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Your Position: 홈 > 인터루킨 단백질군

인터루킨 단백질군

인터루킨 단백질군
소개
인기 제품
인터루킨군 및 관련 단백질
보충 자료
소개

인터루킨(Interleukins, IL)은 다양한 세포에 대해 작용하는 백혈구에 의해 생성되고 분비되는 분자 집단을 말합니다. 일반적으로 IL은 사이토카인으로 분류되지만 림포카인군의 일원이기도 합니다. IL은 다양한 생물학적 기능을 가지고 있습니다. 예를 들어 정보 전달 촉진, 면역 세포의 활성화와 조절 등 면역 반응을 조절하는 데 관여하며 그뿐 아니라 자가면역, 염증성 및 종양 질병 등 신체의 생리학적 및 병리학적 과정을 조절하는 데도 관여합니다. 인터루킨은 사이토카인의 구조적 상동성을 근거로 여러 개의 단백질군, 즉 IL-1, IL-2, IL-6, IL-10, IL-12 및 IL-17군으로 나뉩니다.

인터루킨이 유의한 약물 표적으로 부상했다는 점은 주목할 만한 소식입니다. 그 중 다수는 이미 시판되고 있으며 심지어 유사 질병에 대한 약물에서 상당한 시장 점유율을 차지하고 있습니다.

Data from Pharmacodia
Data from Pharmacodia
Data from Pharmacodia
인기 제품

인터루킨군 및 관련 단백질
IL-1군
IL-1군
IL-1 alphaIL-1 betaIL-1 RAcPIL-1 RIIIL-1 Rrp2IL-1RL1IL-18IL-18 R betaIL-18 R1IL-18BPIL-33IL-37IL-38
IL-2군
IL-2군
IL-2IL-2 R alphaIL-2 R betaIL-2 R gammaIL-2 R beta & IL-2 R gammaIL-2 R beta & IL-2 R alpha & IL-2 R gammaIL-4IL-4 R alphaIL-7IL-7 R alphaIL-7-P2AIL-13IL-13 R alpha 1IL-13 R alpha 2IL-15IL-15 R alphaIL-21 IL-21 R
IL-6군
IL-6군
IL-6IL-6 R alphagp130IL-11IL-11 R alphaIL-31IL-31 RA
IL-10군
IL-10군
IL-10IL-10 R alphaIL-20IL-20 R alphaIL-22IL-26IL-29
IL-17군
IL-17군
IL-17AIL-17BIL-17CIL-17EIL-17FIL-17A & IL-17FIL-17 RAIL-17 RCIL-17 RA & IL-17 RCIL-17 RE
기타 분자
IL-5IL-5 R alphaIL-3IL-3 R alphIL-8
보충 자료
SDS-PAGE 및 SEC-MALS로 검증된 고순도성과 높은 조직 균질성
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.

ELISA로 검증된 높은 생물활성도
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).

SPR 및 BLI로 검증된 친화도
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).

참고 문헌
  • 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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