Interleukin 11 (IL-11) is a multifunctional cytokine isolated from bone marrow-derived stromal cells. It is a key regulator of multiple events in hemtaopoiesis, most notably the stimulation of megakaryocyte maturation.1 It is also known under the names Adipogenesis inhibitory factor (AGIF)2 and Oprelvekin. IL-11 improves platelet recovery after chemotherapy-induced thrombocytopenia, induces acute phase proteins, modulates antigen-antibody responses, participate in the regulation of bone cell proliferation and differentiation and could be use as a therapeutic for osteoporosis. Besides from lymphopoietic/hematopoietic and osteotrophic properties, it has functions in many tissues such as brain, gut and testis.
The predicted molecular weight of Recombinant Mouse IL-11 is Mr 19 kDa.
Predicted Molecular Mass
19
Formulation
This recombinant protein was 0.2 µm filtered and lyophilized from modified Dulbecco’s phosphate buffered saline (1X PBS) and trehalose, pH 7.2 – 7.3 with no calcium, magnesium, or preservatives.
Storage and Stability
This lyophilized protein is stable for six to twelve months when stored desiccated at -20°C to -70°C. After aseptic reconstitution, this protein may be stored at 2°C to 8°C for one month or at -20°C to -70°C in a manual defrost freezer. Avoid Repeated Freeze Thaw Cycles. See Product Insert for exact lot specific storage instructions.
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Recombinant Mouse IL-11 is used in research applications to study its roles in hematopoiesis, immune modulation, tissue regeneration, fibrosis, and disease models, particularly because it is a key cytokine in mouse biology and enables species-specific, physiologically relevant experiments.
Key scientific reasons to use recombinant mouse IL-11 include:
Hematopoiesis and Thrombopoiesis: Mouse IL-11 stimulates the proliferation of hematopoietic stem cells and megakaryocytic progenitors, promotes megakaryocyte maturation, and increases platelet production, making it valuable for studies on blood cell development and recovery after myelosuppression.
Immune Regulation: IL-11 modulates macrophage differentiation and has immunoregulatory effects, which are relevant in inflammation, autoimmunity, and infection models.
Tissue Protection and Regeneration: IL-11 confers mucosal protection in the intestine and has been shown to protect against tissue injury in organs such as the liver, lung, and kidney in mouse models. It also regulates bone metabolism by acting on osteoblasts, osteoclasts, and mesenchymal stem cells.
Disease Modeling: Recombinant mouse IL-11 is essential for modeling diseases where IL-11 signaling is implicated, such as fibrosis, cancer, cardiovascular disease, and inflammatory disorders. Using the mouse version ensures accurate receptor binding and downstream signaling, avoiding the confounding effects seen when using human IL-11 in mice, which can act as a partial antagonist rather than a true agonist.
Species-Specific Activity: Recombinant mouse IL-11 is specifically required for mouse studies because human IL-11 does not fully activate mouse IL-11 receptors and may even block endogenous mouse IL-11 activity, leading to misleading results if used in mouse models.
Experimental Control: Using recombinant mouse IL-11 allows precise control over cytokine concentration and timing, enabling mechanistic studies of IL-11 signaling pathways and their physiological or pathological consequences.
In summary, recombinant mouse IL-11 is critical for mechanistic and translational studies in mice, ensuring species-appropriate receptor activation and reliable modeling of IL-11’s biological functions in hematopoiesis, immunity, tissue repair, and disease.
Yes, recombinant Mouse IL-11 can be used as a standard for quantification or calibration in ELISA assays, provided it is of high purity and properly validated for this purpose. Recombinant IL-11 is commonly used as the standard in commercial Mouse IL-11 ELISA kits, which are designed to quantify both natural and recombinant forms of the cytokine in biological samples.
Key considerations for use:
Standard Preparation: The recombinant IL-11 should be reconstituted and diluted according to the ELISA kit protocol to generate a standard curve covering the expected concentration range in your samples.
Validation: Ensure the recombinant protein matches the mature, full-length mouse IL-11 sequence used in the kit standards, as sequence or glycosylation differences can affect antibody recognition and quantification accuracy.
Purity and Activity: The recombinant standard should be highly purified and biologically active, as impurities or degradation can impact quantification.
Matrix Effects: Dilute the standard in the same buffer or matrix as your samples (e.g., sample diluent provided with the kit) to minimize matrix effects and ensure accurate calibration.
Kit Compatibility: Most ELISA kits specify that both natural and recombinant mouse IL-11 are recognized and quantified equivalently, but always confirm this in the kit documentation for your specific assay.
Limitations:
Bioassay vs. ELISA: Some recombinant proteins are specifically formulated for use as ELISA standards and may not be suitable for bioactivity assays due to lack of functional validation.
Storage and Handling: Prepare fresh standard dilutions for each assay, as working solutions may not be stable over time.
Summary Table: Recombinant Mouse IL-11 as ELISA Standard
Application
Requirement
Notes
ELISA calibration
High purity, validated sequence
Used in commercial kits
Standard curve
Prepare fresh, follow kit protocol
Discard unused dilutions
Matrix compatibility
Dilute in sample diluent or matching buffer
Minimizes matrix effects
Bioactivity assays
Not always suitable
Check product specifications
In summary: Recombinant Mouse IL-11 is widely accepted as a standard for ELISA quantification, provided it is properly prepared and validated for your assay system.
Recombinant Mouse IL-11 has been validated in published research for a range of applications, primarily in cell culture, bioassays, and functional studies involving hematopoiesis, immunology, neurobiology, and tissue injury models.
Key validated applications include:
Cell Culture Supplementation: Used to stimulate hematopoietic stem cell and megakaryocyte progenitor proliferation, megakaryocyte maturation, and platelet production in vitro.
Bioassays: Extensively used in functional assays to study:
Hematopoiesis and thrombopoiesis.
Macrophage differentiation and T cell polarization (notably Th2 and Th17 responses).
B cell IgG production and osteoclast activity.
Endothelial and epithelial cell protection and proliferation.
Oligodendrocyte survival, maturation, and myelin formation in neurobiology models.
Mast cell growth in fibroblast-dependent pathways.
In Vivo Administration: Validated in mouse models for:
Modulating immune responses in autoimmune encephalomyelitis (EAE) and multiple sclerosis models.
Inducing or protecting against tissue injury (e.g., liver, lung, kidney, heart) depending on context and species specificity.
Promoting or inhibiting fibrosis and tissue regeneration.
Modulating inflammatory responses in colitis, arthritis, and other disease models.
Functional Studies: Used in studies of signaling pathways (e.g., Jak/Stat, Smad1), cell differentiation, and lineage tracing in hematopoietic and neural systems.
Cancer Research: Investigated for its role in tumor growth, stromal activation, and as a target for anti-cancer therapies.
Aging and Regeneration: Targeting IL-11 signaling has been explored for effects on aging, healthspan, and tissue regeneration.
Experimental formats validated in the literature:
In vitro cell-based assays (proliferation, differentiation, survival)
In vivo mouse models (systemic administration, disease induction)
Note: The specific use of recombinant mouse IL-11 should be matched to the experimental system and species, as cross-species effects (e.g., human IL-11 in mouse models) can yield different or even opposing biological outcomes due to receptor specificity.
To reconstitute and prepare Recombinant Mouse IL-11 protein for cell culture experiments, dissolve the lyophilized protein in sterile, deionized water at a concentration of 100 μg/mL (0.1 mg/mL) and then dilute further in appropriate cell culture buffer or medium as needed for your assay.
Essential protocol steps:
Centrifuge the vial briefly before opening to ensure all lyophilized material is at the bottom.
Add sterile, deionized water (or PBS if specified by the manufacturer) to achieve the recommended stock concentration (typically 100 μg/mL).
Gently pipette or vortex to fully dissolve the protein, avoiding vigorous agitation or foaming.
If required, add carrier protein (e.g., 0.1–1% BSA or HSA) to the buffer for improved stability, especially for low concentration working solutions.
Aliquot the stock solution to avoid repeated freeze-thaw cycles, which can degrade the protein.
Store aliquots at −20 °C or −80 °C for long-term use; short-term storage at 2–8 °C is acceptable for up to 1 month.
For cell culture, dilute the stock solution into your culture medium to the desired final concentration immediately before use.
Additional considerations:
Use sterile technique throughout to prevent contamination.
If the protein is supplied with stabilizers (e.g., trehalose, mannitol, BSA), these do not need to be removed for cell culture applications.
Confirm the biological activity of your reconstituted protein using a relevant bioassay if necessary.
Avoid repeated freeze-thaw cycles by preparing single-use aliquots.
Summary Table: Preparation Steps
Step
Details
Centrifuge vial
Briefly spin to collect powder at bottom
Add water/PBS
Reconstitute at 100 μg/mL in sterile, deionized water or PBS
Mix gently
Pipette or vortex gently to dissolve
Add carrier protein
Optional: 0.1–1% BSA/HSA for stability in working solutions
Aliquot
Divide into single-use aliquots
Storage
−20 °C or −80 °C long-term; 2–8 °C short-term
Dilute for use
Prepare final working concentration in cell culture medium
Always consult the specific product datasheet for any unique instructions regarding buffer composition or reconstitution, as formulations may vary between suppliers.
References & Citations
1. Williams, DA. et al. (1990) Proc. Natl. Acad. Sci. USA87: 7512
2. Takiguchi, Y. et al. (1991) FEBS Lett.283: 199