Recombinant Cynomolgus IL13 protein(Ser21-Asn132), His-tagged
Cat.No. : | IL13-373C |
Product Overview : | Recombinant Cynomolgus IL-13 (ABG75889.1) (Ser 21-Asn 132) was expressed in HEK293, fused with a polyhistidine tag at the N-terminus. |
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Species : | Cynomolgus |
Source : | HEK293 |
Tag : | His |
Protein Length : | 21-132 a.a. |
Form : | Lyophilized from sterile PBS, pH 7.4. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization. |
Bio-activity : | 1. Measured by its binding ability in a functional ELISA. Immobilized cynomolgus IL-13 at 4 μg/ml (100 μl/well) can bind human IL13RA1 with a linear range of 0.156-2.5 μg/ml. 2. Measured in a cell proliferation assay using TF1 human erythroleukemic cells. The ED50 for this effect is typically 100-400 ng/mL. |
Molecular Mass : | The recombinant cynomolgus IL13 consists of 128 amino acids and has a calculated molecular mass of 14.5 kDa. The apparent molecular mass of the protein is approximately 25-35 kDa in SDS-PAGE under reducing conditions. |
Endotoxin : | < 1.0 EU per μg of the protein as determined by the LAL method |
Purity : | > 95 % as determined by SDS-PAGE |
Storage : | Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles. |
Reconstitution : | It is recommended that sterile water be added to the vial to prepare a stock solution of 0.2 ug/ul. Centrifuge the vial at 4°C before opening to recover the entire contents. |
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Case 1: Okamoto H, et al. Sci Rep. 2019
Malignant melanoma is a particularly challenging cancer to treat, with traditional therapies like chemotherapy proving largely ineffective. This highlights the urgent need for new therapeutic targets to combat melanoma. Interleukin-13 receptor α2 (IL13Rα2) is overexpressed in several cancers, including glioma and pancreatic cancer, and is suspected to play a role in cancer progression. However, its specific impact on malignant melanoma has been unclear. This study found that IL13Rα2 is expressed in about 7.5% of melanoma patients. Interestingly, while IL13Rα2 reduced proliferation in human melanoma cells in vitro, it enhanced tumor growth and angiogenesis in a melanoma xenograft mouse model. Here a correlation between IL13Rα2 expression and amphiregulin, an epidermal growth factor, in melanoma cells and clinical samples. The expression of amphiregulin was found to promote tumor growth, suggesting a direct link between IL13Rα2 and amphiregulin in melanoma progression.

Fig1. The expression of IL13Rα2 in the SK-MEL-28, SK-IL13Rα2 and A375 (IL13Rα2-positive) cells was determined by qRT-PCR.

Fig2. The expression of IL13Rα2 in A375-Control and A375-IL13RA2 KO cells.
Case 2: Li S, et al. Nat Commun. 2023
Neuronal expression of immune system molecules like IL-13 and its receptor IL-13Ra1 has been identified in the brains of mice, rats, and humans. These molecules, when engaged, enhance the phosphorylation of NMDAR and AMPAR subunits, boosting synaptic activity and CREB-mediated transcription. This research indicates that elevated IL-13 levels are a characteristic of traumatic brain injury (TBI) in male mice and in human patient cohorts, and that this upregulation appears to protect neurons from excitotoxicity. IL-13's increase is observed in various human brain samples and cerebrospinal fluid, suggesting it plays a role in synaptic physiology and neuronal survival post-injury. This finding implies that IL-13's neuroprotective effects could be a potential target for therapeutic interventions in TBI pathophysiology.

Fig1. Volcanoplot and list of proteins showing significant change in their phosphorylation 1 h after neurons were exposed to IL-13 or control.

Fig2. High dose IL-13 does not prevent to glutamate induced neuronal toxicity.
Recombinant Cynomolgus IL13 protein, or interleukin-13, is a vital molecule in the field of biomedical research and has a broad range of applications. It plays a significant role in immune regulation and allergy research, being a key cytokine in allergic reactions and a crucial tool in understanding immune response mechanisms. This protein is also gaining attention in cancer research, as certain cancers leverage IL-13 pathways to promote tumor growth and evade immune responses, making it a potential target for developing new therapeutics. In drug development, IL-13 is a promising target for antibody drugs to treat diseases like asthma, and it is used in the screening of new anti-inflammatory drugs. Additionally, IL-13 levels serve as a biomarker for diagnosing inflammatory diseases and studying cellular signaling pathways, such as the STAT6 pathway, which is important for revealing how cells regulate and respond to various stimuli.
In essence, the versatility of recombinant Cynomolgus IL13 protein makes it an important asset in scientific research and clinical applications, with implications in immune response, allergy management, cancer treatment, drug development, and diagnostic tools. Its diverse roles highlight the potential for IL-13 to impact various aspects of human health and disease.

Fig1. Therapeutic strategies based on IL13Rα2. (Marta Jaén, 2022)
Not For Human Consumption!
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