Recombinant Mouse IL22 Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLA-0547P

Recombinant Mouse IL22 Protein (Fc Tag)

Beta LifeScience SKU/CAT #: BLA-0547P
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Product Overview

Host Species Mouse
Accession Q9JJY9
Synonym Cytokine Zcyto18 IL 10 related T cell derived inducible factor IL 21 IL 22 IL D110 IL TIF IL-10-related T-cell-derived-inducible factor IL-22 IL-TIF IL21 Il22 IL22_HUMAN ILD110 ILTIF Interleukin 10 related T cell derived inducible factor interleukin 21 Interleukin 22 Interleukin-22 MGC79382 MGC79384 TIFa TIFIL 23 TIFIL23 UNQ3099/PRO10096 zcyto18
Description Recombinant Mouse IL22 Protein (Fc Tag) was expressed in CHO cells. It is a Full length protein
Source CHO cells
AA Sequence LPVNTRCKLEVSNFQQPYIVNRTFMLAKEASLADNNTDVRLIGEKLFRGV SAKDQCYLMKQVLNFTLEDVLLPQSDRFQPYMQEVVPFLTKLSNQLSSCH ISGDDQNIQKNVRRLKETVKKLGESGEIKAIGELDLLFMSLRNACV
Molecular Weight 17 kDa
Purity >= 98% SDS-PAGE.
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Formulation Lyophilised
Stability The recombinant protein samples are stable for up to 12 months at -80°C
Reconstitution See related COA
Unit Definition For Research Use Only
Storage Buffer Shipped at 4°C. Upon delivery aliquot. Store at -20°C long term. Avoid freeze / thaw cycle.

Target Details

Target Function Cytokine that contributes to the inflammatory response in vivo.
Subcellular Location Secreted.
Protein Families IL-10 family
Database References

Gene Functions References

  1. The level of anti-IL17A autoantibodies that develop in aged Aire-deficient mice is not sufficient for conferring susceptibility to oropharyngeal candidiasis. However, patient-derived monoclonal antibodies that cross-react with murine IL-22 increase the fungal burden on C. albicans infected mucosa. PMID: 29150834
  2. This study defines a critical IL-36/IL-23/IL-22 cytokine network instrumental for antimicrobial peptide production and host defense in intestinal mucosa damage using a mouse inflammatory bowel disease model. PMID: 29760082
  3. The level of lncRNA H19 is increased in inflamed intestinal tissues from mice and patients. The inflammatory cytokine IL22 induces expression of H19 in IECs, which is required for intestinal epithelial proliferation and mucosal healing. H19 lncRNA appears to inhibit p53 protein and microRNA 34a and let-7 to promote proliferation of IECs and epithelial regeneration. PMID: 29621481
  4. Despite the presence of all Notch pathway molecules in the kidney and a model-specific induction of Notch ligands, IL-22 was only up-regulated in acute inflammation, but rapidly down-regulated during regeneration. This implies that for targeting injury responses, e.g. via IL-22, species-specific differences, injury type and time points have to be considered. PMID: 29054964
  5. Knockout of signal transducer and activator of transcription factor-3 (STAT3) in intestine epithelial cells resulted in complete loss of IL-22 protection, demonstrating that STAT3 is required for intestine barrier protection following ethanol combined with injury. PMID: 28498296
  6. Cancer cells induce IL-22 production from memory CD4(+) T cells via activation of the NLRP3 inflammasome and the release of IL-1beta to promote tumor growth. PMID: 29150554
  7. although IL-22 is expressed, it seems to play a minor role in protection and pathology during the acute systemic infection with the reticulotropic Tulahuen strain of T. cruzi PMID: 27650379
  8. IL-22 amplifies the inflammatory response, induces endothelial dysfunction and promotes blood pressure elevation in angiotensin II-induced hypertensive mice via STAT3 signaling. PMID: 28974499
  9. these results demonstrate a strong association between Hh-induced DNA damage and the development of dysplasia, and further suggest that IL-22-dependent induction of iNOS within crypt epithelial cells rather than macrophages is a driving force in this process PMID: 28198364
  10. IL-22 plays an important role in CIA development, and neutralizing this cytokine seems an attractive new strategy in RA treatment. Most importantly, SPECT/CT imaging with 111In-28H1 can be used to specifically monitor therapy responses, and is potentially more sensitive in disease monitoring than the gold standard method of macroscopic arthritis scoring. PMID: 29361119
  11. Protease IV, is responsible for the degradation of IL-22 by P. aeruginosa. The major anti-proteases molecules present in the lungs were unable to inhibit protease IV enzymatic activity. This so far undescribed cleavage of IL-22 by a bacterial protease is likely to be an immune-evasion strategy that contributes to P. aeruginosa-triggered respiratory infections. PMID: 27792459
  12. IL-22 seems to be the critical cytokine for the development of atopic dermatitis (AD) and is induced in AD model by epicutaneous sensitization with ovalbumin. PMID: 28655472
  13. finding demonstrated that IL-22 could exert favorable effects on Diabetic nephropathy (DN) via simultaneously alleviating systemic metabolic syndrome and downregulating renal NLRP3/caspase-1/IL-1beta pathway, suggesting that IL-22 might have therapeutic potential for the treatment of DN. PMID: 28726774
  14. this study shows that IL-22 mediates protective immunity during chronic stages of Mycobacterium tuberculosis HN878 infection in mice PMID: 28247861
  15. this study shows that hepatocyte responses to IL-22 stimulation are reduced in hypoxic environments PMID: 27796296
  16. Epithelial IL-23R signaling enables protective IL-22 responses in experimental colitis. PMID: 27524624
  17. We conclude that IL-22 has an important role in controlling S. aureus nasal colonization through distinct mechanisms, with IL-22 mediating its effect exclusively by inducing AMP expression and controlling availability of staphylococcal ligands. PMID: 27007677
  18. results reveal that IL-22 increases intestinal epithelial permeability by upregulating Claudin-2 expression through the JAK/STAT pathway PMID: 28939759
  19. investigated the function of Card9-mediated innate immunity in inflammation-associated colon carcinogenesis; report that Card9-signaling drives the production of IL-1beta within the damaged intestine and regulates the subsequent generation of IL-22 by group3 innate lymphoid cells, which promotes tumorigenesis via STAT3 activation within the transformed epithelium PMID: 28586167
  20. these results demonstrate that IL-22 has a critical role in vaccine-induced protection against Helicobacter pylori PMID: 27143303
  21. this study shows for the first time that a defect in IL-22 is involved in the acute exacerbation induced by non-typeable Haemophilus influenzae infection during experimental chronic obstructive pulmonary disease PMID: 27143304
  22. hypoxic IL-22 upregulation is dependent on HIF-1alpha PMID: 27534553
  23. Macrophage-derived IL-22 protects hepatocytes from ethanol-induced cell death. IL-22 downregulation is a new regulatory target of LPS in the pathogenesis of AH. PMID: 28637673
  24. IL-22 inhibits acetaldehyde-induced hepatic stellate cells activation and proliferation, which may be related to nuclear translocation of Nrf2 and increased activity of the antioxidant axis Nrf2-keap1-ARE. PMID: 28373766
  25. Endogenous IL-22 and hepatic IL-22R signaling play critical roles in controlling pneumococcal lung burden, and systemic IL-22 decreases bacterial burden in the lungs and peripheral organs by potentiating C3 opsonization on bacterial surfaces, through the increase of hepatic C3 expression. PMID: 27456484
  26. our data suggest that IL-20 subfamily cytokines, particularly IL-20, IL-22, and IL-24, might provide therapeutic benefit for patients with Diabetic foot ulcers (DFU) . PMID: 28125663
  27. innate immune cell-derived IL-22 is required for efficient liver regeneration and secretion of IL-22 in the regenerating liver is modulated by the ATP receptor, P2X1 PMID: 26853442
  28. IL-22 and its receptor have a crucial role in the development and pathogenesis of uveitis by facilitating inflammatory cell infiltration. PMID: 27166675
  29. We therefore postulate IL-22 as an important enhancer of the GC reaction, maintaining chemokine levels for the persistence of GC reactions, essential for the production of autoantibody-secreting plasma cells. Blocking IL-22 might therefore prevent immune-complex deposition and destruction of joints in RA patients. PMID: 27067635
  30. AhR has a direct role in IL-22 production by Th17 cells in the mouse ear skin, but not by gammadelta T cells, CD4(-) CD8(-) TCRbeta(+) T cells and ILCs. PMID: 27000947
  31. Taken together, our results demonstrate that Dok-1 and Dok-2 negatively regulate intestinal inflammation, apparently through the induction of IL-17A and IL-22 expression. PMID: 27450811
  32. Upregulation of IL-22 in combination with a complete loss of its negative regulator IL-22BP, and increased downstream STAT3-signaling in K8(-/-) and K8(-/-)Apc(Min/+) colonic epithelia confirmed that the IL-22 pathway, important in inflammation, proliferation and tissue regeneration PMID: 27234655
  33. this study shows that serum IL-22/IL-22BP protein ratio strongly correlates with psoriasis severity PMID: 28356382
  34. data suggest that the influence of IL-22 on autoimmunity is determined in part by the local microenvironment. In particular, IL-22 deficiency exacerbates tissue injury in inflammatory bowel disease, but has no influence on either the hepatocytes or cholangiocytes in the same model. PMID: 27148790
  35. this study has demonstrated a crucial role for retinoic acid in promoting IL-22 production and tempering dendritic cell function through downregulating S100A4 protein during viral hepatitis PMID: 28363907
  36. this study shows that losartan and dexamethasone may suppress inflammatory responses in IgA nephropathy by inhibiting IL-22 expression in Th22 cells PMID: 27930971
  37. Exogenous recombinant IL-22 protects mice against L-arginine-induced severe acute pancreatitis-associated lung injury by enhancing the expression of anti-apoptosis genes through the STAT3 signaling pathway. PMID: 27275094
  38. Orally administered R848 triggers TLR-7 on CD11c(+) dendritic cells, inducing interleukin-23 (IL-23) expression followed by a burst of IL-22 secretion by innate lymphoid cells, leading to Reg3gamma expression and restoration of colonization resistance against vancomycin-resistant enterococcus. PMID: 26912904
  39. IL-22 Defect During Streptococcus pneumoniae Infection Triggers Exacerbation of Chronic Obstructive Pulmonary Disease PMID: 26870795
  40. Rag-RORgammat-reporter and Rag KO mice undergoing ischemia reperfusion injury expressed high protein levels of both IL-22 and GFP (RORgammat) PMID: 26341825
  41. Overexpression of IL-22 significantly reduced the Klebsiella pneumonia infection in the liver and spleen. PMID: 26729763
  42. IL-22 restrains tapeworm-mediated protection against colitis via regulation of IL-25 expression PMID: 27055194
  43. IL-22 is involved in plaque formation; IL-22 released by immune cells is involved in activation of vascular repair by stimulating medial SMC dedifferentiation into a synthetic phenotype PMID: 26298743
  44. cigarette smoke can inhibit the ROCK2-IRF4 axis and modulate T cell production of IL-22 PMID: 26882474
  45. IL-17A and IL-22 work synergistically to induce antimicrobials and chemokines such as IL-8, components of calprotectin (CP), lipocalin (LCN) and some beta-defensins in both human and primary mouse gastric epithelial cells (GEC) and gastroids PMID: 26867135
  46. The study demonstrated the probable involvement of gamma delta T cells in the immune response of an organism via the secretion of IL-17 and IL-22. PMID: 26400286
  47. IL-22 is not required for type 1 diabetes pathogenesis; suggested that IL-22 may have a regenerative and protective role in the pancreatic islets PMID: 26496462
  48. IL-23, but not IL-17a or IL-22, promotes neutrophil recruitment and inflammatory cytokine and chemokine expression in the colon in response to C. difficile infection. PMID: 26455347
  49. Data suggest that interleukin 22 (IL-22) plays a pro-inflammatory/pathogenic role in the onset of antigen-induced arthritis (AIA) through apoptosis-associated speck-like Pycard protein (ASC)-dependent stimulation of interleukin-1 beta (IL-1beta) production. PMID: 26330334
  50. IL-22 can play a previously unappreciated role in controlling leishmania-induced immunopathology PMID: 26285207

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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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