Recombinant human IL-11 protein - Bioactive cytokine

Human IL-11 protein - Mammalian cell-expressed, tag-free, carrier-free

Recombinant human IL-11 is a high-quality and biologically active cytokine, validated using proprietary IL-11 reporter cells (see figure). This gp130 cytokine receptor family member is produced in CHO cells to ensure protein glycosylation and bona fide 3D structure.

Recombinant human IL-11 can be used together with HEK-Blue™ IL-11 cells for the screening of inhibitory molecules, such as therapeutic monoclonal antibodies targeting IL-11 signaling.

IL-11 signaling and biological functions

Key features

• Each lot is validated using HEK-Blue™ IL-11 cells
• Endotoxin ≤ 0.1 EU/µg
• 0.2 µm sterile-filtered

Applications

• Standard for IL-11 detection and quantification
• Screening and release assays for antibodies blocking IL-11 signaling
• Screening and release assays for engineered IL-11

Interleukin-11 (IL-11) is a member of the IL-6-type cytokine family, known for its diverse roles in hematopoiesis, bone remodeling, and modulation of inflammatory responses. It is upregulated in a variety of fibro-inflammatory diseases such as systemic sclerosis, rheumatoid arthritis, pulmonary fibrosis, and inflammatory bowel disease. Moreover, IL-11 has emerged as a potential therapeutic target in fibrotic diseases and certain cancers. 

 More details

All InvivoGen products are for internal research use only and not for human or veterinary use.

Figures

SDS-PAGE analysis of the recombinant human (h)IL-11 protein. 2 μg of hIL-11 was loaded on a 12% Mini-PROTEAN® TGX Stain-Free™ Precast Gel (Bio-Rad). Detection was performed as per the manufacturer’s instructions. A band was detected at ~18 kDa.

Dose-response of HEK-Blue™ IL-11 cells to recombinant human IL-11. HEK-Blue™ IL-11 cells (cat code: hkb-hil11r) were stimulated with increasing concentrations of recombinant human IL-11. After overnight incubation, the STAT3-induced SEAP activity was determined using QUANTI-Blue™ Solution, a SEAP detection reagent. Data are shown as optical density (OD) at 650 nm (mean ± SEM).

Specifications

Source: Chinese hamster ovary (CHO) cells

Species: Human

Carrier: Carrier-free

Tag: Tag-free

Accession number: P20809-1

Protein size (predicted): 178 a.a. (P22-L199)

Molecular weight: ~ 18 kDa (SDS-PAGE)

Solubility: 100 μg/ml in water

Formulation: Phosphate buffer saline (pH 7.4), 5% saccharose

Form:  Lyophilized

Reconstitution buffer:  Endotoxin-free water (provided)

Purity:  ≥95% (SDS-PAGE)

Endotoxin: ≤ 0.1 EU/μg (measurement by kinetic chromogenic LAL assay)

Tested applications:  Cellular assays

Quality control: Each lot is functionally tested and validated.

Contents

Recombinant human IL-11 is provided lyophilized and is available in two quantities:

• rcyc-hil11: 10 µg
• rcyc-hil11-5: 5 x 10 µg (50 µg)
• 1.5 ml endotoxin-free water for rcyc-hil11 and rcyc-hil11-5

 Recombinant hIL-11 is shipped at room temperature.

 Upon receipt, the product should be stored at -20°C.

 Avoid repeated freeze-thaw cycles.

Details

IL-11 background

Interleukin‑11 (IL‑11) belongs to the IL‑6 cytokine family, which includes Oncostatin M (OSM), IL‑6, ciliary neurotrophic factor (CNTF), leukemia inhibitory factor (LIF), cardiotrophin‑1 (CT‑1), IL‑31, and IL‑27. These cytokines primarily function by binding to specific alpha receptors - sometimes shared among family members - which then associate with the common gp130 co-receptor to trigger intracellular signaling, mainly through the canonical JAK/STAT pathway [1].

While IL‑11 was traditionally regarded as anti-fibrotic, anti-inflammatory, and pro-regenerative, recent studies have challenged this view. Newer studies highlight IL‑11 as a driver of fibrosis, inflammation, and impaired tissue regeneration [1,2].

The profibrotic role of IL‑11 was first identified in 2017 by Schafer and colleagues, who demonstrated that IL-11 mediates the pro-fibrotic effect of TGF-β1, the prototypic profibrotic cytokine [3-4]. Now, IL‑11 is recognized as a key downstream mediator of TGF‑β signaling, promoting fibrosis through ERK pathway activation in stromal cells. This profibrotic activity is implicated in a range of disorders, including pulmonary, cardiac, and hepatic fibrosis [3]. These discoveries have made IL‑11 a promising therapeutic target for fibrotic diseases, with the potential to halt or even reverse tissue fibrosis. Therapeutic approaches under investigation include monoclonal antibodies directed against IL‑11 itself or its receptor [3]. 

Moreover, IL‑11 has also emerged as a key player in cancer biology, particularly in shaping the tumor microenvironment. Targeting IL‑11 or its receptor may not only limit fibrotic remodeling but also improve anti-tumor immune responses, particularly in combination with immune checkpoint inhibitors like anti‑PD‑1 antibody [1,5]. These advances highlight IL‑11 as a compelling candidate for therapeutic intervention in both fibrotic and oncologic settings.

References:

1. Cook SA., 2023. Understanding interleukin 11 as a disease gene and therapeutic target. Biochem J.480(23):1987-2008.
2. Fung KY, et al., 2022. Emerging roles for IL-11 in inflammatory diseases. Cytokine. 149:155750.
3. O'Reilly S., 2023. Interleukin-11 and its eminent role in tissue fibrosis: a possible therapeutic target. Clin Exp Immunol. 214(2):154-161.
4. Schafer S, et al., 2017. IL-11 is a crucial determinant of cardiovascular fibrosis. Nature. 552(7683):110-115.
5. Zhang C, et al. 2025. IL-11/IL-11R signal inhibition by 9MW3811 remodels the immune tumor microenvironment and enhances anti-tumor efficacy of PD-1 blockade. NPJ Precis Oncol. 9(1):138.