IL36A 153 a.a. Mouse

The recombinant murine IL-36α protein contains 153 amino acid residues. It shares 83% amino acid sequence identity with rat IL-36α and 54-60% with human, rabbit, equine, and bovine IL-36α . The amino acid sequence of the recombinant protein is as follows:

RAASPSLRHV QDLSSRVWIL QNNILTAVPR KEQTVPVTIT LLPCQYLDTL ETNRGDPTYM GVQRPMSCLF CTKDGEQPVL QLGEGNIMEM YNKKEPVKAS LFYHKKSGTT STFESAAFPG WFIAVCSKGS CPLILTQELG EIFITDFEMI VVH

The recombinant IL-36α protein is expressed in E. coli and purified using high-performance liquid chromatography (HPLC). The protein is then tested for quality control using SDS-PAGE and Western Blot techniques to ensure its purity and biological activity . The final product is lyophilized from a 0.2 µm filtered concentrated solution in phosphate-buffered saline (PBS) with 1 mM dithiothreitol (DTT) and 3% trehalose .

IL-36α is fully biologically active when compared to standard proteins. It has been shown to induce IL-6 secretion in murine NIH/3T3 cells at concentrations less than 25 ng/mL, corresponding to a specific activity of greater than 4.0 x 10^4 IU/mg . The protein’s functionality is validated through various bioactivity assays, ensuring its effectiveness in research applications.

The lyophilized recombinant IL-36α protein is stable at 2-8°C but should be stored at -20°C for long-term preservation. Upon reconstitution, the preparation is most stable at -20 to -80°C and can be stored for one week at 2-8°C. To maintain maximal stability, it is recommended to apportion the reconstituted preparation into working aliquots and avoid repeated freeze-thaw cycles .

Recombinant IL-36α is widely used in research to study its role in immune responses and inflammatory processes. It is particularly valuable in experiments involving murine models, where it helps elucidate the mechanisms of action of IL-36α and its potential therapeutic applications.