Recombinant Human IL-1 RAcP/IL-1 R3 His Avi-tag Protein, CF Summary
Additional Information |
Biotinylated |
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Human IL-1 RI Fc Chimera
(Catalog #
11085-RI)
is immobilized at 2 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 His-tag Avi-tag (Catalog # AVI9176) with an
ED 50 of 50.0-400 ng/mL. |
Source |
Chinese Hamster Ovary cell line, CHO-derived human IL-1 RAcP/IL-1 R3 protein Human IL-1 RAcP/IL-1 R3 (Ser21-Glu359) Accession # Q9NPH3.2 | 6-His tag | Avi-tag | N-terminus | | C-terminus | |
|
Accession # |
|
N-terminal Sequence |
Ser21 |
Structure / Form |
Biotinylated via Avi-tag |
Protein/Peptide Type |
Recombinant Proteins |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
42 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
59-65 kDa, under reducing conditions. |
Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. |
Purity |
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions |
Reconstitute at 500 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human IL-1 RAcP/IL-1 R3 His Avi-tag Protein, CF
Background
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 (9). Neuronal IL-1 RAcP interacts trans-synaptically with PTP sigma and can induce excitatory pre- and post-synaptic development (10). . Our Avi-tag Biotinylated Human IL-1 RAcP 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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