TIM50
- Known as:
- TIM50
- Catalog number:
- Y213388
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- TIM50
Related genes to: TIM50
- Gene:
- TIMM50 NIH gene
- Name:
- translocase of inner mitochondrial membrane 50
- Previous symbol:
- -
- Synonyms:
- TIM50L
- Chromosome:
- 19q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 2003-12-02
- Date modifiied:
- 2016-03-07
Related products to: TIM50
Antibodies: TIM50 HOST: Goat Clonality: pAbBos taurus,Bovine,Mitochondrial import inner membrane translocase subunit TIM50,TIM50,TIMM50Bovine Mitochondrial import inner membrane translocase subunit TIM50(TIMM50) ELISA kitBovine Mitochondrial import inner membrane translocase subunit TIM50(TIMM50) ELISA kitBovine Mitochondrial import inner membrane translocase subunit TIM50(TIMM50) ELISA kit SpeciesBovineCanine Mitochondrial import inner membrane translocase subunit TIM50(TIMM50) ELISA kitCanine Mitochondrial import inner membrane translocase subunit TIM50(TIMM50) ELISA kitChicken Mitochondrial import inner membrane translocase subunit TIM50(TIMM50) ELISA kitELISA Kit FOR Mitochondrial import inner membrane translocase subunit TIM50; organism: Mouse; gene name: Timm50GOAT ANTI HUMAN TIM50 Polyclonal Antibody Host: Goat Polyclonal IgGGOAT ANTI HUMAN TIM50, Product Type Polyclonal Antibody, Specificity TIM50, Target Species Human, Host Goat, Format Purified, Isotypes Polyclonal IgG, Applications E, WB, CloneGOAT ANTI HUMAN TIM50, Product Type Polyclonal Antibody, Specificity TIM50, Target Species Human, Host Goat, Format Purified, Isotypes Polyclonal IgG, Applications E, WB, CloneGOAT ANTI HUMAN TIM50-POLYCLONAL ANTIBODYGoat Anti-Human TIM50, (internal region) AntibodiesGuinea pig Mitochondrial import inner membrane translocase subunit TIM50(TIMM50) ELISA kit Related articles to: TIM50
- Previous studies have demonstrated the detrimental effects of lactate on patients with esophageal squamous cell carcinoma (ESCC). In this study, six lactate-related hub genes (SLC16A7, GFM1, PDP1, TRMT5,COX5A, and KIF23) were identified in ESCC. Significant differences were observed in various immune cell populations, including naive B cells and memory B cells, between ESCC and normal samples. scRNA-seq analysis revealed distinct cell subpopulations, such as T cells, fibroblasts, and epithelial cells. The lactylation score was notably greater in the ESCC samples than in the normal samples. Further comparison of lactylation scores across subpopulations revealed significantly elevated levels of monocytes, B cells, epithelial cells, and neutrophils in ESCC samples, whereas T cells and fibroblasts had higher scores in normal samples. CellChat analysis revealed that lactylation-associated subpopulations, particularly epithelial and immune cells, presented increased intercellular communication in the high-lactylation group. Additionally, KIF23, TRMT5, TEFM, SLC25A13, TIMM50, DGUOK, DNM1L and COX5A exhibited trends consistent with expectations in the two ESCC cell lines. This study identified six hub genes relevant to ESCC, offering a theoretical foundation for potential therapeutic approaches in ESCC. - Source: PubMed
Publication date: 2025/07/05
Wang XianbingJiang JiayingHe HongjieWang Yi - Mitochondrial dysfunction is an irrefutable hallmark of cellular senescence and aging. The dysfunction is marked by increased mitochondrial volume and reduced function, typified by low Adenosine Triphosphate (ATP) production and higher Reactive Oxygen Species (ROS) generation. Over the years, this dysfunction has been linked to Electron Transport Chain (ETC) malfunction and low NAD levels, augmented by poor mitophagy. However, the genetic regulation of mitochondrial dysfunction is still not clear. Here, using several senescence models, the first report on the role of the downregulation of a mitochondrial protein, Translocase of Inner Mitochondrial Membrane 50 (TIMM50), in senescence is presented. The downregulation of TIMM50 is also sufficient for triggering senescence through impaired mitochondrial function, characterized using a variety of mitochondrial function assessment assays. Reduced levels of TIMM50 initiated all the hallmarks of senescence, and overexpression significantly slowed senescence onset in response to an external trigger. The pathway analysis revealed that TIMM50 loss is mediated by the sirtuin1-dependent downregulation of CCAAT enhancer binding protein alpha (CEBPα), a transcription activator for TIMM50 expression. To establish the translational value of the observation, screening several potential anti-aging compounds revealed TIMM50 stabilizing and senescence-delaying effects only for verapamil and mitochondrial ROS quencher, Mito (2-(2,2,6,6-Tetramethylpiperidin-1-oxyl-4-ylamino)-2-oxoethyl)triphenylphosphonium chloride (MitoTEMPO), both known anti-aging entities. Overall, TIMM50 is identified as the key mitochondrial protein whose downregulation is a critical step in initiating cellular senescence. - Source: PubMed
Publication date: 2025/03/24
Nepalia AmritaSaini Deepak Kumar - The human mitochondrial proteome comprises approximately 1500 proteins, with only 13 being encoded by mitochondrial DNA. The remainder are encoded by the nuclear genome, translated by cytosolic ribosomes, and subsequently imported into and sorted within mitochondria. The process of mitochondria-destined protein import is mediated by several intricate protein complexes distributed among the four mitochondrial compartments. The focus of this mini-review is the translocase of the inner membrane 23 (TIM23) complex that assists in the import of ~60% of the mitochondrial proteome, which includes the majority of matrix proteins as well as some inner membrane and intermembrane space proteins. To date, numerous pathogenic mutations have been reported in the genes encoding various components of the TIM23 complex. These diseases exhibit mostly developmental and neurological defects at an early age. Interestingly, accumulating evidence supports the possibility that the gene for Tim50 represents a hotspot for disease-causing mutations among core TIM23 complex components, while genes for the mitochondrial Hsp70 protein (mortalin) and its J domain regulators represent hotspots for mutations affecting presequence translocase-associated motor (PAM) subunits. The potential mechanistic implications of the discovery of disease-causing mutations on the function of the TIM23 complex, in particular Tim50, are discussed. - Source: PubMed
Publication date: 2024/11/28
Jain SahilPaz EyalAzem Abdussalam - TIMM50, an essential TIM23 complex subunit, is suggested to facilitate the import of ~60% of the mitochondrial proteome. In this study, we characterized a disease-causing mutation in human fibroblasts and noted significant decreases in TIM23 core protein levels (TIMM50, TIMM17A/B, and TIMM23). Strikingly, TIMM50 deficiency had no impact on the steady-state levels of most of its putative substrates, suggesting that even low levels of a functional TIM23 complex are sufficient to maintain the majority of TIM23 complex-dependent mitochondrial proteome. As TIMM50 mutations have been linked to severe neurological phenotypes, we aimed to characterize TIMM50 defects in manipulated mammalian neurons. TIMM50 knockdown in mouse neurons had a minor effect on the steady state level of most of the mitochondrial proteome, supporting the results observed in patient fibroblasts. Amongst the few affected TIM23 substrates, a decrease in the steady state level of components of the intricate oxidative phosphorylation and mitochondrial ribosome complexes was evident. This led to declined respiration rates in fibroblasts and neurons, reduced cellular ATP levels, and defective mitochondrial trafficking in neuronal processes, possibly contributing to the developmental defects observed in patients with TIMM50 disease. Finally, increased electrical activity was observed in TIMM50 deficient mice neuronal cells, which correlated with reduced levels of KCNJ10 and KCNA2 plasma membrane potassium channels, likely underlying the patients' epileptic phenotype. - Source: PubMed
Publication date: 2024/12/16
Paz EyalJain SahilGottfried IritStaretz-Chacham OrnaMahajnah MuhammadBagchi PrithaSeyfried Nicholas TAshery UriAzem Abdussalam - Microglia are resident immune cells of the brain and regulate its inflammatory state. In neurodegenerative diseases, microglia transition from a homeostatic state to a state referred to as disease-associated microglia (DAM). DAM express higher levels of proinflammatory signaling molecules, like STAT1 and TLR2, and show transitions in mitochondrial activity toward a more glycolytic response. Inhibition of Kv1.3 decreases the proinflammatory signature of DAM, though how Kv1.3 influences the response is unknown. Our goal was to identify the potential proteins interacting with Kv1.3 during transition to DAM. We utilized TurboID, a biotin ligase, fused to Kv1.3 to evaluate potential interacting proteins with Kv1.3 via mass spectrometry in BV-2 microglia following TLR4-mediated activation. Electrophysiology, Western blotting, and flow cytometry were used to evaluate Kv1.3 channel presence and TurboID biotinylation activity. We hypothesized that Kv1.3 contains domain-specific interactors that vary during a TLR4-induced inflammatory response, some of which are dependent on the PDZ-binding domain on the C terminus. We determined that the N terminus of Kv1.3 is responsible for trafficking Kv1.3 to the cell surface and mitochondria (e.g., NUDC, TIMM50). Whereas, the C terminus interacts with immune signaling proteins in a lipopolysaccharide-induced inflammatory response (e.g., STAT1, TLR2, and C3). There are 70 proteins that rely on the C-terminal PDZ-binding domain to interact with Kv1.3 (e.g., ND3, Snx3, and Sun1). Furthermore, we used Kv1.3 blockade to verify functional coupling between Kv1.3 and interferon-mediated STAT1 activation. Overall, we highlight that the Kv1.3 potassium channel functions beyond conducting the outward flux of potassium ions in an inflammatory context and that Kv1.3 modulates the activity of key immune signaling proteins, such as STAT1 and C3. - Source: PubMed
Publication date: 2024/06/25
Bowen Christine ANguyen Hai MLin YoungBagchi PrithaNatu AdityaEspinosa-Garcia ClaudiaWerner EricaKumari RashmiBrandelli Amanda DabdabKumar PrateekTobin Brendan RWood LeviFaundez VictorWulff HeikeSeyfried Nicholas TRangaraju Srikant