Recombinant Human IL22 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2829

Recombinant Human IL22 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2829
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Product Overview

Tag His
Host Species Human
Accession NP_065386.1
Synonym IL-21, IL-22, IL-D110, IL-TIF, ILTIF, TIFa, TIFIL-23, zcyto18
Background IL22 is a member of a group of cytokines called the IL-1 family or IL-1 superfamily (including IL-19, IL-2, IL-24, and IL-26), a class of potent mediators of cellular inflammatory responses. It shares use of IL-1R2 in cell signaling with other members of this family, IL-1, IL-26, IL-28A/B and IL-29. IL22 is produced by activated DC and T cells and initiates innate immune responses against bacterial pathogens especially in epithelial cells such as respiratory and gut epithelial cells. IL22 along with IL-17 is rapidly produced by splenic LTi-like cells and can be also produced by Th17 cells and likely plays a role in the coordinated response of both adaptive and innate immune systems. IL22 biological activity is initiated by binding to a cell-surface complex composed of IL-22R1 and IL-1R2 receptor chains and further regulated by interactions with a soluble binding protein, IL-22BP, which shares sequence similarity with an extracellular region of IL-22R1 (sIL-22R1). IL22 and IL-1 receptor chains play a role in cellular targeting and signal transduction to selectively initiate and regulate immune responses. IL22 can contribute to immune disease through the stimulation of inflammatory responses, S1s and defensins. IL22 also promotes hepatocyte survival in the liver and epithelial cells in the lung and gut similar to IL-1. In some contexts, the pro-inflammatory versus tissue-protective functions of IL22 are regulated by the often co-expressed cytokine IL-17A.
Description A DNA sequence encoding the human IL22 (NP_065386.1) (Ala34-Ile179) was expressed with a His tag at the C-terminus.
Source Yeast
Predicted N Terminal Ala 34
AA Sequence Ala34-Ile179
Molecular Weight The recombinant human IL22 consists of 156 a.a. and predicts a molecular mass of 18.1 kDa.
Purity >95% as determined by SDS-PAGE.
Endotoxin Please contact us for more information.
Bioactivity Measured by its ability to induce IL-10 secretion in COLO 205 human colorectal adenocarcinoma cells. The ED50 for this effect is typically 0.2-0.8 ng/mL.
Formulation Lyophilized from sterile PBS, pH 7.4..
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

FAQs

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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