AKR1C3 antibody
- Known as:
- AKR1C3 (anti-)
- Catalog number:
- orb28017
- Product Quantity:
- 5 ug(Trial size)
- Category:
- -
- Supplier:
- Biorb
- Gene target:
- AKR1C3 antibody
Related genes to: AKR1C3 antibody
- Gene:
- AKR1C3 NIH gene
- Name:
- aldo-keto reductase family 1 member C3
- Previous symbol:
- HSD17B5
- Synonyms:
- KIAA0119, DDX, HAKRB, PGFS
- Chromosome:
- 10p15.1
- Locus Type:
- gene with protein product
- Date approved:
- 1998-09-29
- Date modifiied:
- 2016-10-05
Related products to: AKR1C3 antibody
Related articles to: AKR1C3 antibody
- Conventional allele specific PCR (AS-PCR) genotyping using gel electrophoresis and ethidium bromide (EtBr) is costly, particularly in developing countries. It also poses health risks to working personnel as it requires specialized equipment and toxic dyes like ethidium bromide. Hence, the present study developed a simple and cost-effective colorimetric genotyping method using gold nanoparticles solution (AuNPs) and unmodified primers. Specifically, 15μl of AuNPs solution was found sufficient for detecting an amplicon in 5μl of PCR product. In this approach, the amplified PCR products appear red while the non-amplified PCR products appear blue with a PCR mastermix without a dye. Transmission Electron Microscopy (TEM) revealed the sequestration of AuNPs in amplified PCR products and the aggregation of AuNPs in non-amplified PCR products, resulting in red and blue colors, respectively. The method was tested on genotyping of six SNPs from six genes (Akr1c3, Plg, Myf5, Sec14l2, Tpm1, and Lama2) in buffaloes, and the results were perfectly matched with those obtained using agarose gel electrophoresis analysis. Therefore, the AS-PCR combined with AuNPs provides an easy visual detection method for the amplified and non-amplified PCR products of single-nucleotide polymorphisms (SNPs). In addition, the presented method has the potential to replace agarose gel electrophoresis, the use of EtBr, and UV-transilluminator. - Source: PubMed
Publication date: 2026/05/02
Verma Surya KantKumar Lal KrishanMitra Murli DharKumar JitendraSingh PrashantMohiddin RoshanNayan VarijSingh DheerOnteru Suneel Kumar - Developing targeted antitumor agents with minimal systemic toxicity is highly desirable. Exatecan, a potent camptothecin derivative, is clinically restricted due to its toxicity and limited efficacy. Targeting the tumor-enriched enzyme AKR1C3 enables selective drug activation. We designed two novel AKR1C3-responsive Exatecan conjugates, EP-1 and EP-2, with a fluorescence-quenched module for real-time "turn-on" tracking of drug release. The conjugates exhibited potent cytotoxicity in AKR1C3-high cancer cells (IC: 7.7 ± 0.2 nM for EP-1, 4.6 ± 0.4 nM for EP-2), similar to Exatecan, but markedly reduced toxicity in AKR1C3-low and normal cells, and overcame sorafenib resistance. Cellular and zebrafish imaging confirmed a targeted release. In a mouse model, EP-2 displayed potent efficacy with significantly reduced systemic toxicity (MTD > 60 mg/kg) compared to Exatecan. These results nominate EP-2 as an ideal candidate for selective and safe tumor therapy, providing a new paradigm for biomarker-driven antitumor drug design. - Source: PubMed
Publication date: 2026/05/02
Kang NingfangLiu ShuainanLi XiaoyuLuo RuxiangChen WenyanRan ChongzhaoWang PengYang Jing - Ferroptosis, an iron-dependent form of programmed cell death driven by lipid peroxidation, represents a new potential therapeutic target in cancer. However, emerging evidence indicates that hepatocellular carcinoma (HCC) frequently exhibits resistance to ferroptosis induction, while the underlying molecular mechanism is poorly understood. Here, we found that aldo-keto reductase family 1 member C3 (AKR1C3), a protein highly expressed in ferroptosis-resistant HCC cells, negatively regulates ferroptosis in an enzyme-independent manner. Mechanistically, AKR1C3 promotes ubiquitin-proteasomal degradation of the transferrin receptor (TFRC), which is indispensable for cellular iron uptake. AKR1C3 knockdown restores TFRC expression, increases the level of labile iron pool, and sensitizes HCC cells to ferroptosis. Furthermore, AKR1C3 acts as a scaffolding protein to promote the degradation of TFRC and reduce iron uptake by promoting nuclear export of Beta-transducin repeats-containing proteins (β-TrCP) and its binding to TFRC. Notably, AKR1C3 is upregulated in NRF2-driven sorafenib-resistant HCC, and its inhibition reversed ferroptosis and sorafenib resistance. Our work uncovers AKR1C3 suppresses ferroptosis in HCC by promoting β-TrCP-mediated TFRC degradation, positioning AKR1C3 as a promising therapeutic target to enhance ferroptosis-based anticancer strategies. - Source: PubMed
Publication date: 2026/05/02
Qi LeiHua JingyiPan DiYang WanwanTian GengYe FangyuLiu LingxiangMao YuhanGuo QinglongSun HaopengZhao Li - Sepiapterin reductase (SPR) catalyzes several key steps in the biosynthesis of tetrahydrobiopterin (BH4), an essential cofactor for nitric oxide synthases and aromatic amino acid hydroxylases, and therefore for neurotransmitter production. Although several reductases-including carbonyl reductase 1 (CBR1), aldose reductase (AKR1B1), and AKR1C3-can substitute for SPR activity in vitro, their physiological significance remains unresolved. This study examines AKR1C3 as a component of an alternative BH4-generating pathway and evaluates its capacity to compensate for BH4 loss under diminished SPR activity. In vitro assays identified 2'-OXPH4 as the primary product of AKR1C3, redirecting pathway flux away from the canonical 1'-OXPH4 intermediate and the sepiapterin-salvage pathway. To assess the occurrence and efficiency of this route in cells, we generated SPR-knockout (SPR-KO) cell and evaluated pathway products in SPR-KO and wild-type (WT) backgrounds. In WT cells neither AKR1C3 nor SPR overexpression altered BH4 synthesis, indicating that neither enzyme is rate-limiting. In contrast, AKR1C3 increased BH4 levels in SPR-KO cells, while inhibiting sepiapterin production, revealing that AKR1C3 becomes functionally engaged only when SPR activity is decreased. Based on relative enzyme abundance, AKR1C3 and SPR exhibited comparable catalytic efficiency in this context. Importantly, AKR1C3-mediated BH4 production was sufficient to sustain tyrosine hydroxylase (TH) activity in SPR-KO cells, as demonstrated by L-DOPA formation. These findings establish AKR1C3-driven 2'-OXPH4 synthesis as a bona fide, inducible pathway capable of maintaining BH4 levels when SPR activity is limiting. This alternative path provides a compelling therapeutic target and introduces a new diagnostic consideration for patients with diminished SPR activity. - Source: PubMed
Publication date: 2026/04/29
Woodcock JamesTan SidharthaVasquez-Vivar Jeannette - Kaempferol has been shown to be beneficial in the treatment of Alzheimer's disease (AD) in animal models. However, the action mechanism remains unclear. AKR1B1 has been identified as a target of kaempferol, initially suggested by the Therapeutic Target Database, DrugBank, and PubChem, and subsequently confirmed through experimental validation. Kaempferol treatment facilitated the expression of AKR1B1 in PC12 cells exposed to Aβ. Kaempferol treatment mitigated the Aβ-induced increases in Fe, MDA, and lipid ROS and Aβ-induced decreases in GSH synthesis and SOD activity. The reduction in ferroptosis-related proteins (GPX4, NQO1, SLC7A11, AKR1C1, and AKR1C3) and the inhibition of Nrf2 nuclear translocation and Nrf2/HO-1 signaling caused by Aβ were also reversed by kaempferol. Overexpressing AKR1B1 led to decreased levels of Fe, MDA, and lipid ROS, along with increased GSH synthesis and SOD activity in Aβ-treated cells, although these effects were negated by Nrf2 inhibition. The upregulation of GPX4 and AKR1C3 by AKR1B1 overexpression was also reversed when Nrf2 expression was inhibited. Notably, silencing AKR1B1 counteracted the protective effects of kaempferol against Aβ-induced neuronal ferroptosis. In vivo studies revealed that kaempferol improved cognitive impairments, reduced deposition of Aβ and p-Tau, and alleviated neuronal ferroptosis in the hippocampal tissues of an AD mouse model in a dose-dependent manner, effects that were diminished by inhibiting AKR1B1 expression. Following kaempferol treatment, the levels of GPX4 and AKR1C3 in the hippocampus of AD mice were found to be reduced. Overall, our findings indicate that kaempferol treatment enhances cognitive function and mitigates pathological alterations in AD mice by inhibiting neuronal ferroptosis through the activation of the Nrf2/HO-1/GPX4/AKR1C3 signaling via upregulation of AKR1B1. This research supports the need for further investigation and clinical exploration of kaempferol. - Source: PubMed
Li LeYang ManyingTao JialeZhao YonghongZhao NaSun Shiguo