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Recombinant Mouse IL-11 Protein, CF

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Recombinant Mouse IL-11 Protein (Catalog # 11585-IL) stimulates T11 mouse plasmacytoma cell proliferation. The ED50 for this effect is less than 0.750 ng/mL.
2 μg/lane of Recombinant Mouse IL‑11 Protein (Catalog # 11585-IL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 20 ...read more

Product Details

Summary
Reactivity MuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Mouse IL-11 Protein, CF Summary

Details of Functionality
Measured in a cell proliferation assay using T11 mouse plasmacytoma cells. Nordan, R.P. et al. (1987) J. Immunol. 139:813. The ED50 for this effect is less than 0.750 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived mouse IL-11 protein
Pro22-Leu199
Accession #
N-terminal Sequence
Pro22
Protein/Peptide Type
Recombinant Proteins
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
19.
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
20 kDa, under reducing conditions.

Packaging, Storage & Formulations

Storage
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 and EDTA with Trehalose.
Reconstitution Instructions
Reconstitute the 20 μg size at 200 μg/mL in PBS. Reconstitute all other sizes at 500 μg/mL in PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse IL-11 Protein, CF

  • Adipogenesis inhibitory factor
  • AGIF
  • AGIFoprelvekin
  • IL11
  • IL-11
  • IL-11Oprelvekin
  • interleukin 11
  • interleukin-11
  • Oprelvekin

Background

IL-11 (Interleukin 11) is a pleiotropic cytokine in the IL-6 family, which also includes LIF, CNTF, Oncostatin M, Cardiotrophin-1, IL-27 and IL-31 (1-4). In humans, IL-11 was also independently discovered as an adipogenesis inhibitory factor (AGIF) (3). The mouse IL-11 cDNA encodes a 199 amino acid (aa) precursor, which generates a 178 aa, 19 kDa mature unglycosylated protein. Mature mouse IL-11 shares 88%, 97%, and 89% aa sequence identity with human, rat and canine IL-11, respectively. IL-11 is secreted by osteoblasts, synoviocytes, fibroblasts, chondrocytes, intestinal myofibroblasts, and trophoblasts, among other cell types (1). It is found in the plasma mainly during inflammation, such as that associated with viral infection, cancer, or inflammatory arthritis, and is considered to be primarily anti‑inflammatory (1). It stimulates hematopoiesis and thrombopoiesis, regulates macrophage differentiation, and confers mucosal protection in the intestine (1). It has also been found to enhance T cell polarization toward Th2, promote B cell IgG production, increase osteoclast bone absorption, protect endothelial cells from oxidative stress, and regulate epithelial proliferation and apoptosis (1). IL-11 synergizes with several other cytokines to produce these effects, and its effects overlap with those of IL-6 (1). IL-11 receptor activation requires formation of a complex of two IL-11 molecules with two molecules of the ligand-binding IL-11 R alpha subunit and two molecules of the ubiquitously expressed cell signaling beta subunit, gp130 (5). A soluble form of IL-11 R alpha can bind IL-11 and either form a signaling complex with gp130 on the cell surface, or inhibit cell surface IL-11 R alpha /gp130 signaling (6-8).

  1. Putoczki, T. and M. Ernst (2010) J. Leukoc. Biol. 88:1109.
  2. Paul, S.R. et al. (1990) Proc. Natl. Acad. Sci. USA 87:7512.
  3. Kawashima, I. et al. (1991) FEBS Lett. 283:199.
  4. Morris, J.C. et al. (1996) Exp. Hematol. 24:1369.
  5. Barton, V.A. et al. (2000) J. Biol. Chem. 275:36197.
  6. Curtis, D.J. et al. (1997) Blood 90:4403.
  7. Baumann, H. et al. (1996) J. Immunol. 157:284.
  8. Karow, J. et al. (1996) Biochem. J. 318:489.

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