Human Recombinant IL37 protein (V2LY-0526-LY4912)

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Basic Information

Expressed Host
E. coli
Protein Species
Human
Protein Construction
This product is Human Recombinant IL37 protein consist of Amino Acid: 27-192 and predicts a molecular mass of 18.7 kDa.
Molecule Mass
18.7 kDa
Verified
HPLC
Sequence
Amino Acid: 27-192
Species
Human

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
≥96% as determined by SDS-PAGE. ≥90% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it 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.
More Infomation

Target

Full Name
Interleukin 37
Function
Suppressor of innate inflammatory and immune responses involved in curbing excessive inflammation. This function requires SMAD3. Suppresses, or reduces, proinflammatory cytokine production, including IL1A and IL6, as well as CCL12, CSF1, CSF2, CXCL13, IL1B, IL23A and IL1RN, but spares anti-inflammatory cytokines. Inhibits dendritic cell activation.
Biological Process
Cellular response to lipopolysaccharideManual Assertion Based On ExperimentIBA:GO_Central
Cytokine-mediated signaling pathwayManual Assertion Based On ExperimentIBA:GO_Central
Immune response2 PublicationsNAS:UniProtKB
Inflammatory responseManual Assertion Based On ExperimentIBA:GO_Central
Inflammatory response to antigenic stimulusManual Assertion Based On ExperimentIBA:GO_Central
Negative regulation of interleukin-6 productionManual Assertion Based On ExperimentIGI:ARUK-UCL
Negative regulation of tumor necrosis factor productionManual Assertion Based On ExperimentIGI:ARUK-UCL
Positive regulation of gene expressionManual Assertion Based On ExperimentIBA:GO_Central
Regulation of inflammatory responseManual Assertion Based On ExperimentIGI:ARUK-UCL
Cellular Location
Cytoplasm, cytosol; Nucleus; Secreted. Stimulation with IL1B leads to colocalization with SMAD3 mostly in perinuclear regions (PubMed:20935647).
Only the CASP1-cleaved mature form translocates into the nucleus upon LPS stimulation (PubMed:18390730).
The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in protein translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) followed by vesicle entry and secretion (PubMed:32272059).
PTM
Proteolytically converted to the mature form by CASP1.

Schröder, A., Lunding, L. P., Zissler, U. M., Vock, C., Webering, S., Ehlers, J. C., ... & Wegmann, M. (2022). IL‐37 regulates allergic inflammation by counterbalancing pro‐inflammatory IL‐1 and IL‐33. Allergy, 77(3), 856-869.

Rai, V., Dilisio, M. F., Samadi, F., & Agrawal, D. K. (2022). Counteractive Effects of IL-33 and IL-37 on Inflammation in Osteoarthritis. International Journal of Environmental Research and Public Health, 19(9), 5690.

Law, C. C., Puranik, R., Fan, J., Fei, J., Hambly, B. D., & Bao, S. (2021). Clinical implications of IL-32, IL-34 and IL-37 in atherosclerosis: speculative role in cardiovascular manifestations of COVID-19. Frontiers in Cardiovascular Medicine, 8, 630767.

Su, Z., & Tao, X. (2021). Current understanding of IL-37 in human health and disease. Frontiers in immunology, 12, 696605.

Sánchez-Fernández, A., Zandee, S., Amo-Aparicio, J., Charabati, M., Prat, A., Garlanda, C., ... & López-Vales, R. (2021). IL-37 exerts therapeutic effects in experimental autoimmune encephalomyelitis through the receptor complex IL-1R5/IL-1R8. Theranostics, 11(1), 1.

Zhao, T., Jin, F., Xiao, D., Wang, H., Huang, C., Wang, X., ... & Hao, J. (2020). IL-37/STAT3/HIF-1α negative feedback signaling drives gemcitabine resistance in pancreatic cancer. Theranostics, 10(9), 4088.

Wawrocki, S., Seweryn, M., Kielnierowski, G., Rudnicka, W., Wlodarczyk, M., & Druszczynska, M. (2019). IL-18/IL-37/IP-10 signalling complex as a potential biomarker for discriminating active and latent TB. Plos one, 14(12), e0225556.

Jing, L., Kim, S., Sun, L., Wang, L., Mildner, E., Divaris, K., ... & Offenbacher, S. (2019). IL-37-and IL-35/IL-37-producing plasma cells in chronic periodontitis. Journal of Dental Research, 98(7), 813-821.

Sehat, M., Talaei, R., Dadgostar, E., Nikoueinejad, H., & Akbari, H. (2018). Evaluating serum levels of IL-33, IL-36, IL-37 and gene expression of IL-37 in patients with psoriasis vulgaris. Iranian Journal of Allergy, Asthma and Immunology, 179-187.

Cavalli, G., & Dinarello, C. A. (2018). Suppression of inflammation and acquired immunity by IL‐37. Immunological reviews, 281(1), 179-190.

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For research use only. Not intended for any clinical use.

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