Recombinant Human IL-2 R beta His-tag Avi-tag Protein, CF Summary
|Human IL-2 R beta |
Accession # P14784.1
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||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.
Background: IL-2 R beta
Functional IL-2 receptors can exist in two affinity states on cell surfaces, the high affinity complex consisting of heterotrimers of the alpha, beta, and gamma chains, and the intermediate affinity complex comprising heterodimers of the beta and gamma chains. Individual beta chains and alpha chains exhibit low affinity IL-2 binding and the gamma chain alone does not bind IL-2. In addition to their involvement in IL-2 mediated signal transduction, both the beta chain and gamma chain have been shown to be required for IL-15 mediated signaling. IL-2 R beta is a member of the cytokine receptor superfamily. Human IL-2 R beta cDNA encodes a 551 amino acid residue precursor Type I membrane protein with a 26 residue signal peptide, a 214 residue extracellular region, a 25 residue transmembrane region and a 286 residue cytoplasmic domain. A soluble IL-2 R beta (IL-2 sR beta ) has been identified in the culture supernatants of a human lymphoid cell line, YT, that displays IL-2 R beta. At present, the function of IL-2 sR beta is unclear. Recombinant human IL-2 sR beta binds IL-2 with low affinity and is not an effective IL-2 antagonist on cells displaying the high or intermediate affinity IL-2 signaling receptors. Nevertheless, IL-2 sR beta binds IL-15 with sufficient affinity to neutralize IL-15 biological activities. Our Avi-tag Biotinylated Recombinant Human IL‑2 R beta 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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