c-Jun Polyclonal Antibody
- Known as:
- c-Jun Polyclonal Antibody
- Catalog number:
- a-0470-100
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Epigentek inc
- Gene target:
- c-Jun Polyclonal Antibody
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- Pseudomonas species are ubiquitous and have been frequently detected in Arctic and Antarctic environments. They participate in the biogeochemical cycling of carbon, nitrogen, and sulfur in local habitats. Pseudomonas sp. GW-45 was isolated from seawater in Ardley Cove, King George Island, Antarctica. The strain was capable of growing with dimethylsulfoniopropionate (DMSP) as the sole carbon source and producing dimethyl sulfide (DMS). The strain contained a 4,025,523 bp chromosome (G + C content of 55.71 mol%) and two plasmids with lengths of 189,931 and 2183 bp, respectively. A total of 3890 protein-coding DNA sequences, 50 tRNA genes, nine rRNA genes, and one tmRNA gene were identified. Genome-based relatedness analysis revealed that strain GW-45 represented a novel species within the genus Pseudomonas. It harbored genes involved in DMSP biosynthesis (e.g., dsyB) and catabolism (e.g., dmdA and dddP), as well as genes related to nitrate reduction (e.g., glnA, nasA, nirB, nirS, and nosZ). Three types of mobile genetic elements including insertion sequence, genomic island, and prophage were detected in the genome. These findings contribute to an improved understanding of the ecological role and adaptive evolution of Pseudomonas species in the Antarctic coastal marine environment. - Source: PubMed
Publication date: 2026/06/22
Zhang Yi-HeHu Yong-QiangWang Zuo-QiLi Chun-YangHu TingHu ZhongZeng Yin-Xin - Decapod crustaceans synthesize a variety of digestive enzymes. These include various hydrolases and highly active and stable endopeptidases, which have high potential for biotechnological applications. Besides biochemical investigations, knowledge about the amino acid sequence can provide crucial information about the molecular structure and catalytic properties of these enzymes. Therefore, transcripts of the midgut glands of three large decapod species (crab and lobster) were created and will serve as a molecular library for future comparative and applied studies on the gastric enzymes. - Source: PubMed
Publication date: 2026/06/17
Koch MarieHarms LarsMiksch LukasSaborowski Reinhard - As a key marine organic sulfur compound, dimethylsulfoniopropionate (DMSP) is an important carbon and sulfur source for marine microorganisms and the primary precursor of dimethyl sulfide (DMS). The metabolism of DMSP by marine bacteria regulates the air-sea flux of DMS, thereby affecting the global climate. This study reports the genomic features of two Leisingera strains (SA32 and SA215) isolated from marine environments, with an emphasis on genes involved in sulfur metabolism. The genome of strain SA32 is 4,678,260 bp with a GC content of 63.48%, while that of strain SA215 is 4,754,962 bp with a GC content of 62.27%. Genomic analysis shows that both Leisingera strains contain genes encoding DMSP lyases; however, strain SA32 only possesses a DMSP cleavage pathway centered on DddD, while strain SA215 has both a complete DMSP demethylation pathway (involving DmdA, DmdB, DmdC, and DmdD) and cleavage pathways mediated by DddQ, DddP, and DddD, indicating a greater capacity for utilizing marine organic sulfur. This study highlights the functional differentiation of DMSP metabolism in the two marine Leisingera strains, deepening our understanding of the ecological roles of this genus in the marine sulfur cycle. - Source: PubMed
Publication date: 2026/06/04
He KangFang SuyunWang PengyuLiu QingHu Xiaoke - With the increasing awareness of sustainability and physical health, plant protein gels, as alternatives to animal protein gels, have become a research hotspot in the development of new healthy foods. Studies on plant proteins as substitutes for animal proteins have mainly focused on their gel properties, these properties remain inferior to those of animal proteins. Consequently, modulating and enhancing the gel properties of plant proteins constitute a key challenge and research priority. Here, this study explores the influence of gelatin (Gel) modification on the thermal gel behavior of kidney bean protein. When the Gel concentration of 2% (w/v), a denser cross-linked network was formed in kidney bean protein through heat-induced gelation at 90 °C. Additionally, the grafting of kidney bean protein with Gel causes the helical structure to transition to a more stable β-sheet structure (43.97 ± 3.49%). Heat-induced hydrogel K/G exhibited enhanced surface hydrophobicity (68.95 ± 1.91), promoting the formation of intermolecular disulfide bonds between kidney bean protein and Gel. By modifying kidney bean protein with Gel, more 11S acidic peptides and 7S β subunits appeared in heat-induced hydrogel K/G. This study provides a strategy for preparing kidney bean protein with a stable cross-linked network structure, which offers fundamental insights that support its potential use in clinical nutrition and specialized medical food formulations. - Source: PubMed
Publication date: 2026/06/28
Ding ShanshanWang ZhicongZhou YingyingWang YixuDu YinanHu JiangningWu Di - Oleogelation has emerged as a promising strategy for structuring unsaturated oils to address the conflict between food texture and health concerns. However, most oleogelators used in indirect methods rely on complicated pre-processing and lack natural sources. In this study, a pectin-protein-polyphenol complex derived from white grape pomace was investigated as a sole oleogelator to structure canola oil via an emulsion-templated approach. High oil contents of 94.9-97.9% (w/w) were achieved at pectin-to-oil ratios of 2:100-5:100 (w/v), with liquid oil effectively entrapped within the pectin complex network. Rheological analyses confirmed gel-like behaviour, with viscoelastic response associated with network density and integrity. The pectin complex network exhibited a capacity for thermal reinforcement, evidenced by increased viscoelastic moduli during the heating-cooling cycle and enhanced oil retention under thermal stress. Oil binding capacity remained up to 81.8% after heating at 180 °C followed by high-speed centrifugation. This reinforcement can be associated with hydrogen bond rearrangement and strengthened pectin-protein interactions within the network. Moreover, the oleogels exhibited improved oxidative stability, with total oxidation values reduced by 29.9-52.4% compared with unstructured oil in an accelerated oxidation test. Furthermore, when used to replace butter in pound cakes, the oleogels improved air cell formation compared with liquid oil and modulated cake crumb hardness, cohesiveness, and springiness. Overall, this study demonstrates that grape pomace-derived pectin complex can serve as a natural oleogelator with potential for thermally processed foods, while promoting the valorisation of grape pomace as a food waste resource. - Source: PubMed
Publication date: 2026/06/27
Gao YinlingSun YimanMensah Richard QShi JiahuaDunn KameronZhang Zhanying