IL 1 alpha Mouse, His

The recombinant mouse IL-1α protein is typically produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain. This chain contains 179 amino acids and has a molecular mass of approximately 20.4 kDa . The protein is fused to a 23 amino acid His-tag at the N-terminus, which facilitates its purification through chromatographic techniques .

IL-1α exerts its effects by binding to specific cell surface receptors. It is known to stimulate thymocyte proliferation by inducing the release of IL-2, promote B-cell maturation and proliferation, and enhance fibroblast growth factor activity . Additionally, IL-1α is identified as an endogenous pyrogen, meaning it can induce fever by stimulating the release of prostaglandins .

Recombinant IL-1α is widely used in laboratory research to study its role in inflammation and immune responses. It is also utilized in various assays to investigate its effects on different cell types and to understand the signaling pathways it activates .

For optimal stability, the IL-1α protein solution should be stored at 4°C if it will be used within 2-4 weeks. For longer storage periods, it is recommended to freeze the solution at -20°C and add a carrier protein such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA) to prevent degradation . It is important to avoid multiple freeze-thaw cycles to maintain the protein’s integrity.

The recombinant IL-1α protein is typically formulated in a phosphate-buffered saline (PBS) solution with a pH of 7.4 and 10% glycerol . The purity of the protein is greater than 85% as determined by SDS-PAGE .

IL-1α is intended for laboratory research use only and is not suitable for use as a drug, agricultural or pesticidal product, food additive, or household chemical . Researchers handling this protein should follow appropriate safety protocols to ensure safe and effective use.

In summary, recombinant mouse IL-1α with a His-tag is a valuable tool for studying the mechanisms of inflammation and immune responses. Its production in E. coli and subsequent purification allow for high-quality protein suitable for various research applications.