Ning Liu, Age 532748 W Newell Ave, Walnut Creek, CA 94595

2010012, May 20, 2010

Nov 9, 2009

12/615080

Ning Liu - Fremont CA, US
Katrina Academia - Hercules CA, US
Aran Paulus - San Jose CA, US
Tim Wehr - Albany CA, US
Steve Freeby - Vacaville CA, US

BIO-RAD LABORATORIES, INC. - Hercules CA

C07K 1/14

530344

Phosphorylated peptides are extracted from digests of biological liquids and other peptide mixtures by fractionation on ceramic hydroxyapatite. The ceramic hydroxyapatite is readily usable in a centrifuge, allowing for rapid fractionations of a large number of small volume samples, and accordingly high throughput.

2013028, Oct 31, 2013

Apr 25, 2013

13/870710

Ning Liu - Fremont CA, US
Kevin McDonald - Novato CA, US
Aran Paulus - San Jose CA, US
Anton Posch - Grafting, DE

Bio-Rad Laboratories, Inc., LSG - LSD Division - Hercules CA

G01N 33/53

436501

Disclosed herein are methods of protein quantification and normalization using haloalkylated tryptophan fluorescence. Complex protein samples, i.e., samples that each contain 1,000 or more distinct proteins, from diverse sources that do not have common protein profiles are treated with a halo-substituted organic compound (i.e. haloalkane) that reacts with tryptophan residues to form fluorescent products. Irradiation of the samples with ultraviolet light and the detection and quantification of the resultant fluorescent emissions from all proteins in each sample are then used to obtain comparative values for total protein content among the various samples. The values thus obtained are found to be valid indications of comparative total protein content, despite the fact that the tryptophan levels vary widely among the various proteins in any single sample and the samples, due to the diversity of their origins, tend to differ among themselves in the identities and relative amounts of the proteins that they contain. Protein samples are also normalized to correct for differences in sample dilution, sample loading, and protein transfer inconsistencies, by using stain-free detection of total protein in each of the samples, or detection of subsamples within each sample.

2021029, Sep 23, 2021

Mar 5, 2021

17/193060

- Ann Arbor MI, US
- Hercules CA, US
Muneesh Tewari - Ann Arbor MI, US
William Bradley Strong - El Cerrito CA, US
Kenneth J. Oh - Pleasant Hill CA, US
Evan Thrush - San Anselmo CA, US
Ning Liu - Walnut Creek CA, US

C12Q 1/6876
C12Q 1/6809
C12Q 1/6834

Provided herein is technology relating to the detection of analytes and particularly, but not exclusively, to methods, systems, compositions, and kits for detecting analytes such as nucleic acids, proteins, small molecules, metabolites, and other molecules using a technology based on the transient binding of detection probes in combination with a microfluidic device and/or a nanoparticle.

2021011, Apr 22, 2021

Oct 22, 2020

17/077643

- Hercules CA, US
NING LIU - WALNUT CREEK CA, US
CARL MARLOWE - SAN FRANCISCO CA, US
WILLIAM BRADLEY STRONG - EL CERRITO CA, US

G01N 21/552
G06T 7/00

The invention relates to methods for characterizing the binding interactions between binding partners. The invention pertains to methods comprising contacting a first binding partner with a second binding partner that exhibits fast-off rate binding characteristics with the first binding partner to generate the binding interaction between the first binding partner and the second binding partner, wherein the first binding partner is immobilized onto a substrate that is designed to enhance the fluorescence signal of fluorescent molecules located near the substrate's surface, and wherein the second binding partner is a molecule that emits a fluorescent signal or is conjugated to molecule that emits a fluorescent signal. The interactions between the two binding partners can be analyzed based on multiple transient interactions between the two binding partners.

2019033, Nov 7, 2019

Dec 19, 2017

16/475247

- Hercules CA, US
Ning LIU - Walnut Creek CA, US

G01N 33/557
G01N 33/52
G01N 33/68
G01N 21/64
G06T 7/00
G06T 7/13

Methods for characterizing the binding characteristic of at least one protein molecule to a detectably labeled probe are provided.

2019017, Jun 13, 2019

Oct 12, 2018

16/158853

- Herculer CA, US
Ning LIU - Fremont CA, US
Kevin McDONALD - Novato CA, US
Aran PAULUS - San Jose CA, US
Anton POSCH - Grafing, DE

G01N 33/53
G16B 99/00
G06T 11/60
G01N 33/68
G06T 7/00

Disclosed herein are methods of protein quantification and normalization using haloalkylated tryptophan fluorescence. Complex protein samples, i.e., samples that each contain 1,000 or more distinct proteins, from diverse sources that do not have common protein profiles are treated with a halo-substituted organic compound (i.e. haloalkane) that reacts with tryptophan residues to form fluorescent products. Irradiation of the samples with ultraviolet light and the detection and quantification of the resultant fluorescent emissions from all proteins in each sample are then used to obtain comparative values for total protein content among the various samples. The values thus obtained are found to be valid indications of comparative total protein content, despite the fact that the tryptophan levels vary widely among the various proteins in any single sample and the samples, due to the diversity of their origins, tend to differ among themselves in the identities and relative amounts of the proteins that they contain. Protein samples are also normalized to correct for differences in sample dilution, sample loading, and protein transfer inconsistencies, by using stain-free detection of total protein in each of the samples, or detection of subsamples within each sample.

2017003, Feb 2, 2017

Oct 13, 2016

15/293154

- Hercules CA, US
Ning Liu - Fremont CA, US
Kevin McDonald - Novato CA, US
Aran Paulus - San Jose CA, US
Anton Posch - Grafing, DE

G01N 33/68
G06T 7/00
G06T 11/60
G06F 19/10

Disclosed herein are methods of protein quantification and normalization using haloalkylated tryptophan fluorescence. Complex protein samples, i.e., samples that each contain 1,000 or more distinct proteins, from diverse sources that do not have common protein profiles are treated with a halo-substituted organic compound (i.e. haloalkane) that reacts with tryptophan residues to form fluorescent products. Irradiation of the samples with ultraviolet light and the detection and quantification of the resultant fluorescent emissions from all proteins in each sample are then used to obtain comparative values for total protein content among the various samples. The values thus obtained are found to be valid indications of comparative total protein content, despite the fact that the tryptophan levels vary widely among the various proteins in any single sample and the samples, due to the diversity of their origins, tend to differ among themselves in the identities and relative amounts of the proteins that they contain. Protein samples are also normalized to correct for differences in sample dilution, sample loading, and protein transfer inconsistencies, by using stain-free detection of total protein in each of the samples, or detection of subsamples within each sample.

2016021, Jul 28, 2016

Jan 21, 2016

15/003536

- Hercules CA, US
Ning Liu - Hercules CA, US

G01N 33/543

Immunoblotting systems and method are provided. In one embodiment, the method may be achieved by applying an antibody solution to a surface of a membrane having an optically detectable protein and a target protein transferred thereon, wherein the application of the antibody solution is guided by a signal emitted from the optically detectable protein; and detecting the target protein. Systems and other methods are also described and illustrated.