The Recombinant Mouse IL-20 Protein is a high-quality recombinant protein designed for murine biological research applications. This protein serves as an essential reagent in mouse model studies, comparative immunology research, and preclinical therapeutic evaluations, enabling scientists to investigate IL-20 biology and its relevance to human disease mechanisms through translational research approaches.
This product (SKU: RPCB0018) is produced using advanced expression systems and features a N-His tag for convenient detection and purification. The protein exhibits a calculated molecular weight of 18.42 kDa with an observed molecular weight of 15-25 kDa under denaturing conditions, achieving ≥ 95 % as determined by SDS-PAGE., ensuring exceptional quality and consistency for research applications.
High quality, high purity and low endotoxin recombinant Recombinant Mouse IL-20 Protein (RPCB0018), tested reactivity in HEK293 cells and has been validated in SDS-PAGE.100% guaranteed.
Endotoxin:
< 0.01 EU/μg of the protein by LAL method
Purity:
≥ 95 % as determined by SDS-PAGE.
Formulation:
Lyophilized from a 0.22 μm filtered solution of 20mM PB,500mM NaCl, pH 8.0.
Reconstitution:
Centrifμge the vial before opening. Reconstitute to a concentration of 0.1-0.5 mg/mL in sterile distilled water. Avoid vortex or vigorously pipetting the protein. For long term storage, it is recommended to add a carrier protein or stablizer (e.g. 0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose), and aliquot the reconstituted protein solution to minimize free-thaw cycles.
Storage:
Store at -20℃. Store the lyophilized protein at -20℃ to -80℃ up to 1 year from the date of receipt. After reconstitution, the protein solution is stable at -20℃ for 3 months, at 2-8℃ for up to 1 week.
Mouse Interleukin 20 (IL-20) was identified by searching sequence databases for translated sequences with a signal sequence and amphipathic helices found in helical cytokines. Based on the human molecule, mouse IL-20 was discovered in a skin library. Mouse IL-20 is synthesized as a 176 amino acid (aa) precursor that contains a 24 aa signal sequence and a 152 aa mature segment. There are no N-linked glycosylation sites and it is doubtful that the native molecule is glycosylated. Although IL-20 is a distant member of the IL-10 family, it functions as a monomer. IL-20 shares less than 40% aa sequence identity with other IL-10 family members. Mouse and human IL-20 are 77% aa identical in the mature segment. IL-20 production has been found in skin and trachea. In particular, activated keratinocytes and, possibly, monocytes are reported to express IL-20. There are two heterodimeric receptor complexes for IL-20. The first complex is composed of IL-20 R alpha and IL‑20 R beta. The second complex is composed of IL-22 R and IL‑20 R beta. Whereas the IL-22 R/IL-20 R beta complex is shared with IL-24/mda-7, the IL‑20 R alpha /IL‑20 R beta complex is shared with both IL-19 and IL-24. Little is known about the function of IL-20. It is reported to induce the proliferation of multipotential hematopoietic progenitor cells, direct the differentiation and expansion of keratinocytes, and promote the release of proinflammatory mediators in keratinocytes and other IL-20 receptor expressing cells.
Recombinant Mouse IL-20 Protein was determined by SDS-PAGE under reducing conditions with Coomassie Blue.
