Hung T Do

US Patent:

20100119502, May 13, 2010

Filed:

Nov 11, 2009

Appl. No.:

12/616670

Inventors:

Hung V. Do - New Hope PA, US
Ken Valenzano - East Brunswick NJ, US
David J. Lockhart - Del Mar CA, US

Assignee:

AMICUS THERAPEUTICS, INC. - Cranbury NJ

International Classification:

A61K 38/47
A61P 43/00

US Classification:

424 9461

Abstract:

The present application provides a method for treating Pompe disease in a subject in need thereof, that includes a method of administering to the subject a GAA enzyme in combination with an ASSC for the GAA enzyme. The present application also provides methods for increasing the in vitro and in vivo stability of a GAA enzyme formulation.

US Patent:

20110070643, Mar 24, 2011

Filed:

May 26, 2010

Appl. No.:

12/788068

Inventors:

Hung V. Do - New Hope PA, US

International Classification:

C12N 5/07

US Classification:

435357, 435375, 435358, 435367, 435369, 435365, 435354

Abstract:

The present invention provides methods for improving the production of recombinant proteins through the use of pharmacological chaperones for the recombinant proteins. As exemplified by the present invention, the binding of a pharmacological chaperone to a recombinant protein expressed by a cell can stabilize the protein and increase export of the protein out of the cell's endoplasmic reticulum, and increase secretion of the protein by the cell.

US Patent:

20110143419, Jun 16, 2011

Filed:

Nov 22, 2010

Appl. No.:

12/952036

Inventors:

Hung V. Do - New Hope PA, US

International Classification:

C12N 9/26
C12N 9/42

US Classification:

435201, 435209

Abstract:

The present invention provides methods for improving the production of recombinant proteins through the use of pharmacological chaperones for the recombinant proteins. As exemplified by the present invention, the binding of a pharmacological chaperone to a recombinant protein expressed by a cell can stabilize the protein and increase export of the protein out of the cell's endoplasmic reticulum, and increase secretion of the protein by the cell.

US Patent:

20110268721, Nov 3, 2011

Filed:

May 11, 2011

Appl. No.:

13/105720

Inventors:

Hung V. Do - New Hope PA, US
Ken Valenzano - East Brunswick NJ, US
David J. Lockhart - Solana Beach CA, US

Assignee:

Amicus Therapeutics, Inc. - Cranbury NJ

International Classification:

A61K 38/47
A61P 3/00

US Classification:

424 9461

Abstract:

The present application provides a method for treating Pompe disease in a subject in need thereof, that includes a method of administering to the subject a GAA enzyme in combination with an ASSC for the GAA enzyme. The present application also provides methods for increasing the in vitro and in vivo stability of a GAA enzyme formulation.

US Patent:

20120083010, Apr 5, 2012

Filed:

Aug 18, 2011

Appl. No.:

13/212917

Inventors:

Hung V. Do - New Hope PA, US
Brian E. Rane - Somerset NJ, US
John Flanagan - East Windsor NJ, US

International Classification:

C12Q 1/34

US Classification:

435 18

Abstract:

Provided is a method for diagnosing Pompe disease in a patient by measuring acid α-glucosidase activity in a sample from the patient. The invention also provides a method for monitoring the treatment of Pompe disease with specific pharmacological chaperones by measuring acid α-glucosidase activity in a sample from the patient.

US Patent:

20130344054, Dec 26, 2013

Filed:

Nov 8, 2011

Appl. No.:

13/884126

Inventors:

Hung Do - New Hope PA, US

Assignee:

Callidus Biopharama, Inc. - Doylastown PA

International Classification:

C12N 9/24

US Classification:

424 9461, 435200, 536 232

Abstract:

Described herein are variant, recombinant β-glucocerebrosidase proteins characterized as having increased stability relative to recombinant wild-type β-glucocerebrosidase. Also provided herein are variant, recombinant β-glucocerebrosidase proteins characterized as retaining more catalytic activity relative to recombinant wild-type β-glucocerebrosidase. Further described herein are variant, recombinant β-glucocerebrosidase proteins that can have amino acid variations at one or more of the following positions: 316, 317, 321 and 145. Methods of making the variant, recombinant β-glucocerebrosidase proteins are also described as well as methods of treating patients having lysosomal storage diseases.

US Patent:

20140045216, Feb 13, 2014

Filed:

Nov 22, 2011

Appl. No.:

13/988946

Inventors:

Hung Do - New Hope PA, US

Assignee:

Callidus Biopharma, Inc. - Doylestown PA

International Classification:

C07K 14/47
C12N 9/24

US Classification:

435 697, 435188, 4353201, 530303, 530324, 530351, 5303873

Abstract:

Polypeptide signal sequences of modified fragments of human immunoglobulin heavy chain binding protein (Bip) are disclosed. Also disclosed are fusion proteins comprising a modified fragment of human immunoglobulin heavy chain binding protein (Bip) operably linked to a heterologous polypeptide. Also disclosed are protein expression vectors comprising a promoter operably linked to a first DNA sequence encoding a signal sequence comprising a modified fragment of human immunoglobulin heavy chain binding protein (Bip) and a second DNA sequence encoding a heterologous polypeptide fused in frame to the first DNA sequence. Further disclosed are methods of producing a polypeptide comprising expressing a fusion protein comprising a polypeptide signal sequences of modified fragments of human immunoglobulin heavy chain binding protein (Bip) operably linked to a heterologous polypeptide and recovering the heterologous polypeptide.

US Patent:

20210261935, Aug 26, 2021

Filed:

Feb 23, 2021

Appl. No.:

17/249175

Inventors:

- Philadelphia PA, US
Hung V. Do - New Hope PA, US

International Classification:

C12N 9/40
A61K 48/00
C12N 15/09

Abstract:

Recombinant human alpha glucosidase (rhGAA) composition derived from CHO cells that contains a more optimized glycan composition consisting of a higher amount of rhGAA containing N-glycans carrying mannose-6-phosphate (M6P) or bis-M6P than conventional rhGAAs, along with low amount of non-phosphorylated high mannose glycans, and low amount of terminal galactose on complex oligosaccharides. Compositions containing the rhGAA, and methods of use are described.