A novel "off-on" fluorescent probe for the detection of nickel ions and its clinical application.

Nickel serves as an essential micronutrient for the human body, playing a vital role in various enzymatic processes. However, excessive nickel entering the environment can cause pollution and pose serious risks to animals, plants, and human health. High concentrations of nickel ions in the human body increase the risk of various diseases, highlighting the need for accurate measurement of nickel ions levels.

Enhancing extracellular production of recombinant proteins in Escherichia coli by co-expressing with a haloarchaeal protein containing a putative LolA-like domain.

Escherichia coli represents one of the most widely used hosts for recombinant protein production, but its limited capacity for producing extracellular proteins is often cited as a drawback. NJ7G_0991 is an extracellular protein of the haloarchaeon Natrinema sp. J7-2 and comprises a signal peptide, a putative LolA-like domain, and a C-terminal domain of unknown function.

Extracellular Production, Characterization, and Engineering of a Polyextremotolerant Subtilisin-Like Protease From Feather-Degrading Strain CDF.

Here, the gene encoding a subtilisin-like protease (protease Als) was cloned from strain CDF and expressed in . The recombinant enzyme was released into the culture medium of as a mature form (mAls). Purified mAls displayed optimal activity at 60-70°C and pH 10.

The zinc-finger protein ZFYVE1 modulates TLR3-mediated signaling by facilitating TLR3 ligand binding.

Recognition of viral dsRNA by Toll-like receptor 3 (TLR3) leads to the induction of downstream antiviral effectors and the innate antiviral immune response. Here, we identified the zinc-finger FYVE domain-containing protein ZFYVE1, a guanylate-binding protein (GBP), as a positive regulator of TLR3-mediated signaling. Overexpression of ZFYVE1 promoted the transcription of downstream antiviral genes upon stimulation with the synthetic TLR3 ligand poly(I:C).

Complete Genome Sequence of Thermoactinomyces vulgaris Strain CDF, a Thermophilic Bacterium Capable of Degrading Chicken Feathers.

strain CDF was isolated from soil and shown to have the ability to degrade chicken feathers at high temperatures. Here, we report the complete genome sequence of this bacterium, which is 2,595,509 bp long with 2,642 predicted genes and an average G+C content of 48.14%.