Product Specifications for Recombinant Human IL-11 (CHO-expressed) Protein, CF
Chinese Hamster Ovary cell line, CHO-derived human IL-11 protein Pro22-Leu199
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
N-terminal sequence Analysis
Predicted Molecular Mass
20-23 kDa, under reducing conditions.
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 0.02-0.12 ng/mL.
Scientific Data Examples for Recombinant Human IL-11 (CHO-expressed) Protein, CF
Recombinant Human IL-11 Protein Bioactivity Statement.
Measured in a cell proliferation assay using T11 mouse plasmacytoma cells. The ED50 for this effect is 0.02-0.12 ng/mL.
Recombinant Human IL-11 (CHO-expressed) Protein SDS-PAGE.
2 μg/lane of Recombinant Human IL-11 (CHO-expressed) Protein (Catalog # 10836-IL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 20-23 kDa.
Formulation, Preparation and Storage
What does CF mean?
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our
Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant
protein to be stored at a more dilute concentration.
The carrier free version does not contain BSA.
What formulation is right for me?
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or
as an ELISA standard.
In contrast, the carrier free protein is recommended for applications, in which the presence of BSA
Lyophilized from a 0.2 μm filtered solution in PBS and EDTA with Trehalose.
Reconstitute at 50-100 μg/mL in PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
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 (1-3). In humans, IL-11 was also independently discovered as an adipogenesis inhibitory factor (AGIF) (3). The human IL-11 cDNA encodes a 199 amino acid (aa) precursor, which generates a 178 aa, 19 kDa mature unglycosylated protein. Mature human IL-11 shares 88%, 88%, and 96% aa sequence identity with mouse, 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 (4). 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 (5-7).
Putoczki, T. and M. Ernst (2010) J. Leukoc. Biol. 88:1109.
Paul, S.R. et al. (1990) Proc. Natl. Acad. Sci. USA 87:7512.
Kawashima, I. et al. (1991) FEBS Lett. 283:199.
Barton, V.A. et al. (2000) J. Biol. Chem. 275:36197.
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