Recombinant Mouse ST2/IL-33R Fc Chimera Protein, CF Summary
Details of Functionality
Measured by its ability to bind Recombinant Mouse IL‑33 (Catalog # 3626-ML) in a functional ELISA with an estimated KD < 50 nM. Schmitz, J. et al. (2005) Immunity 23:479.
Source
Spodoptera frugiperda, Sf 21 (baculovirus)-derived mouse ST2/IL-33R protein
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
63 kDa (monomer). 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
73 kDa, reducing conditions
Publications
Read Publications using 1004-MR in the following applications:
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.
Purity
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Mouse ST2/IL-33R Fc Chimera Protein, CF
DER4
DER4ST2growth stimulation-expressed
Fit-1
IL-1 R4
IL1R4
IL-1R4
IL-1RL1
IL-33 R
IL33R
IL-33R
interleukin 1 receptor-like 1
interleukin 1 receptor-related protein
interleukin-1 receptor-like 1
Ly84
MGC32623
Protein ST2
ST2
ST2L
ST2V
T1
T1homolog of mouse growth stimulation-expressed
Background
ST2, also known as IL-1 R4 and T1, is an Interleukin-1 receptor family glycoprotein that contributes to Th2 immune responses (1, 2). Mouse ST2 consists of a 306 amino acid (aa) extracellular domain (ECD) with three Ig-like domains, a 23 aa transmembrane segment, and a 212 aa cytoplasmic domain with an intracellular TIR domain (3). Alternate splicing of the 120 kDa mouse ST2 generates a soluble 60 kDa isoform that lacks the transmembrane and cytoplasmic regions (3). Within the ECD, mouse ST2 shares 68% and 81% aa sequence identity with human and rat ST2, respectively. ST2 is expressed on the surface of mast cells, activated Th2 cells, macrophages, and cardiac myocytes (4-7). It binds IL-33, a cytokine that is upregulated by inflammation or mechanical strain in smooth muscle cells, airway epithelia, keratinocytes, and cardiac fibroblasts (4, 8). IL-33 binding induces the association of ST2 with IL-1R AcP, a shared signaling subunit that also associates with IL-1 RI and IL-1 R rp2 (1, 9, 10). In macrophages, ST2 interferes with signaling from IL-1 RI and TLR4 by sequestering the adaptor proteins MyD88 and Mal (6). In addition to its role in promoting mast cell and Th2 dependent inflammation, ST2 activation enhances antigen induced hypernociception and protects from atherosclerosis and cardiac hypertrophy (4, 11-13). The soluble ST2 isoform is released by activated Th2 cells and strained cardiac myocytes and is elevated in the serum in allergic asthma (5, 7, 14). Soluble ST2 functions as a decoy receptor that blocks IL-33’s ability to signal through transmembrane ST2 (9, 12-14).
Barksby, H.E. et al. (2007) Clin. Exp. Immunol. 149:217.
Gadina, M. and C.A. Jefferies (2007) Science STKE 2007:pe31.
Yanagisawa, K. et al. (1993) FEBS Lett. 318:83.
Schmitz, J. et al. (2005) Immunity 23:479.
Lecart, S. et al. (2002) Eur. J. Immunol. 32:2979.
Brint, E.K. et al. (2004) Nat. Immunol. 5:373.
Weinberg, E.O. et al. (2002) Circulation 106:2961.
Sanada S. et al. (2007) J. Clin. Invest. 117:1538
Palmer, G. et al. (2008) Cytokine 42:358.
Chackerian, A.A. et al. (2007) J. Immunol. 179:2551.
Allakhverdi, Z. et al. (2007) J. Immunol. 179:2051.
Verri Jr., W.A. et al. (2008) Proc. Natl. Acad. Sci. 105:2723.
Miller, A.M. et al. (2008) J. Exp. Med. 205:339.
Hayakawa, H. et al. (2007) J. Biol. Chem. 282:26369.
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