Patent application number | Description | Published |
20150108430 | TRANSISTOR CHANNEL - A transistor device includes a substrate having a first region and a second region, a first semiconductor layer of a first semiconductor material having a first portion over the first region and a second portion over the second region, the first portion being separated from the second portion, a second semiconductor layer of a second semiconductor material over the second portion of the first semiconductor layer, a first transistor of a first conductivity type, the first transistor disposed within the first region and having a first set of source/drain regions formed in the first semiconductor layer, and a second transistor of a second conductivity type, the second transistor disposed within the second region and having a second set of source/drain regions formed in the second semiconductor layer. The second conductivity type is different than the second conductivity type, and the second semiconductor material is different from the first semiconductor material. | 04-23-2015 |
20150115397 | SEMICONDUCTOR DEVICE WITH TRENCH ISOLATION - A semiconductor device includes a semiconductor substrate and a trench isolation. The trench isolation is located in the semiconductor substrate, and includes an epitaxial layer and a dielectric material. The epitaxial layer is in a trench of the semiconductor and is peripherally enclosed thereby, in which the epitaxial layer is formed by performing etch and epitaxy processes. The etch and epitaxy process includes etching out a portion of a sidewall of the trench and a portion of a bottom surface of the trench and forming the epitaxial layer conformal to the remaining portion of the sidewall and the remaining portion of the bottom surface. The dielectric material is peripherally enclosed by the epitaxial layer. | 04-30-2015 |
20150243763 | PERFORMANCE BOOST BY SILICON EPITAXY - The present disclosure relates to a method of generating a transistor device having an epitaxial layer disposed over a recessed active region. The epitaxial layer improves transistor device performance. In some embodiments, the method is performed by providing a semiconductor substrate. An epitaxial growth is performed to form an epitaxial layer onto the semiconductor substrate. An electrically insulating layer is then formed onto the epitaxial layer, and a gate structure is formed onto the electrically insulating layer. By forming the epitaxial layer over the semiconductor substrate the surface roughness of the semiconductor substrate is improved, thereby improving transistor device performance. | 08-27-2015 |
20150279894 | CMOS Image Sensor with Epitaxial Passivation Layer - The present disclosure provides a complimentary metal-oxide-semiconductor (CMOS) image sensor (CIS) device. In accordance with some embodiments, the device includes a semiconductor region having a front surface and a back surface; a light-sensing region extending from the front surface towards the back surface within the semiconductor region; a gate stack formed over the semiconductor region; and at least one epitaxial passivation layer disposed at least one of over and below the light-sensing region. In some embodiments, the at least one epitaxial passivation layer includes a p-type doped silicon (Si) layer. | 10-01-2015 |
20150303265 | SEMICONDUCTOR DEVICE WITH TRENCH ISOLATION - A semiconductor device includes a semiconductor substrate and a trench isolation. The trench isolation is located in the semiconductor substrate, and includes an epitaxial layer and a dielectric material. The epitaxial layer is in a trench of the semiconductor and is peripherally enclosed thereby, in which the epitaxial layer is formed by performing etch and epitaxy processes. The etch and epitaxy process includes etching out a portion of a sidewall of the trench and a portion of a bottom surface of the trench and forming the epitaxial layer conformal to the remaining portion of the sidewall and the remaining portion of the bottom surface. The dielectric material is peripherally enclosed by the epitaxial layer. | 10-22-2015 |
20160111511 | TRANSISTOR WITH PERFORMANCE BOOST BY EPITAXIAL LAYER - The present disclosure relates to a transistor device. In some embodiments, the transistor device has an epitaxial layer disposed over a substrate. The epitaxial layer is arranged between a source region and a drain region separated along a first direction. Isolation structures are arranged on opposite sides of the epitaxial layer along a second direction, perpendicular to the first direction. A gate dielectric layer is disposed over the epitaxial layer, and a conductive gate electrode is disposed over the gate dielectric layer. The epitaxial layer overlying the substrate improves the surface roughness of the substrate, thereby improving transistor device performance. | 04-21-2016 |
Patent application number | Description | Published |
20120001095 | LIGHT SOURCE APPARATUS FOR FLUORESCENCE PHOTOGRAPHY - A light source apparatus for fluorescence photography of biomolecule sample gels is disclosed. The light source apparatus comprises a housing, a transparent plate disposed in a light transmission zone at the top of the housing, and at least one LED array disposed in the housing out of the range of the light transmission zone. The LED array irradiates obliquely to the light transmission zone for preventing the light spots from interfering in the observation. Each of LED array may comprises different colors of LEDs for different biomolecule samples. | 01-05-2012 |
20120009088 | HIGH-PERFORMANCE LIGHT SOURCE APPARATUS FOR FLUORESCENCE PHOTOGRAPHY - A high-performance light source apparatus for fluorescence photography of biomolecule sample gels is disclosed. The high-performance light source apparatus comprises a base frame, a supporting region located on the center of the top surface of the base frame for supporting a biomolecule sample gel, and at least one light-emitting module disposed on the top surface of the base frame around the supporting region for emitting an exciting light onto the biomolecule sample gel laterally. Each light-emitting module comprises an LED array having different colors of LEDs for different bio reagents. The exciting light is projected onto the biomolecule sample gel laterally, such that the size of the high-performance light source apparatus can be minimized, and the light spots interference in fluorescence photographing or observation can be prevented. | 01-12-2012 |
20120017633 | COOLING DEVICE - The present invention relates to a cooling device, mainly comprises a carrying unit, a thermal insulation unit, and a temperature-lowering module. The thermal insulation unit is provided over a part of surface of the carrying unit for blocking heat transmission between the carrying unit and the outside. As the carrying unit is placed on the temperature-lowering module, a cooling chip in the temperature-lowering module is able to lower the temperature of the carrying unit and a biological sample. Furthermore, the thermal insulation unit is able to maintain the temperature of the carrying unit and biological sample, when the carrying unit is removed from the temperature-lowering module. Thereafter, a user can conveniently practice observation and experiment with respect to the biological sample, and avoid damaging the biological sample during experiment or transportation by the use of the cooling device. | 01-26-2012 |
20120043212 | REAL-TIME FLUORESCENT ELECTROPHORESIS APPARATUS - A real-time fluorescent electrophoresis apparatus, comprising: an electrophoresis tank comprising a platform, an electrophoresis liquid, a positive electrode and a negative electrode, the platform carrying a gel with a biological sample, the gel comprising a plurality of charged molecules of the biological sample, and the gel, the platform, the positive electrode and the negative electrode being immersed in the electrophoresis liquid; and a lid covering the electrophoresis tank and comprising a filter disposed above the gel and at least one luminous element disposed on at least one side of the filter to irradiate the gel so that the biological sample in the gel is excited to fluoresce. Thereby, the experimenter is able to observe fluorescence phenomenon from the biological sample during electrophoresis so as to trace the electrophoresis process and determine whether the electrophoresis process is to be interrupted and avoid experimental errors. | 02-23-2012 |
Patent application number | Description | Published |
20130302334 | BCL-2-LIKE PROTEIN 11 SRM/MRM ASSAY - Specific peptides, and derived ionization characteristics of those peptides, from the Bcl-2-like protein 11 (BIM) are provided that are particularly advantageous for quantifying the BIM protein directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring (SRM) mass spectrometry, or what can also be termed as Multiple Reaction Monitoring (MRM). Such biological samples are chemically preserved and fixed where the biological sample is selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded. A protein sample is prepared from the biological sample using the Liquid Tissue™ reagents and protocol, and the BIM protein is quantitated in the Liquid Tissue™ sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the peptides described. These peptides can be quantitated if they reside in a modified or an unmodified form. An example of a modified form of a BIM peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence. | 11-14-2013 |
20140199717 | Multiplex MRM Assay for Evaluation of Cancer - The current disclosure provides specific peptides, and derived ionization characteristics of the peptides from the estrogen receptor (ER), progesterone receptor (PR), and/or antigen Ki67 (Ki67) proteins that are particularly advantageous for quantifying the ER, PR, and/or Ki67 proteins directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring/Multiple Reaction Monitoring (SRM/MRM) mass spectrometry. Such biological samples are chemically preserved and fixed wherein the biological sample is selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded. A protein sample is prepared from a biological sample using the Liquid Tissue™ reagents and protocol, and the ER, PR, and/or Ki67 proteins are quantitated in the Liquid Tissue™ sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the peptides described for one or more of the ER, PR, and/or Ki67 proteins. These peptides can be quantitated if they reside in a modified or in an unmodified form. An example of a modified form of an ER, PR, and/or Ki67 peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence. | 07-17-2014 |
20140206775 | SRM/MRM Assay for the Fatty Acid Synthase Protein - Specific peptides, and derived ionization characteristics of the peptides, from the Fatty acid synthase (FASN) protein are provided that are particularly advantageous for quantifying the FASN protein directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring (SRM) mass spectrometry, or what can also be termed as Multiple Reaction Monitoring (MRM) mass spectrometry. Such biological samples are chemically preserved and fixed and are selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded. A protein sample is prepared from said biological sample using the Liquid Tissue™ reagents and protocol and the FASN protein is quantitated in the Liquid Tissue™ sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the peptides described. These peptides can be quantitated if they reside in a modified or an unmodified form. An example of a modified form of an FASN peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence. | 07-24-2014 |
20140206776 | MRM/SRM Assay for Death Receptor 5 Protein - Specific peptides, and derived ionization characteristics of those peptides from Death Receptor 5 (DR5) protein are provided that are particularly advantageous for quantifying the DR5 protein directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring/Multiple Reaction Monitoring (SRM/MRM) mass spectrometry. Such biological samples are chemically preserved and fixed wherein the biological sample is selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded. A protein sample is prepared from a biological sample using the Liquid Tissue™ reagents and protocol, and the DR5 protein are quantitated in the Liquid Tissue™ sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the peptides described for one or more of the DR5 protein. These peptides can be quantitated if they reside in a modified or in an unmodified form. An example of a modified form of a DR5 peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence | 07-24-2014 |
20140213478 | SRM/MRM Assay for the Receptor Tyrosine-Protein Kinase erbB-4 Protein (HER4) - Specific peptides, and derived ionization characteristics of the peptides, from the Receptor Tyrosine-Protein Kinase erbB-4 Protein (HER4) protein are provided that are particularly advantageous for quantifying the HER4 protein directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring (SRM) mass spectrometry, or what can also be termed as Multiple Reaction Monitoring (MRM) mass spectrometry. Such biological samples are chemically preserved and fixed where the biological sample is selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, | 07-31-2014 |
20140322245 | SRM/MRM Assay for the Insulin Receptor Protein - Specific peptides, and derived ionization characteristics of the peptides, from the Insulin Receptor protein (IR), and its isoforms IR-A and IR-B, that are particularly advantageous for quantifying the IR protein, IR-A isoform and/or IR-B isoform, directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring (SRM) mass spectrometry, or what can also be termed as Multiple Reaction Monitoring (MRM) mass spectrometry. Such biological samples are chemically preserved and fixed and are selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded. A protein sample is prepared from said biological sample using the Liquid Tissue™ reagents and protocol and the IR protein, and IR-A and/or IR-B isoforms, is quantitated in the Liquid Tissue™ sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the peptides described. These peptides can be quantitated if they reside in a modified or an unmodified form. An example of a modified form of an IR peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence. | 10-30-2014 |
20140336281 | SRM/MRM Assay for the Ephrin Typa-A Receptor 2 Protein - Specific peptides, and derived ionization characteristics of the peptides, from the Ephrin Type-A Receptor 2 (EPHA2) protein are provided that are particularly advantageous for quantifying the EPHA2 protein directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring (SRM) mass spectrometry, or what can also be termed as Multiple Reaction Monitoring (MRM) mass spectrometry. Such biological samples are chemically preserved and fixed and are selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded. A protein sample is prepared from said biological sample using the Liquid Tissue™ reagents and protocol and the EPHA2 protein is quantitated in the Liquid Tissue™ sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the peptides described. These peptides can be quantitated if they reside in a modified or an unmodified form. An example of a modified form of an EPHA2 peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence. | 11-13-2014 |
20150072895 | SRM/MRM Assay for Subtyping Lung Histology - The current disclosure provides for specific peptides, and derived ionization characteristics of the peptides, from the KRT5, KRT7, NapsinA, TTF1, TP63, and/or MUC1 proteins that are particularly advantageous for quantifying the KRT5, KRT7, NapsinA, TTF1, TP63, and/or MUC1 proteins directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring (SRM) mass spectrometry, or what can also be termed as Multiple Reaction Monitoring (MRM) mass spectrometry. Such biological samples are chemically preserved and fixed wherein said biological sample is selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded. A protein sample is prepared from said biological sample using the Liquid Tissue™ reagents and protocol and the KRT5, KRT7, NapsinA, TTF1, TP63, and/or MUC1 proteins are quantitated in the Liquid Tissue™ sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the peptides described. These peptides can be quantitated if they reside in a modified or an unmodified form. An example of a modified form of a KRT5, KRT7, NapsinA, TTF1, TP63, and MUC1 fragment peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence. | 03-12-2015 |
20160054323 | SRM/MRM Assay for Subtyping Lung Histology - The current disclosure provides for specific peptides, and derived ionization characteristics of the peptides, from the KRT5, KRT7, NapsinA, TTF1, TP63, and/or MUC1 proteins that are particularly advantageous for quantifying the KRT5, KRT7, NapsinA, TTF1, TP63, and/or MUC1 proteins directly in biological samples that have been fixed in formalin by the method of Selected Reaction Monitoring (SRM) mass spectrometry, or what can also be termed as Multiple Reaction Monitoring (MRM) mass spectrometry. Such biological samples are chemically preserved and fixed wherein said biological sample is selected from tissues and cells treated with formaldehyde containing agents/fixatives including formalin-fixed tissue/cells, formalin-fixed/paraffin embedded (FFPE) tissue/cells, FFPE tissue blocks and cells from those blocks, and tissue culture cells that have been formalin fixed and or paraffin embedded. A protein sample is prepared from said biological sample using the Liquid Tissue™ reagents and protocol and the KRT5, KRT7, NapsinA, TTF1, TP63, and/or MUC1 proteins are quantitated in the Liquid Tissue™ sample by the method of SRM/MRM mass spectrometry by quantitating in the protein sample at least one or more of the peptides described. These peptides can be quantitated if they reside in a modified or an unmodified form. An example of a modified form of a KRT5, KRT7, NapsinA, TTF1, TP63, and MUC1 fragment peptide is phosphorylation of a tyrosine, threonine, serine, and/or other amino acid residues within the peptide sequence. | 02-25-2016 |
Patent application number | Description | Published |
20140355732 | Shift Register Circuit - A shift register is disclosed. The shift register circuit includes a pull up control circuit configured to provide a pull up control signal; a first pull up circuit configured to provide a sensor driving signal in response to the pull up control signal and a second clock signal; a second pull up circuit configured to provide a gate driving signal in response to a first clock signal, the pull up control signal and the second clock signal; a first pull down control circuit configured to output a first pull down control signal; a first pull down circuit configured to pull down the pull up control signal, the sensor driving signal and the gate driving signal in response to the first pull down control signal; and a main pull down circuit configured to pull down the pull up control signal and the gate driving signal. | 12-04-2014 |
20140369457 | SHIFT REGISTER CIRCUIT - A shift register circuit includes a first pull-down control circuit, a first pull-down circuit electrically connecting to the first pull-down control circuit, a first inversed pulse signal coupling circuit outputting a first inversed pulse signal, a first pull-up circuit outputting a first gate control signal, and a first main pull-down circuit electrically connecting to the first pull-up circuit. The first pull-up circuit receives a first driving signal and a first pulse signal to output the first gate control signal. The first inversed pulse signal coupling circuit duly outputs the first inversed pulse signal to compensate a surge occurring in the first driving signal. | 12-18-2014 |
20140372494 | GATE DRIVER CIRCUIT - A gate driver circuit includes several shift register stages. One of shifter register stages includes a pull-up unit, a pull-up control unit, and an output unit. The pull-up unit is configured for generating a driving signal according to a first clock signal and an operating signal. The pull-up control unit is configured for generating a next-stage operating signal to a next-stage shift register stage according to the first clock signal, the operating signal and the driving signal. The output unit is configured for receiving the driving signal and generating a first gate driving signal and a second gate driving signal according to a first controlling signal and a second controlling signal, respectively. | 12-18-2014 |
20150049853 | Shift Register Circuit - A shift register circuit includes first-type and second-type shift registers, each comprising a pull-down control circuit, a pull-down circuit, a key pull-down circuit, a 3D-mode pull-up circuit, and a 2D-mode pull-up circuit. The pull-down circuit is connected to the pull-down control circuit. The key pull-down circuit, connected to the pull-down circuit, pulls down a driving signal and a gate control signal. When the 2D-mode pull-up circuit operates, a first-type shift register generates a driving signal for a second-type shift register. When the 3D-mode pull-up circuit operates, a first-type shift register generates another driving signal for another first-type shift register. | 02-19-2015 |
20150194090 | DISPLAY PANEL AND METHOD FOR MANUFACTURING THE SAME - A display panel includes a display area, a shift register circuit, a first start signal line, and a second start signal line. The shift register circuit is electrically coupled to the display area through a plurality of signal output lines. The first start signal line and the second start signal line are electrically coupled to the shift register circuit. The first start signal line and the second start signal line are both arranged without crossing the signal output lines. | 07-09-2015 |
20150255014 | SHIFT REGISTER GROUP AND METHOD FOR DRIVING THE SAME - A shift register group includes a plurality of series-coupled shift registers each being configured to provide an output signal. The third control signal of a first sift register of the plurality of shift registers is the output signal provided by the shift register N stages after the first shift register, and the fourth control signal of the first sift register is the voltage at the driving node of the shift register 2N stages after the first shift register, wherein N is a natural number. A driving method of the aforementioned shift register group is also provided. | 09-10-2015 |
20150288364 | SHIFT REGISTER CIRCUIT - A shift register circuit includes a pull-down circuit, pull-down control circuit, a driving unit, a primary pull-down circuit and a gate driver circuit. The pull-down control circuit is electrically connected to the pull-down circuit and configured to provide an nth-stage pull-down control signal to the pull-down circuit. The a driving unit is electrically connected to the pull-down control circuit and configured to drive the pull-down control circuit. The primary pull-down circuit is electrically connected to the pull-down circuit. The gate driver circuit is electrically connected to the pull-down circuit and configured to output an nth-stage gate driving signal according to an nth-stage control signal. The driving unit is configured to receive a plurality of high-frequency clock signals and accordingly to pre-enable the pull-down control circuit, and n is a positive integer. | 10-08-2015 |