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6 results about "Phosphorylation" patented technology

In chemistry, phosphorylation of a molecule is the attachment of a phosphoryl group. Together with its counterpart, dephosphorylation, it is critical for many cellular processes in biology. Phosphorylation is especially important for protein function; for example, this modification activates (or deactivates) almost half of the enzymes present in yeast, thereby regulating their function. Many proteins (between 1/3 to 2/3 of the proteome in eukaryotes) are phosphorylated temporarily, as are many sugars, lipids, and other biologically-relevant molecules.

Modified phosphorus-containing liquid fertilizer and preparation method thereof

InactiveCN109320364ARich varietyIncrease profitAlkali orthophosphate fertiliserAmmonium orthophosphate fertilisersPhosphorylationPhosphate fertilizer
The invention discloses a modified phosphorus-containing liquid fertilizer and a preparation method thereof. The modified phosphorus-containing liquid fertilizer is prepared from the following raw materials in parts by weight: 2-60 parts of a phosphorylation reagent, 10-300 parts of humic acid salt, 100-700 parts of a macroelement fertilizer body, 0-100 parts of a medium element fertilizer body, 0-30 parts of a microelement fertilizer body, 1-50 parts of a surfactant and 300-800 parts of water. The invention further provides the preparation method for the modified phosphorus-containing liquidfertilizer. According to the modified phosphorus-containing liquid fertilizer and the preparation method thereof, a molecular chain of the humic acid salt is cut under the action of the phosphorylation reagent, in addition, graft modification is achieved, and therefore the variety and the number of functional groups are enriched, the chelating ability is improved, when the humic acid salt is mixedwith macroelements, medium elements and microelements, the multiple effects of activating, converting, moving and the like on the phosphate fertilizer are achieved, high-valence metal cations in soilcan also be adsorbed and complexed, sufficient absorption and utilization of crops are facilitated, the formation of an insoluble phosphate fertilizer is avoided, the environment pollution is reduced, and the damage to the soil structure is reduced.
Owner:QINGDAO SOBEL CROP NUTRITION

Preparation method of stress phosphorylation antibody aiming at human Tudor-SN protein T103 site

InactiveCN104277109AEasy to explore correlationSerum immunoglobulinsImmunoglobulins against enzymesDiseaseHumanin
The invention discloses a stress phosphorylation antibody aiming at a human Tudor-SN protein T103 site and a preparation method thereof. The preparation method adopts a multifunctional human Tudor-SN protein as a research object and comprises the following steps of determining if threonine at a 103 site of a human Tudor-SN protein under external environment oxidation stress is subjected to phosphorylation modification by near-infrared double-color laser imaging and mass spectrometry, synthesizing a T103 phosphorylation site-containing semiantigen polypeptide according to the secondary structure prediction result, coupling the T103 phosphorylation site-containing semiantigen polypeptide and a carrier protein (KLH) into a complete antigen, carrying out immunization on SPF-level New Zealand white rabbit by the complete antigen combined with an adjuvant four times and collecting, purifying and identifying a T103 specific stress phosphorylation polyclonal antibody. In practical application, Tudor-SN protein epigenetic phosphorylation modification in different stress environments can be detected, the effect mechanism of the Tudor-SN protein epigenetic phosphorylation modification in cell stress tumor propagation and migration can be discussed and a latent action target point for clinical tumor disease diagnosis and treatment is provided.
Owner:TIANJIN MEDICAL UNIV

Inhibitors of mTORC2

PendingCN114702552AInhibition of activationInhibit phosphorylationNervous disorderPeptide/protein ingredientsPhosphorylationKinase
The invention discloses an mTORC2 (mammalian TORC2) inhibitor. According to the application, an mTORC2 inhibitor is designed and developed on the basis of a protein region Sin1-N structure of an mTORC2 specific subunit Sin1, and the mTORC2 inhibitor specifically inhibits activation of mTORC2 and specifically inhibits phosphorylation of a downstream kinase Akt activation site Ser473; compared with the existing mTOR inhibition active center-oriented small-molecule inhibitor, the variable configuration inhibitor has the advantages of strong inhibition effect and small side effect.
Owner:SUZHOU SITRI INST OF IMMUNOLOGY CO LTD

Method for enriching N-phosphorylated protein

InactiveCN111323283ARaw materials are easy to obtainShort crosslinking timePreparing sample for investigationMaterial analysis by electric/magnetic meansPolymer scienceCarboxyl radical
The invention discloses a method for enriching N-phosphorylated protein, and relates to protein enrichment. Magnetic nanoparticles connected with a bifunctional connecting agent are used for immobilizing functional protein, substrate protein is crosslinked under the action of a crosslinking agent, and the purpose of enriching phosphorylated protein is achieved. The preparation method comprises thefollowing steps: 1) synthesizing a bifunctional connecting agent H2N-CH2-CH2-S-CH2-S-CH2-CH2-COOH; 2) activating carboxyl-COOH on the magnetic nanoparticles; 3) connecting the magnetic nanoparticleswith a connecting agent; 4) activation of carboxyl-COOH on the coupling agent; 5) connection of phosphorylated kinase McsB protein; 6) crosslinking paraformaldehyde with phosphorylated kinase McsB andsubstrate protein CtsR thereof; and 7), separating the enriched protein with magnetic nano-particles; the method has the advantages that the raw materials are simple and easy to obtain, the crosslinking time is short, the operation is simple and convenient, a high-speed centrifugal machine is not needed in the separation process, and the whole process can be completed at room temperature.
Owner:XIAMEN UNIV
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