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Sangamo BioSciences Reports Fourth Quarter And Full Year 2012 Financial Results
Date:2/6/2013

ageable Platform For Protein Replacement Therapies at the American Society Of Hematology Meeting (ASH). New pre-clinical data were presented demonstrating the successful application of Sangamo's In Vivo Protein Replacement PlatformTM. Based on the Company's zinc finger DNA-binding protein nuclease (ZFN) genome-editing technology, the platform enables the permanent production of therapeutic proteins from the liver with a single systemic treatment, potentially providing curative treatments for a range of monogenic diseases including hemophilia and lysosomal storage diseases (LSD) such as Gaucher and Fabry disease. Such diseases are currently treated by regular infusions of protein or enzyme replacement therapy (ERT) throughout the patient's life.
  • First Presentation of Data from ZFP Therapeutic® for Huntington's Disease at 2012 Annual Meeting of Society for Neuroscience. Data from Sangamo's program with Shire AG (LSE: SHP, NASDAQ: SHPG) to develop a novel ZFP Therapeutic approach to Huntington's disease (HD), an inherited progressive neurodegenerative disease, were presented at the 2012 Annual Meeting of the Society for Neuroscience, the world's largest forum for neuroscientists.  The data demonstrate that Sangamo's ZFP gene regulation technology (ZFP TF) can be used to selectively repress the expression of the mutant disease-causing form of the huntingtin gene (HTT) while leaving expression levels of the normal gene unchanged in cells derived from HD patients. Research in animal models of the disease has shown that lowering the levels of the defective HTT protein can prevent, or even reverse, disease progression.  Sangamo's ZFP approach is unique in that it selectively shuts down the disease-causing HTT gene copy at the DNA-level while preserving activity of the normal gene copy.
  • Financial Guidance for 2013

  • Cash and Investments: Sangamo expects that its cash, cash equivalents and marketable securities will be at lea
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