Abstract: A fusion protein having a non-immunoglobulin polypeptide having a cysteine residue proximal to the C terminal thereof, and an immunoglobulin component with a mutated hinge region is provided. The mutation comprises a point mutated site corresponding in position to the position in a native hinge region of the cysteine residue located nearest the cysteine residue of the non-Ig component. The distance from the cysteine residue of the non-immunoglobulin polypeptide and any remaining cysteine residues of the mutated hinge region is sufficient to prevent the formation of a disulphide bond therebetween.

Abstract: A recombinant fusion protein comprising a human erythropoietin peptide portion linked to an immunoglobulin peptide portion is described. The fusion protein has a prolonged half-life in vivo in comparison to naturally occurring or recombinant native human erythropoietin. In one embodiment of the invention, the protein has a half-life in vivo at least three fold higher than native human erythropoietin. The fusion protein also exhibits enhanced erythropoietic bioactivity in comparison to native human erythropoietin. In one embodiment, the fusion protein comprises the complete peptide sequence of a human erythropoietin (EPO) molecule and the peptide sequence of an Fc fragment of human immunoglobulin IgG1. The Fc fragment in the fusion protein includes the hinge region, CH2 and CH3 domains of human immunoglobulin IgG1. The EPO molecule may be linked directly to the Fc fragment to avoid extraneous peptide linkers and lessen the risk of an immunogenic response when administered in vivo.

Abstract: Disclosed are a yttrium-doped barium fluoride crystal and a preparation method and the use thereof, wherein the yttrium-doped barium fluoride crystal has a chemical composition of Ba(1?x)YxF2+x, in which 0.01?x?0.50. The yttrium-doped BaF2 crystal of the present invention has improved scintillation performance. The yttrium doping may greatly suppress the slow luminescence component of the BaF2 crystal and has an excellent fast/slow scintillation component ratio. The doped crystal is coupled to an optical detector to obtain a scintillation probe which is applicable to the fields of high time resolved measurement radiation such as high-energy physics, nuclear physics, ultrafast imaging and nuclear medicine imaging.

Abstract: A fusion protein having a non-immunoglobulin polypeptide having a cysteine residue proximal to the C terminal thereof, and an immunoglobulin component with a mutated hinge region is provided. The mutation comprises a point mutated site corresponding in position to the position in a native hinge region of the cysteine residue located nearest the cysteine residue of the non-Ig component. The distance from the cysteine residue of the non-immunoglobulin polypeptide and any remaining cysteine residues of the mutated hinge region is sufficient to prevent the formation of a disulphide bond therebetween.

Abstract: Methods for altering leptin resistance and the hormonal control of energy balance, and methods for treating obesity and diabetes, as well as promoting weight gain, using batotin and batotin inhibitors.

Abstract: This application relates to recombinant human interferon-like proteins. In one embodiment a recombinant protein created by gene shuffling technology is described having enhanced anti-viral and anti-proliferative activities in comparison to naturally occurring human interferon like alpha 2b (HuIFN-?2b). The invention encompasses a polynucleotide encoding the protein and recombinant vectors and host cells comprising the polynucleotide. Preferably the polynucleotide is selected from the group of polynucleotides each having a sequence at least 93% identical to SEQ ID: No. 1 and the protein is selected from the group of proteins each having an amino acid sequence at least 85% identical to SEQ ID No: 2. The proteins and compositions comprising the proteins can be used for treatment of conditions responsive to interferon therapy, such as viral diseases and cancer.

Abstract: Embodiments disclosed herein relate to a light emitting device, comprising a first substrate, a pixel isolation structure, electroluminescent structures, and a second substrate, the first substrate and the second substrate are oppositely disposed, and the second substrate is disposed on one side of pixel isolation structure far away from the first substrate, the pixel isolation structure is disposed on the surface of one side of first substrate, the pixel isolation structure forms a plurality of mutually isolated sub-pixel regions on the surface of first substrate, electroluminescent structures are disposed on a portion of first substrate corresponding to each sub-pixel region, the sub-pixel regions further comprise: a quantum dot layer disposed in at least one sub-pixel region, wherein quantum dot layer in each sub-pixel region is located on one side of electroluminescent structures far away from first substrate or located between electroluminescent structure and first substrate.

Abstract: Disclosed are a yttrium-doped barium fluoride crystal and a preparation method and the use thereof, wherein the yttrium-doped barium fluoride crystal has a chemical composition of Ba(1?x)YxF2+x, in which 0.01?x?0.50. The yttrium-doped BaF2 crystal of the present invention has improved scintillation performance. The yttrium doping may greatly suppress the slow luminescence component of the BaF2 crystal and has an excellent fast/slow scintillation component ratio. The doped crystal is coupled to an optical detector to obtain a scintillation probe which is applicable to the fields of high time resolved measurement radiation such as high-energy physics, nuclear physics, ultrafast imaging and nuclear medicine imaging.

Abstract: This application relates to recombinant human interferon-like proteins. In one embodiment a recombinant protein created by gene shuffling technology is described having enhanced anti-viral and anti-proliferative activities in comparison to naturally occurring human inteferon like alpha 2b (HuIFN-?2b). The invention encompasses a polynucleotide encoding the protein and recombinant vectors and host cells comprising the polynucleotide. Preferably the polynucleotide is selected from the group of polynucleotides each having a sequence at least 93% identical to SEQ ID: No. 1 and the protein is selected from the group of proteins each having an amino acid sequence at least 85% identical to SEQ ID No: 2. The proteins and compositions comprising the proteins can be used for treatment of conditions responsive to interferon, therapy, such as viral diseases and cancer.

Abstract: Embodiments disclosed herein relate to a light emitting device, comprising a first substrate, a pixel isolation structure, electroluminescent structures, and a second substrate, the first substrate and the second substrate are oppositely disposed, and the second substrate is disposed on one side of pixel isolation structure far away from the first substrate, the pixel isolation structure is disposed on the surface of one side of first substrate, the pixel isolation structure forms a plurality of mutually isolated sub-pixel regions on the surface of first substrate, electroluminescent structures are disposed on a portion of first substrate corresponding to each sub-pixel region, the sub-pixel regions further comprise: a quantum dot layer disposed in at least one sub-pixel region, wherein quantum dot layer in each sub-pixel region is located on one side of electroluminescent structures far away from first substrate or located between electroluminescent structure and first substrate.

Abstract: A recombinant fusion protein comprising a human erythropoietin peptide portion linked to an immunoglobulin peptide portion is described. The fusion protein has a prolonged half-life in vivo compared to naturally occurring or recombinant native human erythropoietin. In one embodiment, the protein has a half-life in vivo at least three-fold higher than native human erythropoietin. The fusion protein exhibits enhanced erythropoietic bioactivity compared to native human erythropoietin. In one embodiment, the fusion protein comprises the complete peptide sequence of a human erythropoietin (EPO) molecule and the peptide sequence of an Fc fragment of human IgG1, which Fc fragment includes the hinge region, CH2 and CH3 domains. The EPO molecule may be linked directly to the Fc fragment to avoid extraneous peptide linkers and lessen risk of an immunogenic response when administered. In one embodiment the hinge region is a human Fc fragment variant having a non-cysteine residue at amino acid 6.

Abstract: This application relates to recombinant human interferon-like proteins. In one embodiment a recombinant protein created by gene shuffling technology is described having enhanced anti-viral and anti-proliferative activities in comparison to naturally occurring human inteferon like alpha 2b (HuIFN-?2b). The invention encompasses a polynucleotide encoding the protein and recombinant vectors and host cells comprising the polynucleotide. Preferably the polynucleotide is selected from the group of polynucleotides each having a sequence at least 93% identical to SEQ ID: No. 1 and the protein is selected from the group of proteins each having an amino acid sequence at least 85% identical to SEQ ID No: 2. The proteins and compositions comprising the proteins can be used for treatment of conditions responsive to interferon, therapy, such as viral diseases and cancer.

Abstract: A recombinant fusion protein comprising a human erythropoietin peptide portion linked to an immunoglobulin peptide portion is described. The fusion protein has a prolonged half-life in vivo in comparison to naturally occurring or recombinant native human erythropoietin. In one embodiment of the invention, the protein has a half-life in vivo at least three fold higher than native human erythropoietin. The fusion protein also exhibits enhanced erythropoietic bioactivity in comparison to native human erythropoietin. In one embodiment, the fusion protein comprises the complete peptide sequence of a human erythropoietin (EPO) molecule and the peptide sequence of an Fc fragment of human immunoglobulin IgG1. The Fc fragment in the fusion protein includes the hinge region, CH2 and CH3 domains of human immunoglobulin IgG1. The EPO molecule may be linked directly to the Fc fragment to avoid extraneous peptide linkers and lessen the risk of an immunogenic response when administered in vivo.

Abstract: A recombinant fusion protein comprising a human erythropoietin peptide portion linked to an immunoglobulin peptide portion is described. The fusion protein has a prolonged half-life in vivo in comparison to naturally occurring or recombinant native human erythropoietin. In one embodiment of the invention the protein has a half-life in vivo at least three fold higher than native human erythropoietin. The fusion protein also exhibits enhanced erythropoietic bioactivity in comparison to native human erythropoietin. In one embodiment, the fusion protein comprises the complete peptide sequence of a human erythropoietin (EPO) molecule and the peptide sequence of an Fc fragment of human immunoglobulin IgG1. The Fc fragment in the fusion protein includes the hinge region, CH2 and CH3 domains of human immunoglobulin IgG1. The EPO molecule may be linked directly to the Fc fragment to avoid extraneous peptide linkers and lessen the risk of an immunogenic response when administered in vivo.

Abstract: This application relates to recombinant human interferon-like proteins. In one embodiment a recombinant protein created by gene shuffling technology in described having enhanced anti-viral and anti-proliferative activities in comparison to naturally occurring human interferon like alpha 2b (HuIFN-?2b). The invention encompasses a polynucleotide encoding the protein and recombinant vectors and host cells comprising the polynucleotide. Preferably the polynucleotide is selected from the group of polynucleotides each having a sequence at least 93% identical to SEQ ID: No. 1 and the protein is selected from the group of proteins each having an amino acid sequence at least 85% identical to SEQ ID No: 2. The proteins and compositions comprising the proteins can be used for treatment of conditions responsive to interferon therapy, such as viral diseases and cancer.

Abstract: A recombinant fusion protein comprising a human erythropoietin peptide portion linked to an immunoglobulin peptide portion is described. The fusion protein has a prolonged half-life in vivo compared to naturally occurring or recombinant native human erythropoietin. In one embodiment, the protein has a half-life in vivo at least three-fold higher than native human erythropoietin. The fusion protein exhibits enhanced erythropoietic bioactivity compared to native human erythropoietin. In one embodiment, the fusion protein comprises the complete peptide sequence of a human erythropoietin (EPO) molecule and the peptide sequence of an Fc fragment of human IgG1, which Fc fragment includes the hinge region, CH2 and CH3 domains. The EPO molecule may be linked directly to the Fc fragment to avoid extraneous peptide linkers and lessen risk of an immunogenic response when administered. In one embodiment the hinge region is a human Fc fragment variant having a non-cysteine residue at amino acid 6.

Abstract: This application relates to recombinant human interferon-like proteins. In one embodiment a recombinant protein created by gene shuffling technology in described having enhanced anti-viral and anti-proliferative activities in comparison to naturally occurring human interferon like alpha 2b (HuIFN-?2b). The invention encompasses a polynucleotide encoding the protein and recombinant vectors and host cells comprising the polynucleotide. Preferably the polynucleotide is selected from the group of polynucleotides each having a sequence at least 93% identical to SEQ ID: No. 1 and the protein is selected from the group of proteins each having an amino acid sequence at least 85% identical to SEQ ID No: 2. The proteins and compositions comprising the proteins can be used for treatment of conditions responsive to interferon therapy, such as viral diseases and cancer.

Abstract: Provided is a wire-bonding apparatus 10 including a capillary 28 through which a wire 30 is inserted, a nonsticking determination circuit 36, and a controller 80. The nonsticking determination circuit 36 applies a predetermined alternating-current electrical signal between the wire held by the capillary and the bonding target, obtains a capacitance value between the wire held by the capillary and the bonding target, determines that the wire is disconnected from the bonding target when the capacitance value decreases after the first bonding operation, and determines that the disconnected wire drops down and is brought into contact with the bonding target when the capacitance value returns to an original value before reaching the second bonding point.

Abstract: A recombinant fusion protein comprising a human erythropoietin peptide portion linked to an immunoglobulin peptide portion is described. The fusion protein has a prolonged half-life in vivo compared to naturally occurring or recombinant native human erythropoietin. In one embodiment, the protein has a half-life in vivo at least three-fold higher than native human erythropoietin. The fusion protein exhibits enhanced erythropoietic bioactivity compared to native human erythropoietin. In one embodiment, the fusion protein comprises the complete peptide sequence of a human erythropoietin (EPO) molecule and the peptide sequence of an Fc fragment of human IgG1, which Fc fragment includes the hinge region, CH2 and CH3 domains. The EPO molecule may be linked directly to the Fc fragment to avoid extraneous peptide linkers and lessen risk of an immunogenic response when administered. In one embodiment the hinge region is a human Fc fragment variant having a non-cysteine residue at amino acid 6.

Abstract: This application relates to recombinant human interferon-like proteins. In one embodiment a recombinant protein created by gene shuffling technology is described having enhanced anti-viral and anti-proliferative activities in comparison to naturally occurring human inteferon like alpha 2b(HuIFN-?2b). The invention encompasses a polynucleotide encoding the protein and recombinant vectors and host cells comprising the polynucleotide. Preferably the polynucleotide is selected from the group of polynucleotides each having a sequence at least 93% identical to SEQ ID: No. 1 and the protein is selected from the group of proteins each having an amino acid sequence at least 85% identical to SEQ ID No: 2. The proteins and compositions comprising the proteins can be used for treatment of conditions responsive to interferon therapy, such as viral diseases and cancer.