ACAA1 (Human) Recombinant Protein (Q01)
- Known as:
- ACAA1 (Human) Recombinant Protein (Q01)
- Catalog number:
- H00000030-Q01-25
- Product Quantity:
- 25 ug
- Category:
- -
- Supplier:
- Abno
- Gene target:
- ACAA1 (Human) Recombinant Protein (Q01)
Related genes to: ACAA1 (Human) Recombinant Protein (Q01)
- Gene:
- ACAA1 NIH gene
- Name:
- acetyl-CoA acyltransferase 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 3p22.2
- Locus Type:
- gene with protein product
- Date approved:
- 1989-06-30
- Date modifiied:
- 2019-03-22
Related products to: ACAA1 (Human) Recombinant Protein (Q01)
Related articles to: ACAA1 (Human) Recombinant Protein (Q01)
- Hickory nuts were nutrient-rich but were prone to storage deterioration due to high fat content. In this study, using integrated lipidomics and transcriptomics, we profiled 2159 lipids and 5952 differentially expressed genes in hickories stored at 4 °C and 35 °C for 90 days. Results showed that oxidative stress decreased iodine value and increased anisidine and conjugated diene values, reflecting reduced lipid unsaturation and oxidation product accumulation. Upregulation of TGL4 and PLD1_2 accelerated triglyceride and phospholipid hydrolysis. However, ACAA1 downregulation inhibited free fatty acid catabolism generated during this process, which promoted off-flavor generation and anomalous triglyceride accumulation via re-esterification. Additionally, downregulation of DGKs and FAB2 caused the gradual accumulation of LPCs and Cer, disrupting sphingolipid balance and membrane integrity. This multi-omics study elucidates how dysregulation of lipid repair and sphingolipid disruption lead to accelerated oxidation during hickory storage. The findings supported Sustainable Development Goal 12.3 by informing strategies to reduce postharvest nut losses. - Source: PubMed
Publication date: 2026/08/29
Wang ChongchongBi YajunMin Weihong - The lenticulostriate arteries (LSAs) demonstrate developmental variability that is linked to the A1 segment of the anterior cerebral artery (ACA) anatomy. In acute ischaemic stroke (AIS) with MCA occlusion, basal ganglia (BG) infarction extent and haemorrhagic transformation (HT) correlate with LSA involvement. This study aimed to assess whether ipsilateral A1-ACA variations influence BG infarction severity and thrombectomy outcomes. - Source: PubMed
Sun WenpingHe GuangchenLu HaitaoWei LimingXu HaoyangZhu Yueqi - Heat stress leads to excessive hepatic lipid deposition and oxidative imbalance in laying hens, especially during peak laying period. Chlorogenic acid (CGA), a dietary polyphenol with antioxidant and lipid-modulating properties, may improve hepatic lipid homeostasis, yet its effects under heat-stress conditions remain unclear. In this study, 240 Hy-Line Brown laying hens at 36 weeks of age were randomly assigned to one of two treatments (120 hens per treatment, with six replicates of 20 hens each): a basal diet or a basal diet supplemented with 300 mg/kg CGA and subjected to heat-stress conditions for 8 weeks. CGA supplementation significantly reduced liver weight (25.3%), liver index (14.4%), hepatic triglyceride content (29.1%), and serum triglyceride level (61.7%) ( < 0.05). Histological assessment revealed lower steatosis and inflammation scores, alongside increased hepatic SOD activity (13.6%) and decreased MDA content (58.7%) ( < 0.05). RNA-seq analysis identified 420 differentially expressed genes that were significantly enriched in PPAR signaling and fatty acid β-oxidation pathways. CGA upregulated fatty acid oxidation-related genes (, , , ) and downregulated lipogenic markers (, ). Serum metabolomics revealed coordinated changes in lipid and carbon metabolism. These results indicate that dietary CGA alleviates hepatic lipid accumulation and oxidative stress in heat-stressed peak-laying hens, potentially via PPARα-mediated enhancement of fatty acid oxidation and inhibition of de novo lipogenesis. - Source: PubMed
Publication date: 2026/06/12
Wang DanTan HaiqiuPeng LinWu XuanfuGao JiangMa Wenqiang - Crystal adhesion is a key process in the formation of kidney stones, playing a synergistic role at every crystallization stage. Damage to the renal tubular epithelial cell (RTEC) membrane provides essential sites for crystal adhesion. During the terminal phase of ferroptosis, accumulated polyunsaturated phospholipids integrate into the cell membrane, leading to membrane damage and deformation, which may be an important mechanism in calcium oxalate (CaOx) crystallization. In this study, targeted peroxidomics analysis revealed a significant increase in arachidonic acid (AA) levels in a CaOx kidney stone model. Meanwhile, transcriptomic analysis indicated that the key enzyme in fatty acid metabolism, acetyl-coenzyme A (CoA) acyltransferase 1 (ACAA1), was significantly downregulated in the CaOx kidney stone model. Besides, overexpression of ACAA1 (OE-ACAA1) alleviated AA accumulation and reduced oxalate (Ox)-induced RTEC ferroptosis. Notably, the OE-ACAA1 alleviated the accumulation of AA-containing polyunsaturated phospholipids without regulating acyl-CoA synthetase long-chain family member 4 (ACSL4) expression, thereby reducing membrane peroxidative damage and crystal adhesion. Furthermore, transcription factor array analysis identified the downregulation of activating transcription factor 1 (ATF1), an upstream transcriptional regulator of ACAA1, which might be involved in the transcriptional repression of ACAA1. Finally, OE-ATF1 partially alleviated Ox-induced RTEC membrane peroxidative damage and crystal adhesion. These findings demonstrated that ferroptosis participates in the early crystallization process by mediating RTEC membrane peroxidative damage and provided a novel approach to influencing downstream lipid peroxidation by regulating fatty acid activation substrates rather than ACSL4. Therefore, this study offers potential therapeutic targets for the prevention and treatment of CaOx kidney stones. - Source: PubMed
Publication date: 2025/10/10
Jiang QinhongXie YanqiSong ChaoDong CaitaoLiao WenbiaoSong QianlinSu XiaozheXiang HengWang YunhanCheng BoboHe ZiqiYang Sixing - Postprandial variability in glucose and protein levels is one of the elements of insulin resistance (IR) and prediabetes, which is an area precursor to type 2 diabetes mellitus (DM). The objective of the study was a comprehensive proteomic analysis according to glucose tolerance in the general population who did not self-report DM or other diseases. We used Olink Reveal, a novel, high-throughput platform by Olink Proteomics based on their Proximity Extension Assay (PEA), to identify levels of 1034 circulating proteins in small volumes (4 µL) of plasma samples. The study enrolled 508 participants (mean age 52 ± 10.5 years, 47.2% men) from the population-based study, Bialystok PLUS Polish Longitudinal University Study. The study population was categorized according to glucose metabolism in comparison to impaired fasting blood glucose (IFG), impaired glucose tolerance (IGT), and newly diagnosed DM. Analysis of variance (ANOVA) adjusted for age, weight, fat mass, lean mass, and body mass index (BMI), identified 19 proteins significantly associated with categories of glucose tolerance. Of the five markers with the greatest ability to distinguish newly diagnosed diabetes from non-diabetic participants, paralemmin 2 performed best (AUC = 0.81; 77% sensitivity, 75% specificity), whereas furin was the most accurate for detecting any abnormal glucose regulation (AUC = 0.69). A linear regression model adjusted for the same confounding factors showed statistically significant associations between Hb levels and 37 proteins. Our findings highlight multiple proteins with significantly different levels across categories of glucose tolerance, especially between the healthy controls and the group with newly diagnosed DM. The consistent patterns of protein level differences, independent of body composition, suggest potential involvement in the progression of glucose metabolism disturbances and provide unique insights into pathomechanisms. These findings identify PALM2, FURIN, PDZK1, ACAA1, and IL18R1 as potential biomarkers of early dysglycemia. - Source: PubMed
Publication date: 2026/04/26
Zieleniewska NataliaJamiołkowski JacekMalarstig AndersDiamanti KlevChlabicz MałgorzataKondraciuk MarcinWoo KerhanKowalska IrinaKamiński Karol