FITC-Labeled IL-1RAcP/IL-1 R3 Protein, Human (HEK293, His)

IL-1RAcP/IL-1 R3 protein is a co-receptor in the IL-36 and IL-1 signaling systems, forming a receptor complex to activate NF-kappa-B and other pathways. FITC-Labeled IL-1RAcP/IL-1 R3 Protein, Human (HEK293, His) is the recombinant human-derived FITC-Labeled IL-1RAcP/IL-1 R3 protein, expressed by HEK293 , with His labeled tag.

IL-1RAcP/IL-1 R3 protein functions as a coreceptor within the IL-36 and IL-1 signaling systems. It acts as a coreceptor with IL1R1 to form a high-affinity interleukin-1 receptor complex, mediating interleukin-1-dependent activation of NF-kappa-B and other pathways. The formation of this complex involves the association of IL1RAcP/IL-1 R3 with IL1R1 bound to IL1B. The signaling cascade includes the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the TIR domains of the receptor/coreceptor subunits. Notably, IL1RAcP/IL-1 R3 does not independently bind to interleukin-1; rather, the binding of IL1RN to IL1R1 prevents the association of IL1RAcP/IL-1 R3 with IL1R1, thereby inhibiting complex formation and downstream signaling. The cellular response is further modulated through a non-signaling interaction with the membrane IL1R2 decoy receptor. Additionally, IL1RAcP/IL-1 R3 serves as a coreceptor for IL1RL1 in the IL-33 signaling system and can bidirectionally induce pre- and postsynaptic differentiation of neurons by trans-synaptically binding to PTPRD. Furthermore, it may play a role in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells and enhances the ability of secreted IL1R1 to inhibit IL-33 signaling. Moreover, the protein forms a complex with secreted ligand-bound IL1R2, increasing the affinity of secreted IL1R2 for IL1B, which represents a dominant mechanism for the neutralization of IL1B by secreted/soluble receptors.

Human

HEK293

His

Q9NPH3-1 (S21-E359)

3556

Partial

SERCDDWGLDTMRQIQVFEDEPARIKCPLFEHFLKFNYSTAHSAGLTLIWYWTRQDRDLEEPINFRLPENRISKEKDVLWFRPTLLNDTGNYTCMLRNTTYCSKVAFPLEVVQKDSCFNSPMKLPVHKLYIEYGIQRITCPNVDGYFPSSVKPTITWYMGCYKIQNFNNVIPEGMNLSFLIALISNNGNYTCVVTYPENGRTFHLTRTLTVKVVGSPKNAVPPVIHSPNDHVVYEKEPGEELLIPCTVYFSFLMDSRNEVWWTIDGKKPDDITIDVTINESISHSRTEDETRTQILSIKKVTSEDLKRSYVCHARSAKGEVAKAAKVKQKVPAPRYTVE

Approximately 50-60 kDa, based on SDS-PAGE under reducing conditions, due to the glycosylation.

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.