Recombinant Human IL-11 (CHO-expressed) Protein, CF

Catalog # Availability Size / Price Qty
10836-IL-010
10836-IL-050

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Recombinant Human IL‑11 Protein SEC-MALS.
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Recombinant Human IL-11 (CHO-expressed) Protein, CF Summary

Product Specifications

Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
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.
Source
Chinese Hamster Ovary cell line, CHO-derived human IL-11 protein
Pro22-Leu199
Accession #
N-terminal Sequence
Analysis
Pro22
Predicted Molecular Mass
19 kDa
SDS-PAGE
20-23 kDa, under reducing conditions.

Product Datasheets

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10836-IL

Carrier Free

What does CF mean?

CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. 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 could interfere.

10836-IL

Formulation Lyophilized from a 0.2 μm filtered solution in PBS and EDTA with Trehalose.
Reconstitution Reconstitute at  50-100 μg/mL in PBS.
Shipping 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.

Scientific Data

SEC-MALS View Larger

Recombinant Human IL-11 Protein (Catalog # 10836-IL) has a molecular weight (MW) of 18.1 kDa as analyzed by SEC-MALS, suggesting that this protein is a monomer. MW may differ from predicted MW due to post-translational modifications (PTMs) present (i.e. Glycosylation).

Bioactivity View Larger

Measured in a cell proliferation assay using T11 mouse plasmacytoma cells. The ED50 for this effect is 0.02-0.12 ng/mL.

SDS-PAGE View Larger

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.

Reconstitution Calculator

Reconstitution Calculator

The reconstitution calculator allows you to quickly calculate the volume of a reagent to reconstitute your vial. Simply enter the mass of reagent and the target concentration and the calculator will determine the rest.

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Background: IL-11

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).

References
  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. Barton, V.A. et al. (2000) J. Biol. Chem. 275:36197.
  5. Curtis, D.J. et al. (1997) Blood 90:4403.
  6. Baumann, H. et al. (1996) J. Immunol. 157:284.
  7. Karow, J. et al. (1996) Biochem. J. 318:489.
Long Name
Interleukin 11
Entrez Gene IDs
3589 (Human); 16156 (Mouse); 171040 (Rat); 102128313 (Cynomolgus Monkey)
Alternate Names
Adipogenesis inhibitory factor; AGIF; AGIFoprelvekin; IL11; IL-11; IL-11Oprelvekin; interleukin 11; interleukin-11; Oprelvekin

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