AK3L1 Blocking Peptide
- Known as:
- AK3L1 Blocking Peptide
- Catalog number:
- 33r-8265
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- AK3L1 Blocking Peptide
Related genes to: AK3L1 Blocking Peptide
- Gene:
- AK3 NIH gene
- Name:
- adenylate kinase 3
- Previous symbol:
- AK6, AK3L1
- Synonyms:
- AKL3L1
- Chromosome:
- 9p24.1
- Locus Type:
- gene with protein product
- Date approved:
- 2002-12-17
- Date modifiied:
- 2014-11-19
- Gene:
- AK4 NIH gene
- Name:
- adenylate kinase 4
- Previous symbol:
- AK3, AK3L1
- Synonyms:
- -
- Chromosome:
- 1p31.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2014-11-19
Related products to: AK3L1 Blocking Peptide
Related articles to: AK3L1 Blocking Peptide
- αβ Nicotinic acetylcholine receptor (nAChR) has been recognized as an emerging biomarker for the early detection of drug addiction. Herein, αβ nAChR ligands were designed and synthesized to improve the binding affinity and selectivity of two lead compounds, - and -, for the development of an αβ nAChR tracer. The structural modification was achieved by retaining the key features and expanding the molecular structure with a benzyloxy group to increase the lipophilicity for blood-brain barrier penetration and to extend the ligand-receptor interaction. The preserved key features are a fluorine atom for radiotracer development and a -hydroxyl motif for ligand-receptor binding affinity. Four ()- and ()-quinuclidine-triazole (-) were synthesized and the binding affinity, together with selectivity to αβ nAChR subtype, were determined by competitive radioligand binding assay using [H]epibatidine as a radioligand. Among all modified compounds, showed the highest binding affinity and selectivity to αβ nAChR with a value of 3.18 nM, comparable to - and - and 3069-fold higher affinity to αβ nAChR in comparison to α nAChR. The αβ nAChR selectivity of was considerably higher than those of - (11.8-fold) and - (294-fold). was shown to be a promising αβ nAChR tracer for further development as a radiotracer for drug addiction. - Source: PubMed
Publication date: 2023/02/10
Kanasuwan ApinanDeuther-Conrad WinnieChongruchiroj SumetSarasamkan JiradanaiChotipanich ChanisaVajragupta OpaArunrungvichian Kuntarat - Textile wastewater contains dyes mixed with other contaminants in various concentrations. Bacteria-mediated decolorization and degradation of azo dyes have achieved momentum as a method of treatment attributed to their inexpensive, eco-friendly, and application to a wide range of azo dyes. However, a single species of bacteria is inefficient in decolorizing diverse groups of dyes which is one of the most significant challenges for environmental technologists working in bioremediation. In the present study, an aerobic bacterial consortium AUJ consisting of six different bacterial strains (Pseudomonas stutzeri AK1, Pseudomonas stutzeri AK2, Pseudomonas stutzeri AK3, Bacillus spp. AK4, Pseudomonas stutzeri AK5, and Pseudomonas stutzeri AK6) removed the individual azo dyes in the 24-94% range when used in more than 200 ppm concentration within 72-96 h. In addition, the consortium was able to decolorize 52.19% mixed dyes (100 ppm) and 44.55% Acid blue 113 when used at a concentration as high as 1100 ppm within 96 h. Optimization of various nutritional and environmental parameters revealed that glucose and yeast extract were the preferred carbon and nitrogen source, respectively, and analysis of treated dye products using high-performance liquid chromatography (HPLC), Fourier-transform infrared spectroscopy (FTIR), and gas chromatography-mass spectrometry (GC-MS) confirmed the breakdown of dye. In all, we present a bacterial consortium with a good ability of dye decolorization that can be used for degrading a wide variety of azo dyes. - Source: PubMed
Publication date: 2022/07/22
Joshi AnjaliHinsu AnkitKothari Ramesh - Adenylate kinase2 (AK2) catalyzes trans-compartmental nucleotide exchange, but the functional implications of this mitochondrial intermembrane isoform is only partially understood. Here, transgenic AK2-/- null homozygosity was lethal early in embryo, indicating a mandatory role for intact AK2 in utero development. In the adult, conditional organ-specific ablation of AK2 precipitated abrupt heart failure with Krebs cycle and glycolytic metabolite buildup, suggesting a vital contribution to energy demanding cardiac performance. Depressed pump function recovered to pre-deletion levels overtime, suggestive of an adaptive response. Compensatory upregulation of phosphotransferase AK1, AK3, AK4 isozymes, creatine kinase isoforms, and hexokinase, along with remodeling of cell cycle/growth genes and mitochondrial ultrastructure supported organ rescue. Taken together, the requirement of AK2 in early embryonic stages, and the immediate collapse of heart performance in the AK2-deficient postnatal state underscore a primordial function of the AK2 isoform. Unsalvageable in embryo, loss of AK2 in the adult heart was recoverable, underscoring an AK2-integrated bioenergetics system with innate plasticity to maintain homeostasis on demand. - Source: PubMed
Publication date: 2021/02/08
Zhang SongYamada SatsukiPark SungjoKlepinin AleksandrKaambre TuuliTerzic AndreDzeja Petras - The ciliate Paramecium tetraurelia has four arginine kinase genes (AK1, AK2, AK3, and AK4). Of these genes, only AK3 has a signal sequence for farnesylation, a post-translational modification that enables anchoring of the modified enzyme to the ciliary membrane. To confirm this modification, AK3 was synthesized using a cell-free protein synthesis system and the peptide masses were analyzed using peptide mass fingerprinting (PMF). The PMF analysis indicated that the C-terminal peptide of AK3 is farnesylated. Thus, AK3 can be farnesylated under physiologically appropriate conditions. To determine the subcellular localization of P. tetraurelia AK3, Western blot analysis was performed using an AK3 polyclonal antibody for the proteins extracted from intact cells and ciliary fractions. When extraction was performed using Triton X-100, AK3 was detected the ciliary fraction. This result suggested that the ciliary fraction contains AK3. In addition, we investigated the role of P. tetraurelia AKs in ciliary movement using the feeding RNA interference method. The swimming velocity of AK1- and AK3-silenced cells was significantly reduced to half the value of that control cells. In summary, P. tetraurelia AK3 is likely to be located in the ciliary membrane and influences swimming velocity, presumably through the phosphoarginine shuttle system present in cilia. - Source: PubMed
Publication date: 2020/04/23
Yano DaichiFunadani RyoujiUda KoujiMatsuoka TatsuomiSuzuki Tomohiko - Salinity is one of the major abiotic constraints that hinder health and quality of crops. Conversely, halotolerant plant growth-promoting rhizospheric (PGPR) bacteria are considered biologically safe for alleviating salinity stress. - Source: PubMed
Publication date: 2019/10/20
Khan Muhammad AaqilAsaf SajjadKhan Abdul LatifAdhikari ArjunJan RahmatullahAli SajidImran MuhammadKim Kyung-MinLee In-Jung