Recombinant Human IL-1 RAcP/IL-1 R3 Fc Avi-tag Protein, CF
Recombinant Human IL-1 RAcP/IL-1 R3 Fc Avi-tag Protein, CF Summary
Learn more about Avi-tag Biotinylated ProteinsProduct Specifications
When Recombinant Human IL-1 RII Fc Chimera (Catalog # 663-2R) is immobilized at 0.5 µg/mL (100 µL/well), in the presence of Recombinant Human IL-1 beta /IL-1F2 (Catalog # 201-LB), it binds to Biotinylated Recombinant Human IL-1 RAcP/IL-1 R3 Fc Chimera Avi-tag (Catalog # AVI11139) with an ED50 of 4.00-36.0 ng/mL.
Human IL-1RAP (Ser21-Glu359) Accession # Q9NPH3.2 | IEGRMD | Human IgG1 (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.
AVI11139
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.
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Scientific Data
When Recombinant Human IL-1 RII Fc Chimera (663-2R) is immobilized at 0.5 µg/mL (100 µL/well), in the presence of Recombinant Human IL-1 beta /IL-1F2 (201-LB), it binds to Biotinylated Recombinant Human IL-1 RAcP/IL-1 R3 Fc Chimera Avi-tag Protein (Catalog # AVI11139) with an ED50 of 4.00-36.0 ng/mL.
2 μg/lane of Biotinylated Recombinant Human IL‑1 RAcP/IL‑1 R3 Fc Chimera Avi-tag Protein (Catalog # AVI11139) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 83-93 kDa and 170-190 kDa, respectively.
Reconstitution Calculator
Background: IL-1 RAcP/IL-1 R3
IL-1 Receptor Accessory Protein (IL-1 RAcP), also known as IL-1 R3, is a ubiquitously expressed 70-90 kDa member of the Interleukin-1 receptor family of proteins (1). It serves as a non-ligand-binding component of the receptors for IL-1 alpha, IL-1 beta, IL-33, and IL-36 (2-4). It is a subunit of the functional signaling complex with IL-1 RI and associates with IL-1 RII in a non-signaling receptor complex (2, 5). In addition, it interacts with ST2/IL-1 R4 on mast cells and Th2 cells to create a functional IL-33 receptor complex (3). IL-1 RAcP also functions as a co-receptor for IL-36 alpha /IL-1F6, IL-36 beta /IL-1F8, and IL-36 gamma /IL-1F9 (4). Mature human IL-1 RAcP consists of a 347 amino acid (aa) extracellular domain (ECD) with three Ig-like domains, a 21 aa transmembrane segment, and a 182 aa cytoplasmic domain (2). Within the ECD, human IL-1 RAcP shares 86% aa sequence identity with mouse and rat IL-1 RAcP. Alternative splicing generates two secreted decoy receptor isoforms and an isoform with a substituted cytoplasmic domain (6-8). When present with soluble IL-1 RII, soluble IL-1 RAcP increases the IL-1 binding affinity of IL-1 RII more than 100-fold, thus neutralizing the effects of IL-1 (Our Avi-tag Biotinylated human IL-1 RAcP 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.
- Boraschi, D. and A. Tagliabue (2013) Semin. Immunol. 25:394.
- Greenfeder, S.A. et al. (1995) J. Biol. Chem. 270:13757.
- Chackerian, A.A. et al. (2007) J. Immunol. 179:2551.
- Towne, J.E. et al. (2004) J. Biol. Chem. 279:13677.
- Lang, D. et al. (1998) J. Immunol. 161:6871.
- Lu, H.-L. et al. (2008) Mol. Immunol. 45:1374.
- Jensen, L.E. et al. (2000) J. Immunol. 164:5277.
- Jensen, L.E. and A.S. Whitehead (2003) Cell. Signal. 15:793.
- Smith, D.E. et al. (2003) Immunity 18:87.
- Yoshida, T. et al. (2012) J. Neurosci. 32:2588.
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