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50 results about "Specific lysis" patented technology

Tissue Specific Lysis Buffer. A convenient, ready-to-use tissue lysis buffer that is generally used for western blot, Co-IP, Chromatin IP (ChIP), enzyme activity assays, etc.

Lytic phage strain capable of preventing and controlling tomato bacterial wilt and applications of lytic phage strain

The invention discloses a lytic phage strain NJ-P3 capable of preventing and controlling tomato bacterial wilt, the classification name of the lytic phage strain NJ-P3 is Podoviridae phage, and the lytic phage strain NJ-P3 is preserved in the China Center for Type Culture Collection (CCTCC) on March 6, 2018, and is assigned with the accession number of CCTCC NO:M 2018099. The invention further discloses applications of the phage NJ-P3 in preventing and treating soil-borne bacterial wilt of tomato and applications of the phage NJ-P3 in preparing phage preparations for preventing and treating soil-borne bacterial wilt of tomato. The phage can realize specific splitting of pathogenic bacteria of bacterial wilt, when the temperature is 20-40 DEG C and the pH is 5-9, the phage has the highest activity and the strongest splitting capacity, the bactericidal ability is shown, the indoor antibacterial test shows that the antibacterial rate achieves 72.4%, and thus the phage can be used for preventing and treating soil-borne bacterial wilt of tomato. When the phage provided by the invention is used for preventing and treating soil-borne bacterial wilt of tomato, the disease prevention rate for the potted plant achieves 60%, and the biocontrol rate for the field achieves 85.19%.
Owner:NANJING AGRICULTURAL UNIVERSITY

C-1 Inhibitor prevents non-specific plasminogen activation by a prourokinase mutant without impeding fibrin-specific fibrinolysis

InactiveUS20090010916A1High dose toleranceInhibition of activationPeptide/protein ingredientsBlood disorderTolerabilityC1-inhibitor
A mutant prourokinase plasminogen activator (M5) was developed to make prouPA less subject to spontaneous conversion to tcuPA in blood at therapeutic concentrations. Two-chain M5 was shown to form complexes with C1-inhibitor, which was the principal inhibitor of tcM5 in plasma. The effect of supplemental additions of C1-inhibitor on fibrinolysis and fibrinogenolysis by M5 was determined. Supplemental C1-inhibitor restored the stability of high-dose M5 and prevented fibrinogenolysis but not fibrinolysis, the rate of which was not compromised by the inhibitor. Due to higher dose tolerance of M5 in the presence of supplemental C1-inhibitor, the rate of fibrin-specific lysis reached that achievable by nonspecific fibrinolysis, which is the maximum possible for a plasminogen activator. Plasma C1-inhibitor stabilized M5 in plasma by inhibiting tcM5 which would otherwise greatly amplify non-specific plasminogen activation causing more tcM5 generation from M5. This unusual dissociation of inhibitory effects, whereby fibrinogenolysis and not fibrinolysis is inhibited, has significant implications for improving the safety and efficacy of fibrinolysis. Methods of reducing bleeding and non-specific plasminogen activation during fibrinolysis by administering M5 along with exogenous C1-inhibitor are disclosed.
Owner:THROMBOLYTIC SCI

C1-Inhibitor Prevents Non-Specific Plasminogen Activation by a Prourokinase Mutant without Impeding Fibrin-Specific Fibrinolysis

ActiveUS20110081334A1Attenuation of rateHigh dose tolerancePeptide/protein ingredientsBlood disorderC1-inhibitorHigh doses
A mutant prourokinase plasminogen activator (M5) was developed to make prouPA less subject to spontaneous activation during fibrinolysis. C1-inhibitor complexes with tcM5. The effect of C1-inhibitor on fibrinolysis and fibrinogenolysis by M5 was determined. Supplemental C1-inhibitor restores the stability of M5 but not that of prouPA. Clot lysis by M5 with supplemental C1-inhibitor showed no attenuation of the rate of fibrinolysis, whereas fibrinogenolysis was prevented by C1-inhibitor. Due to higher dose tolerance of M5 with C1-inhibitor, the rate of fibrin-specific lysis reached that achievable by nonspecific fibrinolysis without inhibitor. Plasma C1-inhibitor stabilized M5 in plasma by inhibiting tcM5 and thereby non-specific plasminogen activation. At the same time, fibrin-specific plasminogen activation remained unimpaired. This unusual dissociation of effects has significant implications for improving the safety and efficacy of fibrinolysis. Methods of reducing bleeding and non-specific plasminogen activation during fibrinolysis by administering M5 along with exogenous C1-inhibitor are disclosed.
Owner:THROMBOLYTIC SCI

Rapid quantitative detection method capable of specifically identifying survival cells of enterobacter sakazakii and primer thereof

The invention discloses a rapid quantitative detection method capable of specifically identifying survival cells of enterobacter sakazakii and a primer thereof. The detection method comprises the following steps: 1) preparing a specific lysis culture solution containing enterobacter sakazakii bacteriophage; 2) co-culturing the lysis culture solution prepared in the step 1) with a standard strain gradient suspension and a sample diluent respectively; 3) determining the variation of a Ct value of a co-cultured substance in the step 2) through qPCR; and 4) calculating the number of the survival cells of the enterobacter sakazakii in a sample according to a linear relation between the delta Ct value in the step 3) and the viable count of the standard strain gradient suspension, so as to realize rapid quantitative determination of the number of the survival cells of the enterobacter sakazakii in the sample. The detection method disclosed by the invention has no cross reaction on dead cellsand other strains; the detection period is 5.5h and the detection flux is high; and the detection method is suitable for quantitative detection of the survival cells of the enterobacter sakazakii in food or environment samples and is used for rapidly evaluating the effectiveness of disinfection and sterilization conditions on the enterobacter sakazakii.
Owner:YANGZHOU UNIV
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