Abstract: The present disclosure presents a general approach to engineering existing protein-protein interactions through domain addition and evolution. The disclosure teaches the creation of novel fusion proteins that include knottin peptides where a portion of the knottin peptide is replaced with a sequence that has been created for binding to a particular target. Such fusion proteins can also be bispecific or multi specific in that they can bind to and/or inhibit two or more receptors or receptor ligands. Knottins may be fused with an existing ligand (or receptor) as a general platform tor increasing the affinity of a ligand-receptor interaction or for creating a multi specific protein. In addition, the fusion proteins may comprise a knottin peptide fused to another protein where the other protein facilitates proper expression and folding of the knottin.

Abstract: The present disclosure presents a general approach to engineering existing protein-protein interactions through domain addition and evolution. The disclosure teaches the creation of novel fusion proteins that include knottin peptides where a portion of the knottin peptide is replaced with a sequence that has been created for binding to a particular target. Such fusion proteins can also be bispecific or multi specific in that they can bind to and/or inhibit two or more receptors or receptor ligands. Knottins may be fused with an existing ligand (or receptor) as a general platform tor increasing the affinity of a ligand-receptor interaction or for creating a multi specific protein. In addition, the fusion proteins may comprise a knottin peptide fused to another protein where the other protein facilitates proper expression and folding of the knottin.

Abstract: The present disclosure presents a general approach to engineering existing protein-protein interactions through domain addition and evolution. The disclosure teaches the creation of novel fusion proteins that include knottin peptides where a portion of the knottin peptide is replaced with a sequence that has been created for binding to a particular target. Such fusion proteins can also be bispecific or multi specific in that they can bind to and/or inhibit two or more receptors or receptor ligands. Knottins may be fused with an existing ligand (or receptor) as a general platform tor increasing the affinity of a ligand-receptor interaction or for creating a multi specific protein. In addition, the fusion proteins may comprise a knottin peptide fused to another protein where the other protein facilitates proper expression and folding of the knottin.

Abstract: The NK1 fragment of hepatocyte growth factor (HGF) binds to and activates the Met receptor, a transmembrane receptor tyrosine kinase that plays a critical role in embryonic development and organ formation. The instant application discloses NK1 variant polypeptides which act as agonists or antagonists of HGF. Further disclosed are covalently linked NK1 variant polypeptides. Many of the disclosed variant polypeptides possess improved stability characteristics.

Abstract: The present disclosure presents a general approach to engineering existing protein-protein interactions through domain addition and evolution. The disclosure teaches the creation of novel fusion proteins that include knottin peptides where a portion of the knottin peptide is replaced with a sequence that has been created for binding to a particular target. Such fusion proteins can also be bispecific or multi specific in that they can bind to and/or inhibit two or more receptors or receptor ligands. Knottins may be fused with an existing ligand (or receptor) as a general platform tor increasing the affinity of a ligand-receptor interaction or for creating a multi specific protein. In addition, the fusion proteins may comprise a knottin peptide fused to another protein where the other protein facilitates proper expression and folding of the knottin.

Abstract: The present disclosure presents a general approach to engineering existing protein-protein interactions through domain addition and evolution. The disclosure teaches the creation of novel fusion proteins that include knottin peptides where a portion of the knottin peptide is replaced with a sequence that has been created for binding to a particular target. Such fusion proteins can also be bispecific or multi specific in that they can bind to and/or inhibit two or more receptors or receptor ligands. Knottins may be fused with an existing ligand (or receptor) as a general platform for increasing the affinity of a ligand-receptor interaction or for creating a multi specific protein. In addition, the fusion proteins may comprise a knottin peptide fused to another protein where the other protein facilitates proper expression and folding of the knottin.

Abstract: According to one aspect, embodiments of the invention provide a power circuit comprising an input to receive input AC power from an AC source, an auxiliary charger configured to convert the input AC power from the input into DC power, a differential amplifier configured to be powered by the DC power from the auxiliary charger, to monitor the input AC voltage level of the input AC power, and to generate a sense signal based on a status of the input AC voltage level, and a processor coupled to the auxiliary charger and the differential amplifier, the processor configured to be coupled to an LPS, to be powered into a low power mode by the DC power from the auxiliary charger, and to analyze the sense signal from the differential amplifier in the low power mode of operation. According to one embodiment, the auxiliary charger is an offline DC-DC converter.

Abstract: According to one aspect, embodiments of the invention provide a power circuit comprising an input to receive input AC power from an AC source, an auxiliary charger configured to convert the input AC power from the input into DC power, a differential amplifier configured to be powered by the DC power from the auxiliary charger, to monitor the input AC voltage level of the input AC power, and to generate a sense signal based on a status of the input AC voltage level, and a processor coupled to the auxiliary charger and the differential amplifier, the processor configured to be coupled to an LPS, to be powered into a low power mode by the DC power from the auxiliary charger, and to analyze the sense signal from the differential amplifier in the low power mode of operation. According to one embodiment, the auxiliary charger is an offline DC-DC converter.

Abstract: A data transmission system includes a device and a base. The base includes a near field communication (NFC) module and a processing module configured to determine whether a wireless network exits. The NFC module includes a determining unit configured to determine whether the NFC module writes a predetermined tag after the processing module determines the wireless network exits and configured to determine whether the predetermined tag is an authorization code, a sending unit configured to send a service set identifier (SSID) and a password to the device after the predetermined tag is the authorization code, and a control unit configured to switch an input mode of the base to a wireless network mode after the SSID and the password are sent to the device. The device is configured to be connected to the wireless network after receiving the SSID and the password. A communication method is also provided.

Abstract: The NK1 fragment of hepatocyte growth factor (HGF) binds to and activates the Met receptor, a transmembrane receptor tyrosine kinase that plays a critical role in embryonic development and organ formation. The instant application discloses NK1 variant polypeptides which act as agonists or antagonists of HGF. Further disclosed are covalently linked NK1 variant polypeptides. Many of the disclosed variant polypeptides possess improved stability characteristics.

Abstract: The NK1 fragment of hepatocyte growth factor (HGF) binds to and activates the Met receptor, a transmembrane receptor tyrosine kinase that plays a critical role in embryonic development and organ formation. The instant application discloses NK1 variant polypeptides which act as agonists or antagonists of HGF. Further disclosed are covalently linked NK1 variant polypeptides. Many of the disclosed variant polypeptides possess improved stability characteristics.

Abstract: A data transmission system includes a device and a base. The base includes a near field communication (NFC) module and a processing module configured to determine whether a wireless network exits. The NFC module includes a determining unit configured to determine whether the NFC module writes a predetermined tag after the processing module determines the wireless network exits and configured to determine whether the predetermined tag is an authorization code, a sending unit configured to send a service set identifier (SSID) and a password to the device after the predetermined tag is the authorization code, and a control unit configured to switch an input mode of the base to a wireless network mode after the SSID and the password are sent to the device. The device is configured to be connected to the wireless network after receiving the SSID and the password. A communication method is also provided.

Abstract: The present disclosure presents a general approach to engineering existing protein-protein interactions through domain addition and evolution. The disclosure teaches the creation of novel fusion proteins that include knottin peptides where a portion of the knottin peptide is replaced with a sequence that has been created for binding to a particular target. Such fusion proteins can also be bispecific or multi specific in that they can bind to and/or inhibit two or more receptors or receptor ligands. Knottins may be fused with an existing ligand (or receptor) as a general platform for increasing the affinity of a ligand-receptor interaction or for creating a multi specific protein. In addition, the fusion proteins may comprise a knottin peptide fused to another protein where the other protein facilitates proper expression and folding of the knottin.

Abstract: The NK1 fragment of hepatocyte growth factor (HGF) binds to and activates the Met receptor, a transmembrane receptor tyrosine kinase that plays a critical role in embryonic development and organ formation. The instant application discloses NK1 variant polypeptides which act as agonists or antagonists of HGF. Further disclosed are covalently linked NK1 variant polypeptides. Many of the disclosed variant polypeptides possess improved stability characteristics.