Recombinant Human IL-36 gamma/IL-1F9 Protein, CF Summary
Details of Functionality
Measured by its binding ability in a functional ELISA. Immobilized recombinant human IL-36 gamma at 1 µg/mL (100 µL/well) can bind recombinant human IL-1 Rrp2 Fc Chimera (Catalog # 872-RP) with a linear range of 0.15 ‑ 5 µg/mL.
Source
E. coli-derived human IL-36 gamma/IL-1F9 protein Met1-Asp169
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<1.0 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
18.7 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.
Publications
Read Publications using 2320-IL/CF 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 Tris, NaCl and TCEP.
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 Human IL-36 gamma/IL-1F9 Protein, CF
IL-1 epsilon
IL-1 H1
IL-1 Related Protein 2
IL-1(EPSILON)
IL1E
IL-1-epsilon
IL1F9
IL-1F9
IL1H1
IL-1H1
IL-1-Related Protein 2
IL1RP2
IL-1rp2
IL36 gamma
IL-36 gamma
IL36G
interleukin 1 family, member 9
interleukin 1-related protein 2
Interleukin 36, Gamma
Interleukin-1 epsilon
interleukin-1 family member 9
Interleukin-1 homolog 1
Interleukin-36 Gamma
Background
Human interleukin 36 gamma (IL‑36 gamma ; formerly known as IL‑1F9, IL‑1 epsilon (epsilon) and IL‑1H1) is a secreted member of the IL‑1 family of proteins (1‑5). It currently is one of at least four IL‑1 family members that have been renamed, the others being IL‑36 alpha (formerly IL‑1F6), IL‑36 beta (formerly IL‑1F8) IL‑37 (formerly IL‑1F7) and IL‑36ra (formerly IL‑1F5) (1). All family members show a 12 beta ‑strand, beta ‑trefoil configuration, and all family members are believed to have arisen from a common ancestral gene that has undergone multiple duplications (6). IL‑36 gamma is synthesized as a 19 kDa, 169 amino acid (aa) protein that contains no signal sequence, no prosegment and no potential N‑linked glycosylation site(s) (3, 4, 7). The molecule is secreted via a nonclassical pathway and likely requires the presence of extracellular ATP (7, 8). Human to mouse, IL‑36 gamma shares 53% aa identity. Within the family, IL‑36 gamma shares 30% aa identity with IL‑1ra, and 23%, 33%, 57%, 35%, 45% and 32% aa identity with IL‑1 beta , IL‑36ra, IL‑36 alpha , IL‑37, IL‑36 beta and IL‑1F10, respectively. Cells reported to express IL‑36 gamma include Langerhans cells, keratinocytes, monocytes, bronchial epithelium plus Chief cells and Parietal cells of the stomach (6 ‑ 10). The receptor for IL‑36 alpha is reported to be a combination of IL‑1Rrp2 and IL‑1 RAcP (9). Recombinant IL‑136 gamma , along with IL‑36 alpha and IL‑36 beta , has been shown to act as an agonist by activating the pathway involving NF‑ kappa B and MAPK in an IL‑1Rrp2 dependent manner. This suggests that IL‑36 gamma may signal in similar fashion to IL‑1 and IL‑18 by having a binding receptor which, upon ligation, recruits a second receptor as a signaling component, forming an active heterodimeric receptor complex. Activities attributed to IL‑36 gamma include a down‑regulation of betacellulin, an up‑regulation of MMP‑9 and ‑10, and the activation of both macrophages and fibroblasts, resulting in the release of multiple chemokines such as CXCL1, 2, 3 and 8, plus CCL2, 3 and 20 (9 ‑ 11).
Dinarello, C. et al. (2010) Nat. Immunol. 11:973.
barksby, H.E. et al. (2007) Clin. Exp. Immunol. 149:217.
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.
Debets, R. et al. (2001) J. Immunol. 167:1440.
Johnston, A. et al. (2011) J. Immunol. 186:2613.
Chustz, R.T. et al. (2010) Am. J. Respir. Cell Mol. Biol. [Epub ahead of print].
Ramadas, R.A. et al. (2011) Am. J. Respir. Cell Mol. Biol. 44:134.
Towne, J.E. et al. (2004) J. Biol. Chem. 279:13677.
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