Recombinant Human IL1F10 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2769

Recombinant Human IL1F10 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-2769
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Product Overview

Tag His
Host Species Human
Accession AAK68048.1
Synonym FIL1-theta, FKSG75, IL-1HY2, IL-38, IL1-theta, IL1HY2
Description A DNA sequence encoding the human IL1F10 (AAK68048.1) (Met1-Trp152) was expressed with a His tag at the C-terminus.
Source Yeast
Predicted N Terminal Met
AA Sequence Met1-Trp152
Molecular Weight The recombinant human IL1F10 consists 162 a.a. and predicts a molecular mass of 18.4 kDa.
Purity >90% as determined by SDS-PAGE.
Endotoxin Please contact us for more information.
Bioactivity Please contact us for detailed information
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.

Target Details

Target Function Cytokine with immunomodulatory activity. Alone, does not induce cytokine production, but reduces IL22 and IL17A production by T-cells in response to heat-killed Candida albicans. Reduces IL36G-induced production of IL8 by peripheral blood mononuclear cells. Increases IL6 production by dendritic cells stimulated by bacterial lipopolysaccharides (LPS). Ligand for IL-36R/IL1RL2.
Subcellular Location Cytoplasm. Secreted.
Protein Families IL-1 family
Database References
Tissue Specificity Expressed in fetal skin, spleen and tonsil. Expressed mostly in the basal epithelia of skin and in proliferating B-cells of the tonsil.

Gene Functions References

  1. The serum level of IL-38 in the children in the acute phase of Kawasaki disease was significantly lower than that in the healthy control group PMID: 30022755
  2. IL-38 may play an important role in acute and/or chronic inflammation in anticancer drug-induced lung injury and acute exacerbation of idiopathic pulmonary fibrosis. PMID: 28942884
  3. IL-38 may exert its anti-inflammatory effects by decreasing the production of proinflammatory cytokines by macrophages and synovial fibroblasts. PMID: 28288964
  4. this clinical study demonstrates the elevation of anti-inflammatory cytokine IL-38 and the decrement of CD4+CD25highFoxP3+ and CD4+CD25highCD127- Treg in childhood asthma. The negative correlation of IL-38 and Treg lymphocytes may imply a negative feedback of the two anti-inflammatory factors in asthma. PMID: 27438823
  5. this study shows that in vivo expression of human IL-38 in mice has hepatoprotective effects against Con A-induced liver injury by inhibition of inflammatory cytokine production PMID: 27723569
  6. Higher serum IL-38 levels before treatment indicate a greater probability of viral response to telbivudine treatment in chronic hepatitis B. PMID: 27182162
  7. results indicate that circulating IL-38 is a potentially novel biomarker for patients with ST-segment elevation myocardial infarction PMID: 26819499
  8. Data suggest that IL-38 may be protective in SLE. A strong association between IL-38 and SLE severity suggests that IL-38 expression is driven by processes linked to SLE pathogenesis. PMID: 26314375
  9. rs6759676, closest gene locus IL1F10 is associated with increased circulating levels of IL-1 receptor antagonist, a protective factor in development of insulin resistance. PMID: 24969107
  10. The IL1A locus was strongly associated with alkylosing spondyloarthritis phenotype, whereas IL1F10 was associated with non-alkylosing spondyloarthritis. PMID: 22312160
  11. These data provide evidence that IL-38 binds to the IL-36R, as does IL-36Ra.[IL-38, IL-36R] PMID: 22315422

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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