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Your Position: Home > Interleukin Protein Families

Interleukin Protein Families

Interleukin Protein Families
Introduction

Interleukins (ILs) is a term that describes a group of secreted molecules produced by leukocytes that act on a variety of cells. Generally, ILs are classified as cytokines, but are also a member of the lymphokines family. ILs have diverse biological functions; not only is it involved in regulating immune response such as promoting the information transmission, activation and regulation of immune cells, but also is widely involved in regulating the physiological and pathological processes of the body such as autoimmune, inflammatory and tumor diseases. Based on the structural homology of cytokines, interleukins are divided into several protein families, such as IL-1, IL-2, IL-6, IL-10, IL-12, and IL-17 families.

It is worth noting that, the interleukin family has emerged as a significant drug target, many of which are already on the market and even occupy a significant market share of drugs for similar diseases.

Data from Pharmacodia
Data from Pharmacodia
Data from Pharmacodia
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Supplemental Data
High purity and high structural homogeneity verified by SDS-PAGE and SEC-MALS
ILR-H5253

Biotinylated Human IL-1 RAcP, His,Avitag (Cat. No. ILP-H82E5) on SDS-PAGE under reducing (R) condition. The purity of the protein is greater than 90%. As verified by SEC-MALS, the purity is more than 90% and the molecular weight of this protein is around 50-68 kDa.

IL4-C5259

Human IL-2RB&IL-2RA&IL-2RG, Fc Tag&Fc Tag (Cat. No. ILG-H5257) on SDS-PAGE under reducing (R) condition. The purity of the protein is greater than 95%. As verified by SEC-MALS, the purity is more than 90% and the molecular weight of this protein is around 160-190 kDa.

High biological activity verified by ELISA
High purity and structural homogeneity verified by SDS-PAGE and SEC-MALS

Immobilized Mouse IL-2, His Tag (Cat. No. IL2-M52H3) at 5 μg/mL (100 μL/well) can bind Mouse IL-2RB&IL-2RA&IL-2RG, Fc Tag&Fc Tag (Cat. No. ILG-M5253) with a linear range of 0.8-3 ng/mL (QC tested).


High purity and structural homogeneity verified by SDS-PAGE and SEC-MALS

Immobilized Human IL-4 R alpha, Fc Tag (Cat. No. ILR-H5253) at 5 μg/mL (100 μL/well) can bind Biotinylated Human IL-4, Avitag,His Tag (Cat. No. IL4-H82E0) with a linear range of 0.1-2 ng/mL (Routinely tested).

Affinity verified by SPR and BLI
High purity and structural homogeneity verified by SDS-PAGE and SEC-MALS

Human IL-31, His Tag (Cat. No. IL1-H5247) capture on NTA-Series S sensor chip can bind Human IL-31 RA, Fc Tag (Cat. No. ILA-H5256) with an affinity constant of 37.1 nM as determined in a SPR assay (Biacore 8K) (Routinely tested).

High purity and structural homogeneity verified by SDS-PAGE and SEC-MALS

Human IL-13 R alpha 1 Protein, His Tag (Cat. No. IL1-H5224) captured on CM5 chip via anti-His antibody can bind Human IL-13 with an affinity constant of 16 nM as determined in a SPR assay (Biacore T200) (QC tested).

High purity and structural homogeneity verified by SDS-PAGE and SEC-MALS

Loaded Biotinylated Human IL-6, epitope tag free, primary amine labeling (Cat. No. IL6-H8218) on SA Biosensor, can bind Human IL-6 R alpha, His Tag (Cat. No. ILR-H4223) with an affinity constant of 45.9 nM as determined in BLI assay (ForteBio Octet Red96e).

High purity and structural homogeneity verified by SDS-PAGE and SEC-MALS

Loaded Biotinylated Human IL17A, His,Avitag (Cat. No. ILA-H82Q1) on SA Biosensor, can bind Human IL-17 RA, His Tag (Cat. No. ILA-H5222) with an affinity constant of 18.8 nM as determined in BLI assay (ForteBio Octet Red96e).

References
  • 1. Chung S H, Ye X Q, Iwakura Y. Interleukin-17 family members in health and disease[J]. International immunology, 2021, 33(12): 723-729. https://doi.org/10.1093/intimm/dxab075.
  • 2. Wojno E D T, Hunter C A, Stumhofer J S. The immunobiology of the interleukin-12 family: room for discovery[J]. Immunity, 2019, 50(4): 851-870. https://doi.org/10.1016/j.immuni.2019.03.011.
  • 3. Rose-John S. Interleukin-6 family cytokines[J]. Cold Spring Harbor perspectives in biology, 2018, 10(2): a028415. https://doi.org/10.1101/cshperspect.a028415.
  • 4. Netea M G, van de Veerdonk F L, van der Meer J W M, et al. Inflammasome-independent regulation of IL-1-family cytokines[J]. Annual review of immunology, 2015, 33: 49-77. https://doi.org/10.1146/annurev-immunol-032414-112306.
  • 5. Zdanov A. Structural analysis of cytokines comprising the IL-10 family[J]. Cytokine & growth factor reviews, 2010, 21(5): 325-330.doi:10.1016/j.cytogfr.2010.08.003.
  • 6. Dumont F J. Interleukin-2 family cytokines: potential for therapeutic immmunoregulation[J]. Expert Opinion on Therapeutic Patents, 2005, 15(5): 521-554. https://doi.org/10.1517/13543776.15.5.521.
  • 7. Fickenscher H, Hör S, Küpers H, et al. The interleukin-10 family of cytokines[J]. Trends in immunology, 2002, 23(2): 89-96. https://doi.org/10.1016/S1471-4906(01)02149-4.

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