Recombinant Mouse IL-36 beta /IL-1F8 (aa 31‑183) (Catalog # 7060-ML/CF) induces IL-6 secretion in the NIH‑3T3 mouse embryonic fibroblast cell line. The ED50 for this effect is 1-6 ng/mL.
1 µg/lane of Recombinant Mouse IL‑36 beta /IL‑1F8 (aa 31-183) was resolved with SDS-PAGE under reducing (R) conditions and visualized by silver staining, showing a single band at 16 kDa.
Measured by its ability to induce IL-6 secretion by NIH‑3T3 mouse embryonic fibroblast cells. Towne, J.E. et al. (2004) J. Biol. Chem. 279:13677. The ED50 for this effect is 1-6 ng/mL.
Source
E. coli-derived mouse IL-36 beta/IL-1F8 protein Ser31-Lys183
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
17.4 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
16 kDa, reducing conditions
Publications
Read Publication using 7060-ML/CF in the following applications:
Mouse interleukin‑36 beta [IL-36 beta ; previously IL‑1F8, FIL‑1 eta (eta) and IL‑1H2] is a member of the IL‑1 family of proteins that includes IL‑1 beta , IL‑1 alpha , IL‑1ra, IL‑18, IL‑36Ra/IL‑1F5, IL‑36 alpha /IL‑1F6, IL‑37/IL‑1F7, IL‑36 gamma /IL‑1F9 and IL‑1F10 (1 ‑ 6). All family members show a 12 beta ‑stranded beta ‑trefoil configuration, share up to 50% amino acid (aa) sequence identity, and are believed to have arisen from a common ancestral gene (3, 4). Although two alternatively spliced transcript variants for human IL‑36 beta /IL‑1F8 have been described, to date, only one mouse IL‑36 beta /IL‑1F8 isoform is known (3). Mouse IL‑36 beta /IL‑1F8 is synthesized as a 183 amino acid (aa) protein that contains no signal sequence, no prosegment and no potential N‑linked glycosylation site(s) (1, 2). Mouse IL‑36 beta /IL‑1F8 shares 61% and 74% aa identity with human IL‑36 beta isoform 2 and rat IL‑36 beta , respectively. IL‑36 beta is agonistic, stimulating release of inflammatory mediators such as IL‑6 and IL‑8, and cytotoxic peptides such as beta-defensins 2 and 3 that aid in defense against microbial pathogens (7‑10). The receptor for IL-36 proteins is IL‑1 Rrp2, with IL‑1 RAcP as a coreceptor (7, 9). Antagonism of IL‑36 proteins by IL‑36Ra, which also binds IL‑1 Rrp2, has been shown by some investigators (5, 6). Skin keratinocytes express highest levels of IL‑36 proteins and their receptors, followed by epithelia in the esophagus, trachea and bronchae (7 ‑ 9). IL‑36 beta expression is increased in psoriatic skin and may play a role in pathogenesis of psoriasis (7, 8). IL‑36 beta is also expressed in resting and activated monocytes and B cells, synovial fibroblasts, neurons and glia, and is detectable in plasma and body fluids (1, 7, 9, 11). IL‑36 beta , along with IL‑36 alpha and IL‑36 gamma , is up‑regulated by IL‑1 alpha and TNF‑ alpha in keratinocytes, and has been shown to activate NF‑ kappa B and MAPK signaling pathways in an IL‑1 Rrp2‑dependent manner (7‑9). Full‑length recombinant IL‑36 proteins appear less active than their endogenous counterparts, but trimming of the N‑termini enhances their activity (9, 12).
Smith, D.E. et al. (2000) J. Biol. Chem. 275:1169.
Kumar, S. et al. (2000) J. Biol. Chem. 275:10308.
Nicklin, M.J.H. et al. (2002) Genomics 79:718.
Dunn, E. et al. (2001) Trends Immunol. 22:533.
Dinarello, C. et al. (2010) Nat. Immunol. 11:973.
Barksby, H.E. et al. (2007) Clin. Exp. Immunol. 149:217.
Towne, J.E. et al. (2004) J. Biol. Chem. 279:13677.
Johnston, A. et al. (2011) J. Immunol. 186:2613.
Magne, D. et al. (2005) Arthritis Res. Ther. 8:R80.
van Asseldonk, E.J.P. et al. (2010) Obesity 18:2234.
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