Chicken Interleukin 4,IL-4 ELISA Kit
- Known as:
- Chicken Interleukin 4,Interleukin-4 Enzyme-linked immunosorbent assay test Kit
- Catalog number:
- kn0042ch
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Kono Biotech
- Gene target:
- Chicken Interleukin 4 IL-4 ELISA Kit
Related genes to: Chicken Interleukin 4,IL-4 ELISA Kit
- Gene:
- IL4 NIH gene
- Name:
- interleukin 4
- Previous symbol:
- -
- Synonyms:
- BSF1, IL-4, BCGF1, BCGF-1, MGC79402
- Chromosome:
- 5q31.1
- Locus Type:
- gene with protein product
- Date approved:
- 1988-08-10
- Date modifiied:
- 2016-10-05
- Gene:
- TLR2 NIH gene
- Name:
- toll like receptor 2
- Previous symbol:
- -
- Synonyms:
- TIL4, CD282
- Chromosome:
- 4q31.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-06-25
- Date modifiied:
- 2016-10-25
Related products to: Chicken Interleukin 4,IL-4 ELISA Kit
Related articles to: Chicken Interleukin 4,IL-4 ELISA Kit
- Senescent cells, which have irreversibly arrested cell proliferation and a senescence-associated secretory phenotype, are characterized by the production of proinflammatory cytokines and growth factors. The selective clearance of senescent cells might have beneficial effects on physiological functions or aging-related diseases. Senolytic drugs, such as ABT-263, an inhibitor of BCL-2 family proteins, selectively kill senescent cells. In the present study, we investigated the effect of IL-4 and IL-13, which contribute to type 2 immunity and fibrosis, on ABT-263-induced apoptosis in senescent cells. Doxorubicin was used to induce senescence in TIG-1 cells, a normal diploid fibroblast line commonly used to study cellular senescence. Although ABT-263 selectively induced apoptosis in senescent TIG-1 cells at lower concentrations than were required to induce apoptosis in non-senescent cells, IL-4 and IL-13 suppressed ABT-263-induced apoptosis in senescent TIG-1 cells. Pharmacological experiments using inhibitors revealed that the suppressive effects of IL-4 and IL-13 involved the IL-4Rα/JAK/STAT6 signaling pathway. We found that IL-4 and IL-13 altered the expressions of molecules involved in extracellular matrix and cell adhesion, and induced phosphorylation of the downstream FAK/Akt/GSK3β signaling pathway. In addition, senescent TIG-1 cells treated with IL-4 and IL-13 showed increased glucose consumption, and the suppressive effect of IL-4 and IL-13 was partially abolished by inhibitors of the glucose metabolic pathway. Taken together, IL-4/IL-13 signaling had a suppressive effect on ABT-263-induced apoptosis in senescent human fibroblasts. These results suggest that a combination of senolytic drugs and inhibitors targeting IL-4/IL-13 signaling might be effective for aging-related diseases. - Source: PubMed
Publication date: 2026/06/01
Nishinaka TakashiWake HidenoriWatanabe MasahiroToyomura TakaoMori ShujiNishibori MasahiroTakahashi Hideo - Airway fibrosis in severe asthma is a hallmark of disease pathology, yet the mechanisms driving fibroblast activation remain incompletely understood. While interleukin-4 (IL-4) and interleukin-13 (IL-13) are central to type 2 inflammation, their combined role in directly promoting human lung fibroblast-mediated fibrosis is not well defined. This study demonstrates that IL-4 and IL-13 act synergistically on asthmatic fibroblasts to potentiate a pro-fibrotic program via the shared interleukin-4 receptor alpha (IL-4Rα)/Signal Transducer and Activator of Transcription 6 (STAT6) axis. We found that diseased human lung fibroblasts (DHLFs) from asthmatic patients exhibited elevated expression of the type II receptor (IL-4Rα/IL-13Rα1) compared to normal human lung fibroblasts (NHLFs), priming them for activation. Consequently, combined IL-4/IL-13 stimulation synergistically enhanced STAT6 phosphorylation and robustly upregulated key extracellular matrix (ECM) components (collagen I/III, fibronectin) and regulators (matrix metalloproteinase-9 (MMP-9), tissue inhibitor of metalloproteinase-1/2 (TIMP-1/2). Furthermore, IL-4 specifically emerged as the dominant driver of fibroblast proliferation. Critically, the IL-4Rα-blocking antibody dupilumab effectively abrogated this pro-fibrotic response. These findings provide a direct mechanistic basis for targeting the IL-4Rα pathway to mitigate airway remodeling and potentially alter the progressive course of fibrosis in patients with severe, type 2-high asthma. - Source: PubMed
Publication date: 2026/05/30
Sahnoon LinaAbujabal RolaAlanta Tasneem MMdkhana BushraOlivenstein RonaldPuré EllenMahboub BassamLaumonnier YvesHamoudi RifatBajbouj KhuloudHamid Qutayba - Chronic inflammation and aging skew hematopoiesis toward myelopoiesis at the expense of lymphoid output. We screened type 2 and anti-inflammatory cytokines to identify extrinsic signals capable of restoring lymphoid lineage commitment in hematopoietic stem and progenitor cells (HSPCs). Interleukin 4 (IL-4) specifically inhibited inflammation-induced myelopoiesis and shifted multipotent progenitor (MPP) differentiation toward the lymphoid lineage. IL-4 activated a signal transducer and activator of transcription 6 (STAT6)-dependent transcriptional program in MPPs, increasing the expression of lymphoid-specific genes. Mechanistically, the receptor tyrosine kinase FMS-like tyrosine kinase 3 (FLT3), which is highly expressed in MPPs, interacted with IL-4Rα to facilitate STAT6 activation. In vivo, IL-4 reversed inflammation-induced hematopoietic imbalance and accelerated lymphoid recovery. In aged mice, IL-4 administration shifted the MPP composition toward a lymphoid bias and restored B and T lymphocyte output. Long-term IL-4 treatment in aged mice improved immune, metabolic, physical, and cognitive functions; these rejuvenating effects were recapitulated by transplantation of IL-4-treated HSPCs. Promoting IL-4 signaling in MPPs may enable correction of hematopoietic dysregulation in inflammatory and aging-related conditions. - Source: PubMed
Publication date: 2026/05/29
Yao JingfeiWang YutingZhang Yi - Interleukin (IL)-13 can modulate tumor immunosurveillance. The interplay between IL-13 and immunotherapy outcomes has not been well elucidated. - Source: PubMed
Publication date: 2026/05/04
Fountzilas ElenaKurzrock RazelleNishizaki DaisukeSzabo AnikoPabla SarabjotDePietro PaulJensen Taylor JKato ShumeiTsimberidou Apostolia-Maria - Rademikibart (CBP-201) is a human monoclonal antibody with higher binding affinity to IL-4Rα compared to dupilumab. Dupilumab is a first-generation interleukin-4 receptor alpha (IL-4Rα) inhibitor for treating IL-4Rα-dependent inflammatory disorders, including several dermatologic and respiratory conditions. Rademikibart, however, demonstrated better inhibition of STAT6 intracellular signaling and similar potency in inhibiting both IL-4 induced TARC release and IL-4 induced B cell activation. To further characterize the molecular function of rademikibart and its differentiation from dupilumab, we determined the crystal structure of the rademikibart fragment antigen binding (Fab) bound to IL-4Rα at 2.71 Å resolution and compared this to the 2.82 Å resolution structure of dupilumab Fab bound to IL-4Rα. The rotation angle between dupilumab and rademikibart bound to IL-4Rα is 54.88°. This rotation enables the binding epitopes of rademikibart, but not dupilumab, on IL-4Rα to overlap more closely with the conserved binding interface naturally utilized by IL-4 and IL-13 cytokines. Molecular dynamics (MD) studies on rademikibart and dupilumab bound to IL-4Rα examined the stability of the complexes and effects of amino acid mutations on receptor complex formation. MD simulations demonstrated that the third interface loop (residues 145 to 153 in domain 2) of IL-4Rα interacts directly with rademikibart, which is absent in the dupilumab/IL-4Rα complex. This finding is confirmed by increased hydrogen bond interactions at the interface between rademikibart and IL-4Rα, demonstrating superior binding energy for rademikibart. Through analysis of the x-ray crystallography structures, MD-equilibrated structures, and computational point-mutation analysis of rademikibart, we identified residue Y50 and R55 of the light chain and R97, R99, and Y101 of the heavy chain of rademikibart as key residues interacting with IL-4Rα's third interface loop. Our data provides a molecular and structural rationale for the enhanced IL-4Rα inhibition by rademikibart over dupilumab, confirming rademikibart as an optimized second-generation IL-4Rα inhibitor. - Source: PubMed
Publication date: 2026/04/13
Shi YuanjunNolden KelseyHo MinhLi HaoteBatista Victor SCollazo RaúlBunick Christopher G