Rat Anti-Mouse CD86, FITC-labeled
- Known as:
- Rat Antibody toMouse CD86, fluorecein-labeled
- Catalog number:
- 128-10056-2
- Product Quantity:
- 1 mg
- Category:
- -
- Supplier:
- Ray Biotech
- Gene target:
- Rat Anti-Mouse CD86 FITC-labeled
Related genes to: Rat Anti-Mouse CD86, FITC-labeled
- Gene:
- CD86 NIH gene
- Name:
- CD86 molecule
- Previous symbol:
- CD28LG2
- Synonyms:
- B7.2, B7-2
- Chromosome:
- 3q13.33
- Locus Type:
- gene with protein product
- Date approved:
- 1994-12-07
- Date modifiied:
- 2016-10-05
Related products to: Rat Anti-Mouse CD86, FITC-labeled
Related articles to: Rat Anti-Mouse CD86, FITC-labeled
- Our previous study demonstrated that HDAC1 knockdown alleviates traumatic brain injury (TBI), although underlying mechanisms remain unclear. Given the importance of microglial polarization in brain repair and its association with protein lactylation, this study investigated whether neuroprotective effects of HDAC1 inhibition in TBI are mediated through regulation of microglial polarization. In vivo TBI models, in vitro microglial cultures, immunofluorescence, CUT&Tag-seq and RNA-seq were employed to investigate the role of HDAC1 in TBI and its effects on microglial polarization and histone lactylation. Following TBI, microglia exhibited a predominant M1 phenotype with elevated HDAC1 expression, reduced histone lactylation, and altered expression of CD86 and CD206. Pharmacological inhibition of HDAC1, particularly with suberoylanilide hydroxamic acid (SAHA), or lactate supplementation restored histone lactylation and promoted M2 polarization. CUT&Tag-seq and qRT-PCR revealed that HDAC1 inhibition increased histone lactylation at the Gria1 promoter, leading to Gria1 upregulation in microglia. Hyperlactylated genes were enriched in neuroactive ligand-receptor interaction pathway. Overexpression of Gria1 in BV2 cells promoted M2 polarization, characterized by increased CD206 and decreased CD86 expression, which was further enhanced by HDAC1 inhibition or lactate treatment. RNA-seq identified SPP1 as a key downstream effector of Gria1 involved in immune and inflammatory responses. Knockdown of SPP1 suppressed CD206 and abolished the M2 polarization induced by Gria1 overexpression and HDAC1 inhibition. In a mouse TBI model, SAHA improved neurological recovery, reduced cortical lesions, upregulated Gria1 and SPP1, increased CD206, decreased CD86, and attenuated microglial activation. Collectively, pharmacological inhibition of HDAC1-mediated histone delactylation at the Gria1 promoter enhances Gria1-dependent SPP1 expression, thereby promoting microglial M2 polarization and attenuating neuroinflammation after TBI. - Source: PubMed
Publication date: 2026/09/11
Chen YimingWei LiangJi TongjieZhao KaijunZhong Chunlong - Colorectal cancer (CRC) remains a leading cause of cancer mortality, necessitating novel therapeutic strategies. Schisandrin C (SinC), a bioactive lignan from Schisandra chinensis, exhibits diverse pharmacological activities, but its anti-CRC mechanisms are poorly understood. This study investigated the anti-CRC mechanism of SinC, focusing on PPARγ-mediated ferroptosis and macrophage polarization. Network pharmacology predicted core targets and pathways. Direct SinC-PPARγ binding was confirmed by molecular docking, CETSA, and luciferase reporter assays. In HCT116 and LoVo cells, proliferation, migration, and ferroptosis were evaluated, with mechanistic validation using a PPARγ agonist, antagonist, and shRNA. M1/M2 markers in RAW264.7 macrophages were detected. In an AOM/DSS-induced CAC mouse model, ferroptosis and macrophage polarization were assessed by Prussian blue staining, immunohistochemistry, and Western blotting. SinC directly bound and activated PPARγ, concentration-dependently inhibiting CRC cell proliferation, migration, and colony formation while inducing ferroptosis-effects reversed by liproxstatin. Mechanistically, SinC activated PPARγ, suppressed JAK2/STAT3 signaling, and downregulated SLC7A11/GPX4, effects enhanced by a PPARγ agonist and abolished by PPARγ antagonist or shRNA. SinC upregulated M1 markers and pro-inflammatory cytokines, with a predominant M1-associated activation pattern. In CAC model, SinC improved survival, inhibited tumor growth, alleviated colonic pathology, exhibited biochemical features consistent with ferroptosis, and increased intratumoral CD86 cell infiltration. SinC directly binds and activates PPARγ transcriptional activity, inducing ferroptosis in CRC cells via the PPARγ-JAK2/STAT3-SLC7A11/GPX4 axis while concurrently promoting M1 macrophage polarization, exerting a dual antitumor effect. These findings support SinC as a promising therapeutic candidate for CRC. - Source: PubMed
Publication date: 2026/09/10
Wei XiaoWen Hong-PingSong Jian-BoXu Jin-FangGuo Hong-Rui - Myocardial ischemia/reperfusion (I/R) injury triggers sterile inflammation that amplifies tissue damage. We investigated whether metformin limits this response through the Nur77-SPARCL1 axis. RNA sequencing of HL-1 cardiomyocytes (n = 3 biological replicates per group) identified Sparcl1 as a metformin-responsive transcript. Mechanistically, metformin reduced Nur77 and SPARCL1 expression, while Nur77 directly bound the Sparcl1 promoter and activated transcription in a binding-site-dependent manner. Sparcl1 silencing in cardiomyocytes reduced the expression and secretion of pro-inflammatory cytokines (IL-6, TNF-α, and IL-1β) following hypoxia/reoxygenation. In vivo, using a mouse I/R model (n = 5 mice per group), Sparcl1 knockdown protected against myocardial injury by reducing infarct size, improving left ventricular function, and shifting the myocardial environment toward a reparative state-evidenced by increased ARG1- and CD206-positive cells, and reduced CD86- and iNOS-positive cells alongside lowered inflammatory cytokines. Furthermore, Nur77 overexpression alone aggravated I/R injury, increasing SPARCL1 expression, infarct size, and pro-inflammatory macrophage markers while impairing cardiac function and reducing AMPK/ACC phosphorylation. Metformin partially opposed these detrimental effects in Nur77-overexpressing mice. Together, these findings support the involvement of a Nur77-SPARCL1 inflammatory axis in myocardial I/R injury and in metformin-associated cardioprotection, while not excluding parallel Nur77-independent or AMPK-dependent mechanisms. - Source: PubMed
Publication date: 2026/09/10
Wu ZhenhuaBai YunpengChang ChaoJiao YanChen QinliangGuo Zhigang - Acute lung injury (ALI) or its more severe form, acute respiratory distress syndrome, is a life-threatening disease closely associated with an imbalance of M1/M2 macrophage polarization. Dezocine is commonly used clinically for perioperative pain relief, but whether it can regulate lipopolysaccharide (LPS)-induced alveolar macrophage polarization is unclear. This study aimed to determine the effect of dezocine on ALI and its potential ability to modulate macrophage polarization in ALI mouse models. The male C57BL/6 mouse were randomly divided into four groups: Control group, dezocine (DEZ) group, LPS group, and LPS + DEZ group. Samples were collected at 24 h after treatment to evaluate lung injury, inflammatory status and alveolar macrophage polarization. Dezocine ameliorated the severity of ALI, lung wet-to-dry (W/D) weight ratio, and lung injury scores. Additionally, Dezocine inhibited M1 polarization and promoted M2 polarization of alveolar macrophages, including the downregulation of M1-related markers (CD86) in lung tissue, the decrease of pro-inflammatory factors (interleukin-6, IL-6 and tumor necrosis factor-α, TNF-α) in serum and bronchoalveolar lavage fluid (BALF), the upregulation of M2-related markers (CD206) in lung tissue, the increase of ant-inflammatory factors(interleukin-10, IL-10 and transforming growth factor-β, TGF-β) in serum and BALF. These findings indicate that dezocine alleviates lung injury and exerts anti-inflammatory effects by modulating alveolar macrophage polarization balance, suggesting that dezocine might act as a novel anti-inflammatory drug for treating ALI and hence provide a promising strategy for enhanced the therapy in the clinic. - Source: PubMed
Publication date: 2026/09/10
Liu ZhenzhenFeng ManQiu ZiqiangWang LuluLiu GeLiu DongyiFeng Chang - Macrophage-keratinocyte crosstalk is an important component of cutaneous inflammatory responses. Psoriasis is a chronic inflammatory skin disease characterized by dysregulated keratinocyte proliferation and immune dysfunction. While macrophage pro-inflammatory activation is known to exacerbate psoriatic inflammation, the underlying molecular mechanisms remain incompletely understood. TRIM28, a multifunctional regulatory protein, may play a role in this process, but whether TRIM28 regulates macrophage-keratinocyte crosstalk in a psoriasis-relevant inflammatory context remains unclear. The present study was designed as an in vitro mechanistic investigation and does not establish TRIM28 dysregulation in human psoriasis. Therefore, psoriasis is discussed only as a potential disease context, rather than as a conclusion directly supported by the present data. - Source: PubMed
Gao ZheZhang XinWang JuanYang Ni