Recombinant Mouse IL-11 (carrier-free)

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Regulatory Status
RUO
Other Names
Adipogenesis Inhibitory Factor (AGIF)
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IL-11_CF_Mouse_RECOM_BA_031716
Dose-dependent proliferation in 7TD1 cells.
  • IL-11_CF_Mouse_RECOM_BA_031716
    Dose-dependent proliferation in 7TD1 cells.
Cat # Size Price Save
756102 10 µg ¥43,390
756104 25 µg ¥80,600
Description

IL-11, a member of IL6 family of cytokines, exerts a wide range of biological effects on various cell types including hematopoietic cells, hepatocytes, adipocytes, neurons, and osteoblasts. IL-11 works synergistically with other growth factors, which include SCF, IL-4, IL-3, IL-7, IL-12, IL-13, and GM-CSF to stimulate the proliferation of cells from several hematopoietic lineages. The binding of IL-11 to IL-11 receptor (IL-11R) induces membrane bound gp130 homodimerization and triggers STAT3 phosphorylation by JAK. IL-11 shares the common receptor subunit gp130 with IL-6, IL-27, LIF, OSM, CNTF, CT-1, CLC, and NP. Female mice deficient in the IL-11R revealed an important role for IL-11 in embryonic implantation. Additionally, IL-11 shows anti-inflammatory activity in models of inflammatory bowel disease, chemotherapy induced oral mucositis, and inflammatory arthritis. IL-11 and IL-13 are highly expressed in asthmatic airways (Th2 response), and IL-11 can inhibit Th1 responses and inhibits the production of Th1 cytokines such as IL-12 and shifts inflammation in the Th2 direction. Elevated IL-11 expression is associated with tumor grade and invasion in gastric cancer. Recombinant human IL-11 has been clinically approved to improve platelet recovery after chemotherapy-induced thrombocytopenia.

Product Details
Technical data sheet

Product Details

Source
Mouse IL-11, 180 amino acids (Val20-Leu199) (Accession# P47873), was expressed in 293E cells.
Molecular Mass
The 180 amino acid recombinant protein has a predicted molecular mass of approximately 19.3 kD. The DTT-reduced and non-reduced protein migrates at approximately 19.3 kD by SDS-PAGE. The N-terminal amino acid is Valine.
Purity
>98%, as determined by Coomassie stained SDS-PAGE.
Formulation
Sterile-filtered with 0.2 µm filter, solution is comprised of 10 mM Sodium succinate, 4% mannitol, and in pH 5.0.
Endotoxin Level
Less than 0.1 ng per µg cytokine as determined by the LAL method.
Concentration
10 - 100 µg sizes are bottled at 200 µg/mL.
Storage & Handling
Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at -20°C for up to six months, or at -70°C or colder until the expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C or colder. Stock solutions can also be prepared at 50 - 100 µg/mL in appropriate sterile buffer, carrier protein such as 0.2 - 1% BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to one week and stored at -20°C or colder for up to 3 months. Avoid repeated freeze/thaw cycles.
Activity
The ED50 = 4.0 - 12 ng/ml, corresponding to a specific activity of 0.83-2.5 x 105 units/mg, as determined by a dose-dependent stimulation of 7TD1 cells proliferation.
Application

Bioassay

Application Notes

BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue-ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are verified in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at tech@biolegend.com.

Antigen Details

Structure
"Four-helix bundle" protein fold similar to IL-6.
Distribution
IL-11 can be secreted by various cell types that include epithelial, endothelial, keratinocytes, stromal, neuronal, fibroblasts, osteoclasts, and bone marrow stromal cells.
Function
IL-11 is a multifunctional cytokine that plays important roles in hemopoiesis, thrombopoiesis, megakaryocytopoiesis, and bone resorption. It regulates macrophage differentiation and confers mucosal protection after chemotherapy and radiation therapy. IL-11 expression can also be up-regulated by oncogenic Ras or respiratory virus infections. Also, IL-11 and IL-11Rα are induced by IL-13.
Interaction
Hematopoietic cells, hepatocytes, adipocytes, neurons, osteoblasts, fibroblasts, and gastrointestinal epithelial cells.
Ligand/Receptor
Membrane bound or soluble IL-11Rα heterodimerize with gp130.
Cell Type
Hematopoietic stem and progenitors
Biology Area
Cell Biology, Cell Motility/Cytoskeleton/Structure, Immunology, Stem Cells
Molecular Family
Cytokines/Chemokines
Antigen References

1. Putoczki T, Ernst M. 2010. J. Leuko. Biol. 6:1109-17.
2. Wilde MI, Faulds D. 1998. BioDrugs 10:159-71.
3. Barton VA. 2000. J. Biol. Chem. 2000. 275:36197-203.
4. Robb L, et al. 1998. Nat. Med. 4:303-8.
5. Lemoli RM, et al. 1995. Br. J. Haematol. 91:319-26.
6. Elias JA, et al. 1994. J. Biol. Chem. 269:22261-8.
7. Chen Q, et al. 2005. J. Immunol. 4:2305-13.
8. Howlett M, et al. 2012. Gut 10:1398-409.
9. Dams-Kozlowska H, et al. 2012. BMC Biotechnology 12:8.

Gene ID
16156 View all products for this Gene ID
UniProt
View information about IL-11 on UniProt.org

Related FAQs

Why choose BioLegend recombinant proteins?

     • Each lot of product is quality-tested for bioactivity as indicated on the data sheet.
     • Greater than 95% Purity or higher, tested on every lot of product.
     • 100% Satisfaction Guarantee for quality performance, stability, and consistency.
     • Ready-to-use liquid format saves time and reduces challenges associated with reconstitution.
     • Bulk and customization available. Contact us.
     • Learn more about our Recombinant Proteins.

How does the activity of your recombinant proteins compare to competitors?

We quality control each and every lot of recombinant protein. Not only do we check its bioactivity, but we also compare it against other commercially available recombinant proteins. We make sure each recombinant protein’s activity is at least as good as or better than the competition’s. In order to provide you with the best possible product, we ensure that our testing process is rigorous and thorough. If you’re curious and eager to make the switch to BioLegend recombinants, contact your sales representative today!

What is the specific activity or ED50 of my recombinant protein?

The specific activity range of the protein is indicated on the product datasheets. Because the exact activity values on a per unit basis can largely fluctuate depending on a number of factors, including the nature of the assay, cell density, age of cells/passage number, culture media used, and end user technique, the specific activity is best defined as a range and we guarantee the specific activity of all our lots will be within the range indicated on the datasheet. Please note this only applies to recombinants labeled for use in bioassays. ELISA standard recombinant proteins are not recommended for bioassay usage as they are not tested for these applications.

Have your recombinants been tested for stability?

Our testing shows that the recombinant proteins are able to withstand room temperature for a week without losing activity. In addition the recombinant proteins were also found to withstand four cycles of freeze and thaw without losing activity.

Does specific activity of a recombinant protein vary between lots?

Specific activity will vary for each lot and for the type of experiment that is done to validate it, but all passed lots will have activity within the established ED50 range for the product and we guarantee that our products will have lot-to-lot consistency. Please conduct an experiment-specific validation to find the optimal ED50 for your system.

How do you convert activity as an ED50 in ng/ml to a specific activity in Units/mg?

Use formula Specific activity (Units/mg) = 10^6/ ED50 (ng/mL)

Go To Top Version: 1    Revision Date: 03/18/2016

For Research Use Only. Not for diagnostic or therapeutic use.

 

This product is supplied subject to the terms and conditions, including the limited license, located at www.biolegend.com/terms) ("Terms") and may be used only as provided in the Terms. Without limiting the foregoing, BioLegend products may not be used for any Commercial Purpose as defined in the Terms, resold in any form, used in manufacturing, or reverse engineered, sequenced, or otherwise studied or used to learn its design or composition without express written approval of BioLegend. Regardless of the information given in this document, user is solely responsible for determining any license requirements necessary for user’s intended use and assumes all risk and liability arising from use of the product. BioLegend is not responsible for patent infringement or any other risks or liabilities whatsoever resulting from the use of its products.

 

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