Certificate of Analysis & Data Sheet

IL-22 is a member of the IL-10 family of regulatory cytokines which includes IL-10, IL-19, IL-20, IL-22, IL-24 and IL-26. 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. Recombinant murine IL-22 mutant Y51A (numbering according to human IL-22 including signal peptide) produced in E.Coli is a single, non-glycosylated polypeptide chain containing 147 amino acids and having a molecular mass of 16.7 kDa. Preparation of recombinant mIL-22 antagonists provides new tools for the study of IL-22 activity and of eventual therapeutic means for attenuating its negative effects. For more details see L. Niv-Spector et al. Protein Eng Des Sel. (PEDS) 25:397-404 (2012).

E. coli

Lypohylized white powder

Interleukin-22 Y51A s lyophilized from a concentrated (1mg/ml) solution in water containing NaHCO3.

It is recommended to reconstitute the lyophilized IL-22 Y51A in sterile H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions containing carrier protein such as BSA, HSA or similar.

Lyophilized IL-22 Y51A although stable at 4C, should be stored desiccated below -18C. Upon reconstitution interleukin-22 Y51A should be stored at 4C between 2-7 days and for future use below -18C. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.

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

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

Less than 2% as determined by gel filtration under non-denaturing conditions.

PLR’s murine IL-22 Y51A mutant is capable of full inhibition of STAT3 phosphorylation induced by mouse interleukin 22 in HepG cells. Its affinity toward immobilized mIL-22 receptor α1 extracellular domain (mIL-22 Rα1-ECD) or IL-22 binding protein is similar to the non mutated mouse interleukin 22. Mouse IL-22 antagonist (Y51A) has no agonistic activity in this bioassay.

Less than 0.05 ng/µg (0.5 EU/µg) of recombinant IL-22 (Y51A).

Protein quantitation was carried out by UV spectroscopy at 280 nm using the absorbency value of 0.18 as the extinction coefficient for a 0.1% (1mg/ml) solution. This value is calculated by the DNAman computer analysis program of protein sequences.

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