Recombinant Human IL-1 RAcP/IL-1 R3 His Avi-tag Protein, CF New

Recombinant Human IL-1 RAcP/IL-1 R3 His Avi-tag Protein, CF Summary

Product Specifications

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.

Scientific Data

Binding Activity View Larger

When Recombinant Human IL‑1 RI Fc Chimera Protein (11085-RI) is immobilized at 2 µg/mL (100 µL/well) in the presence of Recombinant Human IL‑1 beta /IL‑1F2 Protein (201-LB), it binds to Biotinylated Recombinant Human IL‑1 RAcP/IL‑1 R3 His-tag Avi-tag Protein (Catalog # AVI9176) with an ED₅₀ of 50.0-400 ng/mL.

SDS-PAGE View Larger

2 μg/lane of Recombinant Human IL-1 RAcP/IL-1 R3 His-tag Avi-tag Protein (Catalog # AVI9176) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 59-65 kDa.

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.