SLC7A5 antibody, Polyclonal Antibodies, Host Rabbit
- Known as:
- SLC7A5 (anti-), Polyclonal Antibodies, Host Rabbit
- Catalog number:
- 20R-SR026
- Product Quantity:
- 50 ug
- Category:
- -
- Supplier:
- Fitzgerald
- Gene target:
- SLC7A5 antibody Polyclonal Antibodies Host Rabbit
Related genes to: SLC7A5 antibody, Polyclonal Antibodies, Host Rabbit
- Gene:
- SLC7A5 NIH gene
- Name:
- solute carrier family 7 member 5
- Previous symbol:
- -
- Synonyms:
- LAT1, E16, D16S469E, MPE16, CD98
- Chromosome:
- 16q24.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-01-28
- Date modifiied:
- 2016-10-05
Related products to: SLC7A5 antibody, Polyclonal Antibodies, Host Rabbit
Related articles to: SLC7A5 antibody, Polyclonal Antibodies, Host Rabbit
- Hepatocellular carcinoma (HCC) cells are metabolically reprogrammed for excessive uptake and metabolism of many nutrients. The tumor suppressive microRNA-148a-3p (miR-148a-3p) is downregulated in HCC, whereas its function in regulating HCC cell metabolism remains obscure. Herein we aimed to delineate the role of miR-148a-3p in HCC cell metabolism by using novel bioengineered miR-148a-3p (BioRNA/miR-148a-3p) agent produced . - Source: PubMed
Publication date: 2026/04/08
Guan SuLi XinWang YimeiTu Mei-JuanYu Ai-Ming - Left ventricular hypertrophy (LVH) is a major complication of chronic hypertension and an independent cardiovascular risk factor. No clinically validated markers exist to identify hypertensive individuals at risk for developing LVH. We previously described metabolic changes preceding LVH in hypertensive rat hearts, including alterations in branched-chain amino acid (BCAA) metabolism. This study investigated whether impaired cardiac leucine uptake, measured with dynamic 5-[F]fluoroleucine ([F]FLE) PET imaging, could serve as marker for hypertension-induced LVH development. - Source: PubMed
Publication date: 2026/06/18
Terrell WilliamLi JieKommi Damodara NBurt MeganJansen Maurits AKhanapur ShivashankarKeller Susanna RKundu Bijoy - Brain microvascular endothelial cells (BMECs) form the blood-brain barrier (BBB), a highly selective interface that restricts paracellular diffusion and regulates the transport of nutrients and drugs into the central nervous system via specialized transporters and receptors. Tight junction-associated protein 1 (Tjap1), also termed protein incorporated later into tight junctions (Pilt), has been localized to tight junctions (TJs) in epithelial cells and to the trans-Golgi network in fibroblasts; however, its expression, subcellular localization, and functional significance in BMECs are still unknown. We characterized Tjap1 subcellular localization in mouse and human BMEC cell lines as well as primary mouse BMECs by immunofluorescence with and without pharmacological Golgi disruption by treatment with Brefeldin A, Golgicide A or Pitstop 2. CRISPR/Cas9-mediated Tjap1 knockout cells were generated and examined with regard to their Golgi morphology using immunostaining. Tjap1 mRNA localization was examined by RNAscope in situ hybridization. Quantitative real-time PCR and Western blot was performed to assess the expression of BBB-associated efflux transporters, solute carrier transporters, and cellular receptors in control and Tjap1 knockout cells. Tjap1 predominantly localized to the cis-Golgi compartment, co-localizing with Gm130 rather than Tgn38, and was absent from TJs in BMECs. Tjap1 knockout induced pronounced Golgi fragmentation BMECs. Importantly, Tjap1 knockout significantly downregulated mRNA-expression of Abcb1a, Abcb1b, Abcc4, Slc2a1, Slc7a1, Slc7a5 and Tfrc, while Abcg2 was upregulated. At the protein level, a decrease in the protein levels of Abcb1, Abcc4, Slc2a1, Slc7a1, and Tfrc was observed in Tjap1 knockout cEND cells. In BMECs, Tjap1 is a cis-Golgi-associated protein required for the structural integrity of the Golgi apparatus. Its deletion is associated with Golgi fragmentation and significant alterations in the mRNA and protein expression of drug transporters and receptors at the BBB. These findings identify Tjap1 as a candidate regulator of both Golgi architecture and the BBB transporter profile in vitro, with potential implications for modulating drug transport across the BBB. - Source: PubMed
Publication date: 2026/05/28
Mi JunqiaoSchoder AnnabelleSun AiliMeybohm PatrickBurek Malgorzata - Metabolic reprogramming within the tumor microenvironment (TME) limits the efficacy of chemo-immunotherapy in triple-negative breast cancer (TNBC). Despite advances in high-resolution profiling, the specific intercellular metabolic crosstalk driving immune evasion remains incompletely understood. Here, we present a comprehensive single-cell metabolic atlas of the TNBC ecosystem to decode spatial and cell-type-specific metabolic vulnerabilities. Our multidimensional analysis reveals a distinct paracrine metabolic communication axis: CXCL9 macrophages upregulate rate-limiting enzymes (IDO1/2) to become a potential source of local kynurenine, which is subsequently imported by cytotoxic T cells. Through in vitro co-culture and in vivo models, we demonstrate that this kynurenine uptake triggers impaired effector function and phenotypic exhaustion. Crucially, pharmacological blockade of SLC7A5 with the specific inhibitor JPH203 abrogates this metabolic toxicity, restores T cell effector function, and enhances the anti-tumor efficacy of combined cisplatin and anti-PD-1 therapy. Collectively, our findings delineate the Kynurenine-SLC7A5 metabolic axis as a critical driver of immunosuppression, providing a compelling rationale for integrating amino acid transport blockade to overcome resistance to chemo-immunotherapy. - Source: PubMed
Publication date: 2026/06/25
Zhong SenYu BolinZhou ShengyiChen WenlongLiu FanglongZhu HuanhuanMin FangQian Fengyuan - Reprogramming of amino acid metabolism is crucial for the rapid proliferation of cancer cells, including cancer stem cells. However, the molecular mechanisms underlying this reprogramming in glioma stem cells (GSCs) remain poorly understood. Here, we report that the RNA-binding protein RBM12 increases the intracellular levels of large neutral amino acids, thereby activating the mTORC1 pathway and promoting GSC proliferation, self-renewal, and glioblastoma (GBM) growth. Mechanistically, RBM12 stabilizes the mRNA of the amino acid transporter SLC7A5, thereby increasing intracellular levels of large neutral amino acids, which subsequently activates the mTORC1 pathway. Further studies reveal that RBM12 enhances SLC7A5 mRNA stability by recruiting ALKBH5 to remove mA modifications on SLC7A5 mRNA. Importantly, pharmacological inhibition of the RBM12-SLC7A5 axis using the SLC7A5 inhibitor JPH203 effectively suppresses GBM growth. These findings elucidate a novel role for RBM12-SLC7A5 signaling in the malignant growth of GBM and highlight the therapeutic potential of targeting this axis for GBM treatment. - Source: PubMed
Publication date: 2026/06/22
Lei HongLuo WenlongZhou ShuWan LihaoLing PengHuang ZhihuaQian ZhihuaLu ChenfeiGuo MengyueXue ZhenQin JunZhao NingweiMan JianghongZhou WenchaoDong ZhiqiangXu ShutongZhou ZhipengWang XiuxingTao Weiwei