MIL 22A Recombinant eiwit

Source : Escherichia Coli. Interleukin-22 Antagonist Mouse Recombinant produced in E.Coli is a single, non-glycosylated homodimeric polypeptide chain containing 147 amino acids and having a total molecular mass of 16.7 KDa. The Mouse IL-22 Antagonist is purified by proprietary chromatographic techniques. IL-22 is a member of the IL-10 family of regulatory cytokines.Members of this family share partial homology in their amino acid sequences, but they are dissimilar in their biological functions. Produced by T lymphocytes, IL-22 inhibits IL-4 production by Th2 cells, and induces acute phase reactants in the liver and pancreas. IL-22 signals through a receptor system consisting of IL-10R-beta/CRF2-4 and IL-22R, both of which are members of the class II cytokine-receptor family.

IL-TIF||TIFa||IL-10-related T-cell-derived-inducible factor||IL-22||ILTIF||IL-D110||zcyto18||MGC79382||MGC79384||TIFIL-23.

Greater than 98.0% as determined by: (a) Gel filtration chromatography under non-denaturing conditions. (b) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel.

IL-22 Antagonist Mouse is lyophilized from a concentrated (1mg/mL) solution in water containing NaHCO3.

Lyophilized Interleukin-22 Mouse Antagonist although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL22 Antagonist should be stored at 4°C between 2-7 days and for future use below -18°C.Please prevent freeze-thaw cycles.

It is recommended to reconstitute the lyophilized Interleukin -22 in sterile 18MΩ-cm H2O not less than 100μg/ml, which can then be further diluted to other aqueous solutions. IL-22 E117A mutant is capable of full inhibition of STAT3 phosphorylation induced by mouse interleukin 22 in HepG cells. Its affinity toward immobilized mIL-22 receptor a1 extracellular domain (mIL-22 Ra1-ECD) or IL-22 binding protein is similar to the non-mutated mouse interleukin 22. Mouse IL-22 antagonist (E117A) has very low agonistic activity in this bioassay.

The sequence of the first five N-terminal amino acids was determined and was found to be Ala-Leu-Pro-Val-Asn.