NAGK Antibody (C-term)
- Known as:
- NAGK Antibody (C-terminus)
- Catalog number:
- AP7080b
- Category:
- -
- Supplier:
- Abgen
- Gene target:
- NAGK Antibody (C-term)
Related genes to: NAGK Antibody (C-term)
- Gene:
- NAGK NIH gene
- Name:
- N-acetylglucosamine kinase
- Previous symbol:
- -
- Synonyms:
- GNK
- Chromosome:
- 2p13.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-11-16
- Date modifiied:
- 2016-04-25
Related products to: NAGK Antibody (C-term)
Related articles to: NAGK Antibody (C-term)
- MYCN gene copy number in neuroblastoma tissue sections is a well-established prognostic parameter used to guide clinical risk stratification. Nevertheless, the majority of neuroblastoma cases are identified at late stages, when tumors are bulky and unresectable, precluding safe tissue sampling through surgery or core biopsy and thereby compromising the accuracy of molecular risk assessment. To address this critical diagnostic challenge, we have developed a nonbiopsy fluorescent signal conversion strategy capable of detecting MYCN amplification status without relying on tissue biopsies. The core of this method is a DNA-based biosensor based on cascade cyclic amplification (CCA), which undergoes conformational activation upon specific hybridization with intracellular MYCN or NAGK mRNA, releasing tunable fluorescent signals. The normalized fluorescence intensity ratio (referred to as the M/N ratio) quantitatively reflects the MYCN copy number status. This CCA system integrates two orthogonal functional modules-MYCN-CCA and NAGK-CCA-both exploiting elevated cytoplasmic APE1 activity in pathologically altered neuroblastoma cells as a tumor-specific molecular switch and endogenous enzymatic amplifier. APE1-mediated interactions trigger structural changes that drive the dissociation of fluorophore from quencher, generating stable and quantifiable fluorescent signals. Analytical validation demonstrates exceptional sensitivity, with detection limits of 0.52 aM for MYCN mRNA and 0.65 aM for NAGK mRNA. Importantly, the CCA platform enables precise quantification of the M/N ratio in both cell line-derived and patient-derived xenograft models, and allows rapid in situ evaluation in frozen sections of clinical neuroblastoma samples. Collectively, this work introduces a biopsy-independent detection scheme for MYCN amplification, which holds promise for broad deployment in precision medicine and routine diagnostics. - Source: PubMed
Publication date: 2026/09/15
Sun ShiyaoTian ZhenzhenZhang XianweiZhao NaLi ZirongZhang MengxinSun MengYang JunWang PengZhang Wancun - N-Acetyl-L-glutamate kinase of Prasinoderma coloniale is an example of an evolutionary hack that allows this alga survival without the protein PII. N-Acetyl-L-glutamate kinase (NAGK) catalyzes the phosphorylation of N-acetyl-L-glutamate to N-acetyl-L-glutamyl-phosphate, which is the rate-limiting step in the ornithine/arginine biosynthesis pathway. In cyanobacteria and Archaeplastida, NAGK activity is strictly regulated by the end product, arginine (Arg), and is controlled by the PII signaling protein. During evolution, Prasinoderma coloniale, a phytoplankton species from an early-branching lineage within the Archaeplastida, lost the gene encoding PII protein. PcNAGK shows a unique feature: it has evolved to be an enzyme that is virtually insensitive to intracellular levels of Arg with an IC of 9.5 mM. Using molecular and biochemical characterization, we demonstrated that substitution of amino acids Lys24 with Gln and Ile282 with Glu restored the sensitivity of the recombinant PcNAGK protein to Arg. Physiological studies have shown that NAGK activity in P. coloniale cells is among the lowest reported to date, which may contribute to energy conservation in this alga. These results not only indicate that NAGK characteristics may vary more across oxygenic phototrophs than previously thought, but also expand our understanding of metabolic adaptation to deep-sea oligotrophic environments. - Source: PubMed
Publication date: 2026/09/12
Statinov VladislavLapina TatianaMusaelyan DavidErmilova Elena - Reactive cysteines serve important functions in proteins, and characterizing their engagement by different electrophiles facilitates biological discovery and covalent drug development. Here, we show that the common lysis buffer components phenylmethylsulfonyl fluoride (PMSF) and orthovanadate generate a lysis-derived oxidant that engages cysteines during cell lysis. This oxidant sulfonylates N-acetyl-D-glucosamine kinase (NAGK) C217, producing a mobility shift on SDS-PAGE. C217 lies within the ATP-binding pocket, and a C217S mutant exhibits reduced ATP affinity and enzymatic activity. Competitive iodoacetamide-alkyne activity-based protein profiling (IAA-ABPP) chemoproteomics further showed that the PMSF/orthovanadate oxidant defines a cysteine-engagement profile that partially differs from that of pervanadate. These findings reveal an unrecognized source of chemical reactivity during protein extraction that expands the toolkit for cysteine-engagement profiling and underscores how sample preparation chemistry shapes chemoproteomic measurements. - Source: PubMed
Publication date: 2026/08/31
Schaffer Bethany ENam Jung SeungCohen Ceci AMesaros ClementinaMyers Robert WBaxt LeighWellen Kathryn ECantley Lewis CDephoure NoahSnyder Nathaniel WChio Iok In ChristineBlenis John - Fluorescence hybridization (FISH) is commonly used to detect the copy number (M/N ratio) in postoperative or biopsy-derived neuroblastoma (NB) tissue samples, a critical indicator for risk stratification of NB. However, most NB patients present with large tumors at an advanced stage, making tissue acquisition difficult both surgically and biopsy. Therefore, a triple-amplified sequential activation allosteric DNA biosensor, termed TASA (comprising -TASA and -TASA), which leverages the elevated enzymatic activities of apurinic/apyrimidinic endonuclease 1 (APE1) and telomerase in the cytoplasm of NB cells as molecular switches and signal amplification molecules, was developed for quantitative detection of the M/N ratio of NB. -TASA and -TASA sequentially interact with APE1, (or ), and telomerase, undergoing a conformational change that cyclically separates the fluorophore from the quencher with high efficiency, thereby producing a detectable fluorescence signal. -TASA and -TASA exhibit superior sensitivity, with limits of detection of 0.45 aM and 0.75 aM for mRNA and mRNA, respectively. In addition, -TASA and -TASA enable rapid quantitative determination of the M/N ratio in NB tissues. In particular, -TASA and -TASA enable accurate quantification of the M/N ratio in clinical NB tissues. In summary, this study presents a novel strategy for quantifying the NB M/N ratio, demonstrating significant potential for future applications in biomedical research and clinical diagnosis. - Source: PubMed
Publication date: 2026/07/16
Zhao LiangZhang YingyuTian HengyunZhang MengxinLiu KangboSun MengLi ZirongHou LigongZhang XianweiZhang Wancun - Bacterial peptidoglycan fragments (PGNs) are pathogen-associated molecular patterns that activate the mammalian innate immune system, particularly through NOD2 signaling pathways. Since NOD2 is a cytosolic sensor in mammalian cells, cellular assays are commonly used to identify bioactive PGNs that elicit NOD2 response, with muramyl dipeptide (MDP) long recognized as the minimal NOD2 agonist. However, recent studies have highlighted the intracellular phosphorylation of MDP by mammalian -acetylglucosamine kinase (NAGK) as a critical prerequisite for NOD2 activation, emphasizing the need for further investigation into other host-mediated processing of PGNs. In this study, we examined how various bacterial PGNs, differing in saccharide and stem peptide length, undergo intracellular structural modifications within mammalian cells. Our findings show that disaccharide PGNs are processed through intracellular glycosidic cleavage to generate monosaccharide MurNAc-containing PGNs intracellularly, followed by NAGK-dependent phosphorylation, uncovering an additional essential step that precedes NOD2 activation. To identify the glycosidase responsible for disaccharide PGN cleavage, we provide biochemical and cellular observations that human -GlcNAcase functions as a promiscuous glycosidase capable of processing certain disaccharide PGNs and potentially modulate their NOD2 activation. Furthermore, we demonstrate that PGNs with a lysine-type tripeptide stem are specifically cleaved into dipeptides and that phosphorylated PGNs are subjected to dephosphorylation in mammalian cells. Together, these findings offer insights into the metabolism and intracellular processing of PGNs in mammalian cells, which are crucial in shaping the host innate immune responses. - Source: PubMed
Publication date: 2026/07/07
Feng ShiliuAdamson ChristopherLi ChenyuNg Evan Wei LongQiao Yuan