NME2 Forward PCR Primer (500bp position)
- Known as:
- NME2 Forward PCR test kit Primer (500bp position)
- Catalog number:
- MP1161
- Product Quantity:
- ea
- Category:
- -
- Supplier:
- Panomics
- Gene target:
- NME2 Forward PCR Primer (500bp position)
Related genes to: NME2 Forward PCR Primer (500bp position)
- Gene:
- NME2 NIH gene
- Name:
- NME/NM23 nucleoside diphosphate kinase 2
- Previous symbol:
- -
- Synonyms:
- NM23-H2, NDPKB
- Chromosome:
- 17q21.33
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-26
- Date modifiied:
- 2016-07-15
Related products to: NME2 Forward PCR Primer (500bp position)
Related articles to: NME2 Forward PCR Primer (500bp position)
- Enolase 2 (ENO2) is a crucial an important glycolytic enzyme involved in glycolysis and is also recognised as a multifunctional protein. However, its interacting proteins in intestinal porcine epithelial cells (IPEC-J2 cells) remain unclear. This study investigates the interacting proteins of Cystoisospora suis (Biester et Murray, 1934) ENO2 (CsENO2) in IPEC-J2 cells. According to our previous research, CsENO2 is highly expressed in sporulated oocysts. Co-immunoprecipitation/liquid chromatography-mass spectrometry (Co-IP/LC-MS) was conducted using the pcDNA3.1-Flag vector carrying the enolase 2 gene, which was transfected into IPEC-J2 cells to co-immunoprecipitate with cellular proteins. The Co-IP/LC-MS-based protein sequencing identified three cellular proteins: NME2, RPS3, and Vimentin. Subsequently, cDNAs encoding the complete coding sequences of these proteins were cloned into the pGEX-4T-1 expression vector. Immunofluorescence assays revealed the localisation of CsENO2 in sporulated oocysts and sporozoites. Most CsENO2 protein was found in the cytoplasm of sporulated oocysts. In sporozoites, CsENO2 protein was primarily distributed around and outside the nucleus. This study aims to identify CsENO2-interacting proteins in IPEC-J2 cells and determine the localisation of CsENO2 within sporulated oocysts and sporozoites. - Source: PubMed
Publication date: 2026/08/31
Chiu Hung-ChuanAo YuhaoTang Yaoxue - Performing selective proton-coupled electron transfer (PCET) to substrates such as N2, CO2, and unsaturated organic molecules under electrochemical conditions requires the suppression of the competing hydrogen evolution reaction (HER). To address this challenge, our laboratory previously demonstrated a PCET mediator strategy using a dimethylaniline-appended cobaltocene complex, [(CpCoCpNMe2)H]+, which performs selective reductive chemistry while suppressing the HER. However, the origin of the suppressed, yet still observable, HER has not been thoroughly established. In this work, we perform density functional theory (DFT) calculations to elucidate the HER mechanism involving this redox mediator and to provide atomistic insights into the bifurcation between the PCET and HER pathways. We find that protonation of the aniline moiety to form [CpCoCpNMe2H]+ is more favorable, both kinetically and thermodynamically, than formation of the ring-protonated species [(CpCo(Cp-H)NMe2)]+. Furthermore, PCET to acetophenone is energetically more favorable via [CpCoCpNMe2H]+ than via [(CpCo(Cp-H)NMe2)]+1/0. In contrast, the most favorable HER pathway involves the ring-protonated Co(I) species. These results offer mechanistic insights into HER versus PCET bifurcation and establish guiding principles for designing PCET mediators for selective electroreductive transformations. - Source: PubMed
Banerjee SayanPeters Jonas C - We report the synthesis of a new family of chiral dipicolinamide systems presenting an extended π-conjugated backbone connecting an electron-donating group (─NMe) to a pyridine unit. The chirality is introduced on the amide chains located at positions 2 and 6 of the pyridine, by employing commercially available enantiopure amines. Besides the good quantum yields shown in solution (up to 15%), two of the synthesized molecules are endowed with nonreciprocal chiroptical properties when they form thin films on a glass substrate, showing a strong circularly polarized luminescence with |g| values as high as 0.06. - Source: PubMed
Publication date: 2026/08/31
Petri FilippoGherardi LucaBari Lorenzo DiArrico Lorenzo - Renal cell carcinoma (RCC), particularly the clear cell subtype (ccRCC), is a prevalent malignancy characterized by aggressive progression and heterogeneous therapeutic responses. Although mitochondrial dynamics are increasingly recognized as critical regulators of cancer metabolism and survival, the role of nucleoside diphosphate kinase 3 (NME3) in this process remains poorly understood. In this study, we integrated bioinformatic analyses of public datasets with validation in patient-derived tissues, in vitro functional assays, and in vivo xenograft models to elucidate the role of NME3 in ccRCC. We found that NME3 is significantly upregulated in ccRCC and correlates with poor survival, serving as an independent prognostic factor. Functionally, NME3 knockdown suppresses proliferation, migration, invasion, and xenograft tumor growth, while its overexpression promotes malignant phenotypes. Mechanistic investigations revealed that NME3 knockdown induces mitochondrial fragmentation, reduces ATP production, increases reactive oxygen species (ROS) levels, and activates PINK1/Parkin-mediated mitophagy; whereas NME3 overexpression enhances mitochondrial fusion and oxidative phosphorylation. Further analyses revealed that NME3 forms homomeric or heteromeric hexamers with NME2 and interacts with the mitochondrial fusion regulators MFN1 and MFN2 to facilitate mitochondrial fusion. Importantly, NME3 expression modulated the cellular response to tyrosine kinase inhibitors (TKIs), including sorafenib and sunitinib, with NME3 depletion enhancing drug sensitivity in vitro and in xenograft models. Collectively, these findings identify NME3 as a regulator of mitochondrial dynamics in ccRCC and highlight a potential link between mitochondrial remodeling and therapeutic response. - Source: PubMed
Publication date: 2026/07/10
Cao SenmingChen XinranZhang ChiFeng YiShi ChangweiWang JichenXu QingjiangHuang XingMa XinFan Wenmei - Developing multifunctional redox mediators (RMs) is critical for mitigating cathode passivation, parasitic reactions, and high discharge overpotential in Li-O batteries. While the computational studies of RMs relied on gas-phase electronic descriptors, here, we investigate through explicit-solvent ab initio molecular dynamics (AIMD) that the solution-phase mechanism is governed by previously unrecognized solvation-dependent coordination site exchange dynamics. Using benzo[1,2-b:4,5-b'] dithiophene-4,8-dione (BDTD) as a model RM across varying electrolyte environments with dimethyl ether (DME), Dimethyl sulfoxide (DMSO), and acetonitrile (ACN) solvents, we uncover a unique mechanistic divergence. In bidentate solvents like DME, a flexible coordination rearrangement enables the spontaneous formation of a BDTD:Li complex via a transient trigonal-bipyramidal intermediate. Conversely, this process is sterically hindered in monodentate solvents (DMSO and ACN), forcing the reaction to proceed via a significantly slower solvent-reorganization pathway. The flexibility is absent in monodentate solvents, such as DMSO and ACN. The complex formation in the DME environment proceeds through coordination rearrangement site exchange phenomena, whereas in DMSO and ACN, it proceeds through solvent reorganization phenomena. The descriptor for controlling redox activity evaluated by screening 18 BDTD derivatives with various substituents (-NMe, -NH, -Me, -OMe, -OH, -Cl, -CN, -NO, and -COOH) at two positions is systematically evaluated. Structure-property relationships show that the nature of the substituent, positional effects, hydrogen bonding, and reduced state stability collectively govern the reduction potential and discharge overpotential. One of the positioned -COOH functionalized BDTD provides bidentate coordination, stabilizing the reduced state and leading to a more favorable redox shift and lower overpotential. RM activity cannot be predicted solely by LUMO energy; instead, a combined descriptor involving electronic effects, substitution position, and reduced-state stabilization is required. These results establish a new framework for RM chemistry, shifting the design paradigm from simple electronic tuning to the active management of the dynamic solvation shell, providing a blueprint for the next generation of high-efficiency electrochemical energy storage. - Source: PubMed
Publication date: 2026/07/01
Behera Bibhuti BhusanMallik Bhabani S