Detects human IL-1RAcP/IL-1 R3 in direct ELISAs. In direct ELISAs, no cross-reactivity with recombinant human (rh) IL-1 RI, rhIL-1 RII, rhST2, rhIL-18 R alpha, IL-1 Rrp2, rhIL-18 RAP, rhSIGIRR, rhIL-1 RAPL1, rhIL-1 RAPL2, rhTLR1, rhTLR2, rhTLR3, rhTLR4, rhTLR5, rhTLR7, rhTLR8, rhTLR9, rhTLR10, rhMD-1, rhMD-2, or recombinant mouse RP105 is observed.
Monoclonal Mouse IgG1 Clone # 89412
Protein A or G purified from hybridoma culture supernatant
S. frugiperda insect ovarian cell line Sf21-derived recombinant human IL-1RAcP/IL-1 R3 Ser21-Glu359 (predicted) Accession # Q9NPH3
Supplied in a saline solution containing BSA and Sodium Azide.
Detection of IL‑1 RAcP/IL‑1 R3 in Human Monocytes by Flow Cytometry.
Human peripheral blood monocytes were stained with Mouse Anti-Human IL‑1 RAcP/IL‑1 R3 Alexa Fluor® 700‑conjugated Monoclonal Antibody (Catalog # FAB676N, filled histogram) or isotype control antibody (Catalog # IC002N, open histogram). View our protocol for Staining Membrane-associated Proteins.
Preparation and Storage
The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage
Protect from light. Do not freeze.
12 months from date of receipt, 2 to 8 °C as supplied.
Background: IL-1 RAcP/IL-1 R3
IL-1 Receptor Accessory Protein (also IL-1 R3) is a ubiquitous 70-90 kDa member of the interleukin-1 receptor family of proteins (1-5). It serves as a non-ligand-binding accessory component of the receptors for IL-1 alpha, IL-1 beta, and IL-33 (6, 7). Together with IRAK4 and MyD88, it generates a functional signaling complex with IL-1 RI; by itself, it generates a non-signaling, but high-affinity binding complex with IL-1 RII (8). In addition, it interacts with ST2 on mast cells and Th2 T cells to create a functional IL-33 receptor complex (7). Mature human IL-1 RAcP is a type I transmembrane glycoprotein that is 550 amino acids in length. It contains a 347 amino acid (aa) extracellular region (aa 21-367), a 21 aa transmembrane segment, and a 182 aa cytoplasmic domain (9). The extracellular region shows three C2-type Ig-like domains, the most membrane proximal of which is suggested to be responsible for dimerization with IL-1 RI (10). There are three alternative splice forms reported for IL-1 RAcP. One is transmembrane and shows a 239 aa substitution for the C-terminal 122 amino acids (11). The other two are soluble; one shows a six aa substitution for aa 351-570, while a second shows a 45 aa substitution for aa 302-579 (12, 13). The soluble receptor isoforms appear to be inhibitory to IL-1 signaling. 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 (14). The human and mouse IL-1 RAcP precursors are 89% aa identical; within the extracellular region, they share 86% aa identity.
Subramaniam, S. et al. (2004) Dev. Comp. Immunol. 28:415.
Boraschi, D. and A. Tagliabue (2006) Vitam. Horm. 74:229.
Dunne, A. and L.A.J. O'Neill (2003) Sci STKE. Feb 25;2003(171):re3.
Huang, J. et al. (1997) Proc. Natl. Acad. Sci. USA 94:12829.
Greenfeder, S. A. et al. (1995) J. Biol. Chem. 270:13757.
Brikos, C. et al. (2007) Mol. Cell. Proteomics 6:1551.
Chackerian, A.A. et al. (2007) J. Immunol. 179:2551.
Lang, D. et al. (1998) J. Immunol. 161:6871.
SwissProt. Accession # Q9NPH3.
Yoon, D-Y. and C.A. Dinarello (1998) J. Immunol. 160:3170.
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.
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