HIF1A polyclonal antibody
- Known as:
- HIF1A pab (anti-)
- Catalog number:
- PAB9946
- Product Quantity:
- 100 uL
- Category:
- -
- Supplier:
- Abno
- Gene target:
- HIF1A polyclonal antibody
Related genes to: HIF1A polyclonal antibody
- Gene:
- HIF1A NIH gene
- Name:
- hypoxia inducible factor 1 subunit alpha
- Previous symbol:
- -
- Synonyms:
- MOP1, HIF-1alpha, PASD8, HIF1, bHLHe78
- Chromosome:
- 14q23.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-03-27
- Date modifiied:
- 2018-04-23
Related products to: HIF1A polyclonal antibody
Related articles to: HIF1A polyclonal antibody
- The malignant progression of nonsmall cell lung cancer (NSCLC) is closely related to cancer stemness. Histone deacetylase 4 (HDAC4) plays a regulatory role in lung cancer, but its effect on NSCLC stemness remains unclear. This study aimed to investigate the role and mechanism of HDAC4 in NSCLC stemness. - Source: PubMed
Chen ChangxianJiang XiaomingYao ZhenwuSun JiaxueZhang LijuXu MingyuBao WeiminLiu Weijun - Intracerebral hemorrhage (ICH) is a devastating neurological disorder characterized by extensive neuronal death, in which ferroptosis has emerged as a central pathological mechanism. Yet, the role of mitophagy in regulating ferroptosis during ICH remains elusive. Herein, we identified a lactylation-mediated HSPA5 (heat shock protein family A (Hsp70) member 5)-VGLL3 (vestigial like family member 3) signaling axis that confers neuroprotection following ICH. We observed a marked upregulation of VGLL3 expression in ICH models, and loss-of-function experiments revealed that VGLL3 silencing exacerbated BNIP3 (BCL2/adenovirus E1B interacting protein 3)-BNIP3L/NIX (BCL2/adenovirus E1B interacting protein 3-like)-mediated, mitophagy-dependent ferroptosis. Mechanistically, VGLL3 enhanced EGLN3 (egl-9 family hypoxia-inducible factor 3) expression and reduced HIF1A/HIF-1α (hypoxia inducible factor 1, alpha subunit) stability, thereby suppressing BNIP3-BNIP3L-driven mitophagy. Upstream, HSPA5 activated VGLL3, and HSPA5 knockdown phenocopied the effects of VGLL3 silencing. Pharmacological activation of HSPA5 with the selective agonist BIP inducer X (BIX) suppressed mitophagy-dependent ferroptosis in cultured neurons, while BIX administration alleviated neuronal death and improved motor function in ICH mice. Epigenetic analyses further demonstrated that HSPA5 expression was transcriptionally modulated by histone H3-Lys18 (H3K18) lactylation, while its non-histone lactylation was catalyzed by the acetyltransferase EP300 (E1A binding protein p300) and removed by the NAD-dependent protein deacetylase SIRT1 (sirtuin 1). Collectively, our findings delineate a lactylation-driven HSPA5-VGLL3-EGLN3-HIF1A/HIF1-1α axis that represses BNIP3-BNIP3L-mediated, mitophagy-dependent ferroptosis. Targeting this pathway may provide a mechanistic rationale and therapeutic strategy for mitigating neuronal injury and functional deficits following ICH. BNIP3: BCL2/adenovirus E1B 19 kDa protein-interacting protein 3; BNIP3L/NIX: BCL2/adenovirus E1B interacting protein 3-like; EGLN3: egl-9 family hypoxia-inducible factor 3; GPX4: glutathione peroxidase 4; GSH: glutathione; GSSG: oxidized glutathione; HIF1A/HIF-1α: hypoxia inducible factor 1, alpha subunit; HSPA5: heat shock protein family A (Hsp70) member 5; IB: immunoblot; ICH: intracerebral hemorrhage; MDA: malondialdehyde; ROS: reactive oxygen species; SLC7A11: solute carrier family 7 member 11; VGLL3: vestigial like family member 3. - Source: PubMed
Publication date: 2026/09/28
QiXiang ZhangQiKai TangBaoFeng WangYiKui LiuYuXiao MaAoQian XuYuXiao XueSun YuHaoBian LiuGuan - To explore the expression levels and diagnostic value of miR-138-5p and hypoxia-inducible factor-1α (HIF-1α) in newly diagnosed acute myeloid leukemia (AML) patients. - Source: PubMed
Zhang Cong-CongLi Yin-LingChang Wei - Hepatocellular carcinoma (HCC) exhibits a suboptimal response to immune checkpoint blockade (ICB) therapy; to overcome this resistance, we aimed to delineate key immune resistance factors via multi-omics analysis, develop strategies to block their immunosuppressive axes, and engineer a targeted nanosystem to enhance immunotherapy efficacy against PD-1 resistance in HCC. Using transcriptomic and proteomic data from anti-PD-1-treated HCC patients, along with functional validation in murine models and mechanistic molecular and cell biology studies, we identified transketolase-like 1 (TKTL1) as a dual-nature biomarker where overexpression predicted poor baseline prognosis yet enhanced response to ICB. Mechanistically, TKTL1 diverts glucose flux into glycolysis rather than pentose phosphate pathway (PPP), recruiting USP9X to deubiquitinate and stabilize HIF-1α, which upregulates HK2 to amplify glycolytic output and lactate accumulation. This metabolic rewiring orchestrates dual immunosuppressive circuits through HIF-1α-driven CCL4 secretion recruiting PD-L1 dendritic cells (DCs), coupled with lactate-induced TRIM28 lactylation that stabilizes PD-L1 by blocking ubiquitin-mediated degradation. We engineered a hepatoma-membrane-coated MnO₂ nanosystem (CQLH) co-delivering a TKTL1 inhibitor and lactate oxidase, which disrupted the TKTL1-HIF-1α-HK2 axis, depleted lactate, and reprogrammed the tumor microenvironment, thereby enhanced anti-PD-1 therapy to suppress tumor growth, especially in TKTL1 tumors. These findings define a critical "TKTL1-glycolysis-lactate-DC" axis driving anti-PD-1 sensitivity in HCC, position TKTL1 as both a potential biomarker for ICB response and a tractable therapeutic target, and demonstrate that the targeted CQLH nanosystem overcomes resistance and enhances anti-PD-1 efficacy, offering a precision immunotherapeutic strategy for TKTL1 HCC. - Source: PubMed
Publication date: 2026/09/28
Cao HengsongHuang TianChai YueLu ZhengqingDai ShipengXu DanyangHe YanshuYu NaWang YuliangLiu ZiyuanXia YidongZhao JieWang HongyuRong DaweiXie YuchenWang ChongyuChen PengyuZhou JuyueLiu LiLi ZhuozhengLiu HanyuanLi XiaoWang XuehaoTang WeiweiXia Yongxiang - The M1-to-M2 macrophage phenotypic switch is critical for resolving inflammation and restoring homeostasis in hypoxic lung injury, but the underlying molecular mechanisms are unclear. Here, we show that hypoxia-induced histone lactylation (Kla) upregulates FTO via HIF1a-P300 interaction; lactylation-driven FTO then promotes late-stage M2 polarization by stabilizing Arg1 mRNA through the mA-YTHDF2 axis. Mechanistically, HIF1a/YY1 liquid-liquid phase separation (LLPS) regulates macrophage glycolysis and oxidative phosphorylation (OXPHOS) via the cGAS-STING pathway downstream of lactylation. Importantly, lactylation exerts context-dependent dual effects: physiological lactylation in wild-type mice facilitates M2 polarization, maintains metabolic balance, and promotes lung repair, whereas excessive lactylation in IL-10-deficient mice disrupts the FTO-Arg1 cascade, perturbs metabolism, blocks M2 polarization, and aggravates injury. Collectively, histone lactylation is a core switch governing macrophage polarization and metabolic homeostasis in hypoxic lung injury, with its function dictated by IL-10 status and lactylation abundance. - Source: PubMed
Publication date: 2026/09/25
Zhao XingwangZhang MengjieYin JunLiao JingyiLi DenghuiTian ZhiqiangYou YiZhang LonglongNi Bing