Polyclonal Rabbit ATPG Antibody
- Known as:
- Polyclonal Rabbit ATPG Antibody
- Catalog number:
- KA0346
- Product Quantity:
- 100ul
- Category:
- -
- Supplier:
- KareBay
- Gene target:
- Polyclonal Rabbit ATPG Antibody
Related genes to: Polyclonal Rabbit ATPG Antibody
- Gene:
- CARNS1 NIH gene
- Name:
- carnosine synthase 1
- Previous symbol:
- ATPGD1
- Synonyms:
- KIAA1394
- Chromosome:
- 11q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2008-10-21
- Date modifiied:
- 2016-10-05
Related products to: Polyclonal Rabbit ATPG Antibody
Related articles to: Polyclonal Rabbit ATPG Antibody
- The flavor of chicken meat is formed by a series of complex chemical reactions, and the flavor precursors are affected by regulatory genes. In order to study the differences of muscle flavor precursors between Tengchong Snow chickens and AA broilers, integrated metabolomics and transcriptomics analyses were used to investigate muscle metabolite profiles and the key genes involved in the metabolism of muscle flavor compounds. The results showed that 42 significantly differentially metabolites were detected, and (5-L-Glutamyl)-L-glutamate, gamma-Glutamylalanine, S-Adenosylhomocysteine, Homo-L-arginine and GMP were important flavor metabolites. The key candidate genes with high correlation with flavor precursor metabolites were identified through correlation analysis as , , , , , and . In addition, the gene-metabolite interaction network for flavor formation in chicken breast muscle was constructed. This study could provide some basic data for the formation mechanism of local chicken excellent meat quality, and provide reference for the development and utilization of local chicken breeds and the selection and breeding of high-quality broilers. - Source: PubMed
Publication date: 2026/03/10
Yang MinZhang RuifangZhao JingyingJian ZonghuiWu HaoZi XiannianWang KunXu ZhiqiangGe ChangrongJia JunjingLiu LixianDou Tengfei - Neuronal axon regeneration is a complex and coordinated reorganization process that requires the involvement of mitochondria. Here, we demonstrated that FUNDC1 (FUN14 domain containing 1)-mediated mitophagy played a crucial role in determining the intrinsic capacity for axonal regrowth and peripheral nerve recovery. We found that acute nerve injury resulted in the accumulation of impaired mitochondria at the axonal injury site, accompanied by an increase in the expression of the mitophagy receptor FUNDC1. Strikingly, overexpression of FUNDC1 enhanced axonal regeneration both in vitro and in vivo, likely by maintaining a healthy mitochondrial population through mitophagy. Similarly, treatment with urolithin A (UA), a natural mitophagy inducer, promoted axon regrowth after injury. Conversely, deletion impaired regeneration, an effect reversed by reintroducing wild type (WT) FUNDC1 in neurons but not an MAP1LC3B/LC3 (microtubule associated protein 1 light chain 3 beta)-interacting region (LIR) mutant. Metabolic profiling further demonstrated that FUNDC1-mediated mitophagy drives dorsal root ganglion (DRG) neurons regeneration through enhanced carnosine biosynthesis. Mechanistically, sciatic nerve injury (SNI) in transgenic (TG) mice upregulated NRF1 (nuclear respiratory factor 1) and PPARGC1A/PGC-1α (PPARG coactivator 1 alpha), which stimulated mitochondrial biogenesis and activated (carnosine synthase 1) transcription. This increased carnosine biosynthesis, aiding peripheral nerve recovery through its antioxidant effects. Our findings highlighted FUNDC1-mediated mitophagy as a key mechanism in nerve regeneration, linking mitochondrial quality control, metabolic adaptation, and nerve regeneration.: Δψm: mitochondrial membrane potential; DIV: days in vitro; DRG: dorsal root ganglion; KO: knockout; LIR: LC3-interacting region; P60: postnatal day 60; PNS: peripheral nervous system; PSI: post sciatic nerve injury; ROS: reactive oxygen species; SD: standard deviation; SNI: sciatic nerve injury; TEM: transmission electron microscopy; TG: transgenic; TMRE: tetramethylrhodamine ethylester; UA: urolithin A; WT: wild type. - Source: PubMed
Publication date: 2026/03/08
Li WenleiLiu YujiaoLiu RuixuanFan YuyuanLiu JinmingGuo YingjieHu ZepingLiu LeiChen QuanZhou Bing - Evidence suggests that muscle activity can affect muscle carnosine, but the results are mixed. To address this question, we investigated muscle carnosine under two extremes of the muscle activity-inactivity spectrum. Forty-five male Wistar rats were divided into three groups: immobilization ( = 16), SHAM control ( = 14), and immobilization + exercise ( = 15). In the immobilized groups, one side was submitted to a sciatic nerve sectioning surgery, with the opposite side being submitted to a SHAM control surgery, creating four experimental conditions: denervated (DEN), SHAM active control (SHAM), denervated + exercise (DEN + Ex), and SHAM + exercise (SHAM + Ex). The immobilization period was 12 wk, and the swimming training period was 10 wk (4 times per week, up to 30 min per session). The (TA) and soleus muscles from both sides were assessed for carnosine and anserine contents, total histidine-dipeptides (HCDs), cross-sectional fiber area (CSA), and fiber type distribution. Contractile function was determined ex vivo in the , and the expression of the , , and genes was determined with real-time polymerase chain reaction in TA. Physical inactivity drastically reduced muscle mass, contractile function, and fiber CSA. Long-term postdenervation muscle paralysis reduced muscle carnosine and anserine content, which was not dependent on diet, age, sex, or fiber type. This demonstrates that muscle inactivity is a strong modulator of muscle HCD content, at least under extreme conditions. Gene expression was not significantly altered in any of the experimental conditions. Exercise training, on the other hand, did not affect muscle HCDs and may be a less potent regulator of muscle HCD content. This study demonstrated that an extreme model of muscle inactivity in rats (i.e., 12 wk of hindlimb paralysis following denervation) resulted in a substantial decline in muscle carnosine and anserine, which occurred irrespective of fiber type shift. Conversely, exercise training had no effect on histidine-dipeptide content. These findings, along with previously published studies, reinforce the notion that muscle inactivity is an important modulator of histidine-dipeptide homeostasis in skeletal muscle. - Source: PubMed
Publication date: 2026/02/23
Santana Amanda RomualdoVargas Bianca SciglianoBechara Luiz Roberto GrassmannFormalioni AndressaMöller Gabriella BerwigRodrigues Maria Rita de CamargoPereira Wagner Ribeiroda Silva Beatriz CristinaDos Prazeres Silva KarolineCury Diego PulzattoRoschel HamiltonMoriscot Anselmo SigariFerreira Julio C BMedeiros Marisa Helena Gennari deGonçalves Livia de SouzaArtioli Guilherme Giannini - Differences in growth rates among broiler chickens within a single commercial genetic line have important economic implications; however, their molecular basis remains incompletely understood. This study analyzed male Ross 308 broilers classified into early- and late-growth lines based on weight gain from 1 to 5 days of age. We integrated RNA sequencing, metabolomics based on gas chromatography-mass spectrometry, and exploratory SNP analysis of pectoralis major muscle tissue collected at 35 days of age. Our integrative analysis revealed contrasting energy utilization programs. Slow early-growth phenotype chickens showed a Warburg-like metabolic profile characterized by glycolytic reliance, lactate fermentation, ketone metabolism, and enhanced proteolysis, accompanied by a bottleneck in mitochondrial oxidative phosphorylation. In contrast, fast early-growth phenotype chickens displayed enhanced oxidative phosphorylation, elevated glycerol-3-phosphate levels, and coordinated activation of pathways related to mitochondrial function and immune responses. Notably, reduced CARNS1 expression in the fast early-growth group suggested a potential trade-off with muscle quality, consistent with the role of carnosine in pH buffering and maintaining redox balance. Multi-omics integrated analysis revealed coordinated changes in metabolites and gene expression within glycolysis, lipid metabolism, and mitochondrial pathways. These findings indicate that the weight gain phenotype during early growth is associated with specific transcriptional and metabolic states during later development. - Source: PubMed
Publication date: 2026/01/07
Ishihara ShinyaShimamoto SakiFujimura ShinobuKamimura MiyuIjiri Daichi - Cancer cells reprogram their metabolism to sustain energy production and biosynthesis for malignant proliferation; however, their metabolic phenotypes vary significantly across different growth environments, creating discrepancies between in vitro and in vivo findings. These inconsistencies pose challenges for translating metabolic research into clinical applications. The emergence of 3D culture models as in vitro systems that accurately mimic the in vivo environment can mitigate these challenges by providing conditions that reflect physiological architecture and metabolic interactions. Therefore, we investigated the impact of the purine metabolism enzyme hypoxanthine-guanine phosphoribosyltransferase 1 (HPRT1) on the proliferation and metabolism of SCLC cells using 2D and 3D culture models, with the goal of identifying context-specific metabolic regulation not captured in conventional 2D cultures. - Source: PubMed
Tabata ShoFujimoto IchiroSoga TomoyoshiMakinoshima Hideki