Jun Kameoka

 Jun Kameoka

Jun Kameoka

  • Courses1
  • Reviews1
May 2, 2018
N/A
Textbook used: No
Would take again: Yes
For Credit: Yes

0
0


Not Mandatory



Difficulty
Clarity
Helpfulness

Awesome

Prof. Kameoka informs you about what you will be tested over and he's really great Lectures are good but you don't really need them or the textbook to get a good grade. Keep track of the course's equations and he gives the solutions to the homework so you should be fine.

Biography

Texas A&M University College Station - Engineering


Resume

  • 1995

    Japanese

    Ph.D

    Expertise: Nano and microfluidics

    bio-microstructure hybrid system

    microrobotics

    Electrical Engineering

    Cornell University

  • Image Processing

    Higher Education

    Mathematica

    University Teaching

    Experimentation

    Simulations

    Nanotechnology

    Research

    Mathematical Modeling

    Physics

    Microfluidics

    Nanoparticles

    Science

    Theory

    Microscopy

    LaTeX

    Matlab

    Nanofabrication

    Signal Processing

    Numerical Analysis

    Measurement of Protein 53 Diffusion Coefficient in Live HeLa Cells Using Raster Image Correlation Spectroscopy (RICS)

    Mien-Chie Hung

    Chao-Kai Chou

    Pei-Hsiang Tsou

    Hirohito Yamaguchi

    Ying-Nai Wang

    Measurement of Protein 53 Diffusion Coefficient in Live HeLa Cells Using Raster Image Correlation Spectroscopy (RICS)

    Mien-Chie Hung

    Jennifer L. Hsu

    Hong-Jen Lee

    Ying-Nai Wang

    Hirohito Yamaguchi

    Jung-Mao Hsu

    Chun-Te Chen

    Heng-Huan Lee

    [Abstract] Signal transduction is a dynamic process that regulates cellular functions through multiple types of biomolecular interactions

    such as the interactions between proteins and between proteins and nucleic acids. However

    the techniques currently available for identifying protein-protein or protein–nucleic acid complexes typically provide information about the overall population of signaling complexes in a sample instead of information about the individual signaling complexes therein. We developed a technique called “microchannel for multiparameter analysis of proteins in a single complex” (mMAPS) that simultaneously detected individual target proteins either singly or in a multicomponent complex in cell or tissue lysates. We detected the target proteins labeled with fluorophores by flow proteometry

    which provided quantified data in the form of multidimensional fluorescence plots. Using mMAPS

    we quantified individual complexes of epidermal growth factor (EGF) with its receptor EGFR

    EGFR with signal transducer and activator of transcription 3 (STAT3)

    and STAT3 with the acetylase p300 and DNA in lysates from cultured cells with and without treatment with EGF

    as well as in lysates from tumor xenograft tissue. Consistent with the ability of this method to reveal the dynamics of signaling protein interactions

    we observed that cells treated with EGF induced the interaction of EGF with EGFR and the autophosphorylation of EGFR

    but this interaction decreased with longer treatment time. Thus

    we expect that this technique may reveal new aspects of molecular interaction dynamics.

    mMAPS: A Flow-Proteometric Technique to Analyze Protein-Protein Interactions in Individual Signaling Complexes

    Mien-Chie Hung

    Chin B. Su

    Hirohito Yamaguchi

    [Abstract] A simple microfluidic 3D hydrodynamicflow focusing device has been developed and demonstrated quantitative determinations of quantum dot 525 with antibody (QD525-antibody) and hemagglutinin epitope tagged MAX (HA-MAX) protein concentrations. This device had a step depth cross junction structure at a hydrodynamicflow focusing point at which the analyte stream was flowed into a main detection channel and pinched not only horizontally but also vertically by two sheath streams. As a result

    a triangular cross-sectional flow profile of the analyte stream was formed and the laser was focused on the top of the triangular shaped analyte stream. Since the detection volume was smaller than the radius of laser spot

    a photon burst histogram showed Gaussian distribution

    which was necessary for the quantitative analysis of protein concentration. By using this approach

    a linear concentration curve of QD525-antibody down to 10 pM was demonstrated. In addition

    the concentration of HA-MAX protein in HEK293 cell lysate was determined as 0.283 ± 0.015 nM. This approach requires for only 1 min determining protein concentration. As the best of our knowledge

    this is the first time to determinate protein concentration by using single molecule detection techniques.

    Microfluidic three-dimensional hydrodynamic flow focusing for the rapid protein concentration analysis

    Takeyuki Misawa

    Keiyo Nakano

    Hiroshi Miyamoto

    Masayuki Yasuike

    Pei-Hsiang Tsou

    Rapid antibiotic efficacy screening with aluminum oxide nanoporous membrane filter-chip and optical detection system.

    Kameoka

    Texas A&M University

    Cornell University

    Texas A&M University

    Associate Professor

    Texas A&M University

    Post Doctoral Associate、Nanobiotechnology Center

    Cornell University

Possible Matching Profiles

The following profiles may or may not be the same professor:

  • Jun Kameoka (80% Match)
    Associate Professor
    Texas A&M University - Texas A&m University