Recombinant Human IL-6R alpha His-tag Avi-tag Protein, CF Summary
|Human IL-6R alpha|
Accession # P08887.1
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 1 mg/mL in PBS.|
|Shipping||The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Human IL-6 (7270-IL) is immobilized at 0.25 μg/mL (100 μL/well), Biotinylated Recombinant Human IL-6R alpha His-tag Avi-tag (Catalog # AVI10537) binds with an ED50 of 0.1-1 μg/mL.
2 μg/lane of Biotinylated Recombinant Human IL-6R alpha His-tag Avi-tag (Catalog # AVI10537) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 65-80 kDa.
Background: IL-6R alpha
Interleukin-6 receptor subunit alpha (IL-6Ra), also known as membrane glycoprotein 80 (gp80), IL-6R 1 or CD126, is a single-pass type I membrane protein of the interleukin receptor family. Human IL-6Ra is an 80 kDa receptor component that binds IL-6 with low affinity and forms one-half of the IL-6R receptor complex. IL-6Ra associates with a non-ligand binding 130 kDa glycoprotein signal-transducing component (CD130; gp130) for high-affinity binding to IL-6 (1-4). When bound to IL-6, the IL-6R complex forms a trimer, which homodimerizes to form a hexameric cellular signaling complex (1, 4). Human IL-6Ra consists of an extracellular domain (ECD) with an N-terminal Ig-like C2-type domain and a cytokine-binding domain containing two fibronectin type-III domains with a WSXWS motif, a helical transmembrane segment and a cytoplasmic domain. Within the mature ECD, human IL-6Ra shares 51% and 52% amino acid sequence identity with mouse and rat IL-6Ra, respectively. Soluble forms of IL-6Ra can be generated via ADAM10 and ADAM17 cleavage of membrane bound IL-6Ra, alternative mRNA splicing and microvesicle release (3, 4). Unlike gp130 that is expressed ubiquitously, the cellular distribution of IL-6 R alpha is predominantly limited to hepatocytes and leukocyte subpopulations such as monocytes, neutrophils, T and B cells. Soluble IL-6R alpha has been found in various body fluids (5). It has been documented that elevated soluble IL-6 R is associated with numerous diseases including arthritic lesions, multiple myeloma and Crohn's disease (6, 7). Our Avi-tag Biotinylated IL-6Ra 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.
- Hansen, Morton. (2020) Immun. Inflamm. Dis. 8:170.
- Salem, D. et al. (2018) Leuk Lymphoma. 59:178.
- Dayer, J. and Choy, E. (2009) Rheumatology. 49:15.
- Schumacher, N. et al. (2015) J. Biol. Chem. 290:26059.
- Novick, D. et al. (1989) J. Exp. Med. 170:1409.
- Jones, S.A. et al. (2001) FASEB J. 15:43.
- Jones, S.A. and S. Rose-John (2002) Biochim. Biophys. Acta 1592:251.
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