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US Patent 8257699 Soluble glycosaminoglycanases and methods of preparing and using soluble glycosaminoglycanases

Patent 8257699 was granted and assigned to Halozyme, Inc. on September, 2012 by the United States Patent and Trademark Office.

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Contents

Is a
Patent
Patent

Patent attributes

Current Assignee
‌
Halozyme, Inc.
Patent Jurisdiction
United States Patent and Trademark Office
United States Patent and Trademark Office
Patent Number
8257699
Patent Inventor Names
Anirban Kundu0
Gregory I. Frost0
Louis H. Bookbinder0
Date of Patent
September 4, 2012
Patent Application Number
13374248
Date Filed
December 15, 2011
Patent Citations Received
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US Patent 12123035 PH20 polypeptide variants, formulations and uses thereof
0
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US Patent 12060590 PH20 polypeptide variants, formulations and uses thereof
0
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US Patent 12077791 PH20 polypeptide variants with a modification at position 309 of the PH20 polypeptide and a method of making thereof
0
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US Patent 12091692 PH20 polypeptide variants, formulations and uses thereof
0
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US Patent 12104184 PH20 polypeptide variants, formulations and uses thereof
0
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US Patent 12104185 PH20 polypeptide variants, formulations and uses thereof
0
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US Patent 12110520 PH20 polypeptide variants, formulations and uses thereof
0
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US Patent 11952600 PH20 polypeptide variants, formulations and uses thereof
0
...
Patent Primary Examiner
‌
Nashaat Nashed
Patent abstract

The invention relates to the discovery of novel soluble neutral active Hyaluronidase Glycoproteins (sHASEGPs), methods of manufacture, and their use to facilitate administration of other molecules or to alleviate glycosaminoglycan associated pathologies. Minimally active polypeptide domains of the soluble, neutral active sHASEGP domains are described that include asparagine-linked sugar moieties required for a functional neutral active hyaluronidase domain. Included are modified amino-terminal leader peptides that enhance secretion of sHASEGP. The invention further comprises sialated and pegylated form of a recombinant sHASEGP to enhance stability and serum pharmacokinetics over naturally occurring slaughterhouse enzymes. Further described are suitable formulations of a substantially purified recombinant sHASEGP glycoprotein derived from a eukaryotic cell that generate the proper glycosylation required for its optimal activity.

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