Recombinant Human IL-31RA Fc Chimera Avi-tag Protein, CF
Recombinant Human IL-31RA Fc Chimera Avi-tag Protein, CF Summary
Learn more about Avi-tag Biotinylated ProteinsProduct Specifications
Human IL-31RA (Ala20-Ser516) Accession # Q8NI17.1 | DIEGRMD | Human IgG1 Fc (Pro100-Lys330) | Avi-tag |
N-terminus | C-terminus | ||
Analysis
Product Datasheets
Carrier Free
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.
AVI11028
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Reconstitution | Reconstitute at 200 μg/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.
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Scientific Data
When Recombinant Human IL-31 (HEK293-expressed) Protein (10425-IL) is immobilized at 1.0 µg/mL (100 µL/well), the concentration of Biotinylated Recombinant Human IL-31RA Fc Chimera Avi-tag (Catalog # AVI11028) that produces 50% of the optimal binding response is 0.10-1.00 μg/mL
2 μg/lane of Biotinylated Recombinant Human IL-31R Fc Chimera Avi-tag Protein (Catalog # AVI11028) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 120-145 kDa and 240-290 kDa, respectively.
Reconstitution Calculator
Background: IL-31RA
The interleukin-31 receptor A subunit (IL-31 RA), also known as gp130-Like Monocyte Receptor (GLM-R or GPL), is a ~100 kDa type I transmembrane glycoprotein that is classified as being a type I cytokine receptor (1, 2). A heterodimeric complex of IL-31 RA and the oncostatin M receptor (OSM-R) functions as the signaling receptor for IL-31 (3). Both subunits are inducibly expressed throughout the myelomonocytic lineage and are upregulated by interferon-gamma and bacterial lipopolysaccharides (1-3). IL-31 RA is also expressed on keratinocytes, dorsal root ganglia neurons, and variably on lung epithelial cells (3-6). The 732 amino acid (aa) IL-31 RA contains a 19 aa signal sequence, a 500 aa extracellular domain (ECD), a 21 aa transmembrane domain and a 192 aa cytoplasmic domain. The ECD shares 60%, 58%, 73% and 70% aa identity with mouse, rat, canine and bovine IL-31 RA ECD, respectively. Human IL-31 receptors do not respond to mouse IL-31 (7). The ECD contains five fibronectin type III domains; the first two contain four conserved cysteine residues and a WSXWS motif common to type I cytokine receptors (2). Twelve alternately spliced human IL-31 RA isoforms are known and range in size from 356-745 amino acids. A long (745 aa) and a short (560 aa) transmembrane form are the predominant forms, and many cell lines express both forms (8). The long form, like the 732 aa form, signals by recruiting STAT3, 5 or 1, while the short form does not recruit STATs and inhibits IL-31 signaling. The ratio of these forms and their co-expression with OSM-R determines a cell's response to IL-31 (8). In both humans and transgenic mice, IL-31 from skin-homing Th2 cells may contribute to the pruritis (itching) associated with nonatopic dermatitis, especially in infected skin (3, 9, 10). Our Avi‑tag Biotinylated IL-31 RA Fc Chimera 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
- Ghilardi, N. et al. (2002) J. Biol. Chem. 277:16831.
- Diveu, C. et al. (2003) J. Biol. Chem. 278:49850.
- Dillon, S. R. et al. (2004) Nat. Immunol. 5:752.
- Chattopadhyay, S. et al. (2007) J. Biol. Chem. 282:3014.
- Perrigoue, J. G. et al. (2007) J. Exp. Med. 204:481.
- Bando, T. et al. (2006) Neuroscience 142:1263.
- Broxmeyer, H. E. et al. (2007) Exp. Hematol. 35:78.
- Diveu, C. et al. (2004) Eur. Cytokine. Netw. 15:291.
- Bilsborough, J. et al. (2006) J. Allergy Clin. Immunol. 117:418.
- Sonkoly, E. et al. (2006) J. Allergy Clin. Immunol. 117:411.
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