IL-22BP blocks the interaction of IL-22 with IL-22 R, preventing IL-22 induced production of reactive oxygen species, IL6, IL-10, and TNFa (3-8). In vivo, it regulates the proinflammatory effe-cts of IL-22 (e.g. neutrophil infiltration) but not of IL-10 (7). Mouse IL-22BP can neutralize the bioactivity of both mouse and human IL-22 (6). IL-22BP is produced by dendritic cells (DC), epithelial cells, activated B cells, and activated monocytes (3, 6, 9, 10). It is constitutively expressed by DC but is down regulated during local inflammation and in response to tissue damage (11-13). IL-22BP is critical for limiting IL-22 induced epithelial cell proliferation during wound healing, and its deficiency can enable uncontrolled proliferation and enhance tumor development (12). Mature human IL-22BP contains two Fibronectin type-III domains (4, 6). Alternative splicing generates additional isoforms that contain a 32 amino acids (aa) insertion in the first FnIII domain and may also be truncated within the second Fc-III domain (3, 4, 14). Human IL-22BP without the 32 aa insertion shares 68% and 73% amino acid (aa) sequence identity with mouse and rat IL-22BP, respectively. Our Avi-tag Biotinylated Recombinant Human IL‑22BP 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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