Abstract: A method for cleaning semiconductor substrate without damaging patterned structure on the semiconductor substrate using ultra/mega sonic device comprises applying liquid into a space between a substrate and an ultra/mega sonic device; setting an ultra/mega sonic power supply at frequency f1 and power P1 to drive the ultra/mega sonic device; before bubble cavitation in the liquid damaging patterned structure on the substrate, setting the ultra/mega sonic power supply at zero output; after temperature inside bubble cooling down to a set temperature, setting the ultra/mega sonic power supply at frequency f1 and power P1 again; detecting power on time at power P1 and frequency f1 and power off time separately or detecting amplitude of each waveform output by the ultra/mega sonic power supply; comparing the detected power on time with a preset time ?1, or comparing the detected power off time with a preset time ?2, or comparing detected amplitude of each waveform with a preset value, if the detected power on time

Abstract: A system for controlling damages in cleaning a semiconductor wafer comprising features of patterned structures, the system comprising: a wafer holder for temporary restraining a semiconductor wafer during a cleaning process; an inlet for delivering a cleaning liquid over a surface of the semiconductor wafer; a sonic generator configured to alternately operate at a first frequency and a first power level for a first predetermined period of time and at a second frequency and a second power level for a second predetermined period of time, to impart sonic energy to the cleaning liquid, the first predetermined period of time and the second predetermined period of time consecutively following one another; and a controller programmed to provide the cleaning parameters, wherein at least one of the cleaning parameters is determined such that a percentage of damaged features as a result of the imparting sonic energy is lower than a predetermined threshold.

Abstract: The present disclosure discloses an intelligent point-of-care testing device for mycotoxins based on a quantum dots test strip. A first light source and a second light source are used for exciting a test strip which is placed in a shell and coated with a mycotoxin antigen to obtain emitted light, and a light filtering component is used for filtering out impurity light. A clamping mechanism is used for clamping and fixing an image capturing component. The image capturing component is used for capturing, an image of mycotoxins based on a quantum dots test strip. A processor is used for analyzing and calculating image information to obtain a mycotoxin content result. The testing time is shortened, and the portability and practicability of mycotoxin testing are improved. Quantitative instant testing of single or multi-toxin mixed pollution is achieved, and the technical problem of fluorescence quantification is solved.

Abstract: The present disclosure belongs to the technical field of biosensors and particularly provides a construction method for a photocathode indirect competition sensor and an evaluation method. The construction method includes: using Z-type Bi2O3/CuBi2O4 as a sensing platform; calculating a photoinduced electron Z-type transfer path and an energy band structure of Bi2O3 and CuBi2O4 using a density functional theory (DFT); and constructing a Bi2O3/CuBi2O4-based biosensor. A photoelectrochemical (PEC) photocathode biosensor based on a Bi2O3/CuBi2O4 heterojunction prepared through the solution has good repeatability, reproducibility, stability, and specificity for detecting a target. The PEC biosensor constructed in the solution of the present disclosure has a broad application prospect in the fields of healthcare, environment, and food.

Abstract: The present disclosure discloses an intelligent point-of-care testing device for mycotoxins based on a quantum dots test strip. A first light source and a second light source are used for exciting a test strip which is placed in a shell and coated with a mycotoxin antigen to obtain emitted light, and a light filtering component is used for filtering out impurity light. A clamping mechanism is used for clamping and fixing an image capturing component. The image capturing component is used for capturing, an image of mycotoxins based on a quantum dots test strip. A processor is used for analyzing and calculating image information to obtain a mycotoxin content result. The testing time is shortened, and the portability and practicability of mycotoxin testing are improved. Quantitative instant testing of single or multi-toxin mixed pollution is achieved, and the technical problem of fluorescence quantification is solved.

Abstract: A time-resolved fluorescence immunochromatographic kit for simultaneous detection of mixed contamination of five mycotoxins such as aflatoxin B1 and an application thereof are disclosed. The kit comprises a time-resolved fluorescent immunochromatographic test strip and sample reaction vials each containing a europium-labeled monoclonal antibody lyophilized product; wherein the fluorescent test strip comprises a PVC substrate, and a surface of the PVC substrate is adhered with a water absorbing pad (1), a detection pad (2) and a sample pad (3) from top to bottom, adjacent pads being connected and overlapping at connections. The detection pad (2) adopts a nitrocellulose membrane as the base thereof and is arranged with a lateral quality control line (5) and five detection lines (5, 6, 7, 8, 9) from top to bottom each covered by a bovine serum albumin conjugate of each toxin.

Abstract: A time-resolved fluorescence immunochromatography kit for the simultaneous detection of a mixed pollutant of aflatoxin and carbaryl, a preparation method therefor, and an application thereof. The kit comprises a time-resolved fluorescence immunochromatography test strip and a sample reaction vial containing a europium-labeled anti-aflatoxin monoclonal antibody and a europium-labeled anti-carbaryl monoclonal antibody lyophilized product, detection lines of the time-resolved fluorescence immunochromatography test strip being coated with an aflatoxin-bovine serum albumin conjugate and a carbaryl-ovalbumin conjugate respectively, and the anti-carbaryl monoclonal antibody is produced by secretion of a hybridoma cell line Jnw1D2 with a preservation number of CCTCC NO. 0201654. The kit can be used for the simultaneous detection of aflatoxin and carbaryl content in a sample, and features simple and quick operations and a high sensitivity.

Abstract: An immunoadsorbent for purifying fumonisin B1, aflatoxin B1, ochratoxin A, zearalenone and sterigmatocystin; a complex affinity column and its preparation method; and a method for detecting the mycotoxins using the same are provided. The immunoadsorbent comprises a solid-phase support, and an anti-fumonisin B1 monoclonal antibody, an anti-aflatoxin B1 monoclonal antibody, an anti-ochratoxin A monoclonal antibody, an anti-zearalenone monoclonal antibody and an anti-sterigmatocystin monoclonal antibody which are coupled to the solid-phase support, wherein the anti-fumonisin B1 monoclonal antibody is secreted by a hybridoma cell strain Fm7A11. The complex affinity column can be used for purification and detection of a fumonisin B1 sample, an aflatoxin B1 sample, an ochratoxin A sample, a zearalenone sample and a sterigmatocystin sample at the same time.

Abstract: The invention relates to an immunoadsorbent for purifying five kinds of mycotoxins including fumonisin B1 and aflatoxin B1, and a complex affinity column. The immunoadsorbent comprises a solid-phase support, and an anti-fumonisin B1 monoclonal antibody, an anti-aflatoxin B1 monoclonal antibody, an anti-ochratoxin A monoclonal antibody, an anti-zearalenone monoclonal antibody and an anti-sterigmatocystin monoclonal antibody which are coupled to the solid-phase support, wherein the anti-fumonisin B1 monoclonal antibody is secreted by a hybridoma cell strain Fm7A11, and the hybridoma cell strain Fm7A11 has been preserved at China Center for Type Culture Collection, Wuhan University, Wuhan, China on Mar. 29, 2016 with the preservation number of CCTCC No. C201636. The complex affinity column can be used for purification and detection of a fumonisin B1 sample, an aflatoxin B1 sample, an ochratoxin A sample, a zearalenone sample and a sterigmatocystin sample at the same time.

Abstract: A fluorescence polarization immunoassay (FPIA) method for detecting carbaryl. The method includes the steps of mixing a sample to be tested, a fluorescent marker solution and an anti-carbaryl monoclonal antibody solution; incubating for carrying out a competitive reaction; determining a fluorescence polarization value of the resulting system; calculating the concentration of carbaryl in the sample to be tested according to a standard curve of fluorescence polarization values-carbaryl concentrations in carbaryl standard samples. According to the FPIA method for detecting carbaryl provided in the present invention, only the addition of a sample is required, and no separation and washing operations are needed.

Abstract: An aflatoxin nanobody immunoabsorbent and immunoaffinity column and preparation method and use thereof. The immunoabsorbent comprises a solid phase carrier and aflatoxin B1 nanobody 2014AFB-G15 coupled with the solid phase carrier. The 50% inhibiting concentration IC50 of aflatoxin B1 nanobody 2014AFB-G15 to aflatoxin B1 is 0.66 ng/mL, and the cross-reactivity of aflatoxin B1 nanobody 2014AFB-G15 to aflatoxins B2, G1, G2, and M1 are respectively 22.6%, 10.95%, 32.1% and 26%. The amino acid sequence of aflatoxin B1 nanobody 2014AFB-G15 is as depicted by SEQ ID NO: 7, and the coding gene sequence thereof is as depicted by SEQ ID NO: 8. The aflatoxin nanobody immunoaffinity column can be used for purification and concentration of sample extract prior to computer testing, and the immunoaffinity column can be reused repeatedly.

Abstract: An aflatoxin nanobody immunoabsorbent and immunoaffinity column and preparation method and use thereof. The immunoabsorbent comprises a solid phase carrier and aflatoxin B1 nanobody 2014AFB-G15 coupled with the solid phase carrier. The 50% inhibiting concentration IC50 of aflatoxin B1 nanobody 2014AFB-G15 to aflatoxin B1 is 0.66 ng/mL, and the cross-reactivity of aflatoxin B1 nanobody 2014AFB-G15 to aflatoxins B2, G1, G2, and M1 are respectively 22.6%, 10.95%, 32.1% and 26%. The amino acid sequence of aflatoxin B1 nanobody 2014AFB-G15 is as depicted by SEQ ID NO: 7, and the coding gene sequence thereof is as depicted by SEQ ID NO: 8. The aflatoxin nanobody immunoaffinity column can be used for purification and concentration of sample extract prior to computer testing, and the immunoaffinity column can be reused repeatedly.

Abstract: An aflatoxin M1 nanobody, an immunosorbent and an immunoaffinity column. The aflatoxin M1 nanobody 2014AFM-G2 has the amino acid sequence of SEQ ID NO:7, is encoded by the nucleic acid sequence of SEQ ID NO:8, has a 50% inhibiting concentration IC50 to aflatoxin M1 of 0.208 ng/mL, and has cross reaction rates with aflatoxins B1, B2, G1, and G2 of 9.43%, 5.93%, 4.87% and 6.17%, respectively. The immunosorbent includes a solid phase carrier and aflatoxin M1 nanobody 2014AFM-G2 coupled with the solid phase carrier. The immunoaffinity column is loaded with the aflatoxin M1 nanobody immunosorbent. It can be used for purifying and concentrating an extracting solution of a sample before loading to a machine for detection and the immunoaffinity column can be used repeatedly for many times.

Abstract: A hybridoma cell line ST03 having China Center for Type Culture Collection (CCTCC) accession number C2013187, a monoclonal antibody against aflatoxin biosynthetic precursor ST produced by the hybridoma cell line ST03, and the use of the monoclonal antibody. The hybridoma cell line ST03 can be used for preparing a high-titer monoclonal antibody against aflatoxin biosynthetic precursor ST, and the titer of mouse ascites antibody against aflatoxin biosynthetic precursor ST determined by enzyme linked immunosorbent assay (ELISA) can reach 6.4×105. The monoclonal antibody against aflatoxin biosynthetic precursor ST has high sensitivity, has 50% inhibiting concentration IC50 to aflatoxin biosynthetic precursor ST of 0.36 ng/mL, has no cross reaction with all of aflatoxin B1, aflatoxin B2, aflatoxin G1, and aflatoxin G2, and can be used for the content determination of aflatoxin biosynthetic precursor ST.

Abstract: Aflatoxin M1 nanobody 2014AFM-G2 has the amino acid sequence of SEQ ID NO:7, and is encoded by the gene sequence of SEQ ID NO:8. The aflatoxin M1 nanobody 2014AFM-G2 obtained via screening has the properties of tolerance to organic reagents, tolerance to high temperature, tolerance to acids and bases and the like, and good stability. The aflatoxin M1 nanobody 2014AFM-G2 has 50% inhibiting concentration IC50 to aflatoxin M1 of 0.208 ng/mL, and has cross reaction rates with aflatoxin B1, B2, G1, G2 are 9.43%, 5.93%, 4.87% and 6.17%, respectively.

Abstract: A hybridoma cell line ST03 having China Center for Type Culture Collection (CCTCC) accession number C2013187, a monoclonal antibody against aflatoxin biosynthetic precursor ST produced by the hybridoma cell line ST03, and the use of the monoclonal antibody. The hybridoma cell line ST03 can be used for preparing a high-titer monoclonal antibody against aflatoxin biosynthetic precursor ST, and the titer of mouse ascites antibody against aflatoxin biosynthetic precursor ST determined by enzyme linked immunosorbent assay (ELISA) can reach 6.4×105. The monoclonal antibody against aflatoxin biosynthetic precursor ST has high sensitivity, has 50% inhibiting concentration IC50 to aflatoxin biosynthetic precursor ST of 0.36 ng/mL, has no cross reaction with all of aflatoxin B1, aflatoxin B2, aflatoxin G1, and aflatoxin G2, and can be used for the content determination of aflatoxin biosynthetic precursor ST.

Abstract: An aflatoxin M1 nanobody, an immunosorbent and an immunoaffinity column. The aflatoxin M1 nanobody 2014AFM-G2 has the amino acid sequence of SEQ ID NO:7, is encoded by the nucleic acid sequence of SEQ IDNO:8, has a 50% inhibiting concentration IC50 to aflatoxin M1 of 0.208 ng/mL, and has cross reaction rates with aflatoxins B1, B2, G1, and G2 of 9.43%, 5.93%, 4.87% and 6.17%, respectively. The immunosorbent includes a solid phase carrier and aflatoxin M1 nanobody 2014AFM-G2 coupled with the solid phase carrier. The immunoaffinity column is loaded with the aflatoxin M1 nanobody immunosorbent. It can be used for purifying and concentrating an extracting solution of a sample before loading to a machine for detection and the immunoaffinity column can be used repeatedly for many times.

Abstract: Aflatoxin M1 nanobody 2014AFM-G2 has the amino acid sequence of SEQ ID NO:7, and is encoded by the gene sequence of SEQ ID NO:8. The aflatoxin M1 nanobody 2014AFM-G2 obtained via screening has the properties of tolerance to organic reagents, tolerance to high temperature, tolerance to acids and bases and the like, and good stability. The aflatoxin M1 nanobody 2014AFM-G2 has 50% inhibiting concentration IC50 to aflatoxin M1 of 0.208 ng/mL, and has cross reaction rates with aflatoxin B1, B2, G1, G2 are 9.43%, 5.93%, 4.87% and 6.17%, respectively.

Abstract: Hybridoma cell line 10G4 and monoclonal antibody against total aflatoxins produced by the hybridoma cell line 10G4. The hybridoma cell line 10G4 is used to produce the monoclonal antibody that binds specifically total aflatoxin B1, B2, G1 and G2. The titer of the mouse ascites antibody produced by the 10G4 treated mouse is determined through non-competitive enzyme-linked immunosorbent assay and the titer can reach up to 5.12×105. The monoclonal antibody against total aflatoxin B1, B2, G1 and G2 are used for better identification of aflatoxin B1, B2, G1 and G2 with good consistency. The 50% inhibitory concentrations (IC50) of the antibody against aflatoxin B1, B2, G1 and G2 are 2.09 ng/mL, 2.23 ng/mL, 2.19 ng/mL and 3.21 ng/mL respectively. The range of cross reaction rate for aflatoxin B1, B2, G1 and G2 is about 65.2%-100%. The antibody is used for quantitative measurement of total aflatoxin B1, B2, G1 and G2.

Abstract: Hybridoma cell line 10G4 and monoclonal antibody against total aflatoxins produced by the hybridoma cell line 10G4. The hybridoma cell line 10G4 is used to produce the monoclonal antibody that binds specifically total aflatoxin B1, B2, G1 and G2. The titer of the mouse ascites antibody produced by the 10G4 treated mouse is determined through non-competitive enzyme-linked immunosorbent assay and the titer can reach up to 5.12×105. The monoclonal antibody against total aflatoxin B1, B2, G1 and G2 are used for better identification of aflatoxin B1, B2, G1 and G2 with good consistency. The 50% inhibitory concentrations (IC50) of the antibody against aflatoxin B1, B2, G1 and G2 are 2.09 ng/mL, 2.23 ng/mL, 2.19 ng/mL and 3.21 ng/mL respectively. The range of cross reaction rate for aflatoxin B1, B2, G1 and G2 is about 65.2%-100%. The antibody is used for quantitative measurement of total aflatoxin B1, B2, G1 and G2.