IL5 Canine

Interleukin-5 (IL-5) is a cytokine, a type of signaling molecule that plays a crucial role in the immune system. It is primarily produced by T lymphocytes, eosinophils, and mast cells. IL-5 is involved in the regulation of eosinophils, which are white blood cells that play a key role in the body’s response to allergens and infections. The recombinant form of canine IL-5 is a laboratory-produced version of this cytokine, designed to mimic its natural counterpart in dogs.

Canine IL-5 is synthesized as a 134 amino acid precursor, which includes a 21 amino acid signal sequence and a 113 amino acid mature segment . The recombinant form is typically produced in various expression systems, such as mouse myeloma cell lines (NS0-derived), HEK293 cells, or Sf9 Baculovirus cells . The recombinant protein is often tagged with a His-tag at the C-terminus to facilitate purification .

IL-5 functions as a homodimer, meaning it forms a complex with two identical molecules linked together. This cytokine is crucial for the growth, differentiation, and activation of eosinophils. It binds to the IL-5 receptor on the surface of eosinophils, triggering a cascade of intracellular signals that promote the survival and activation of these cells .

Recombinant canine IL-5 is used in various research applications, including:

• Cell Proliferation Assays: It is used to measure the proliferation of cells, particularly in studies involving eosinophils.
• ELISA and Western Blot: These techniques are used to detect and quantify IL-5 in biological samples .
• Disease Models: IL-5 is studied in the context of diseases such as asthma, allergies, and gastrointestinal disorders, where eosinophils play a significant role .

Recombinant canine IL-5 is typically lyophilized and stored at -20°C to -80°C. Upon reconstitution, it should be stored at -20°C to -70°C under sterile conditions to maintain its stability and activity . It is essential to avoid repeated freeze-thaw cycles to prevent degradation of the protein.