Abstract: Provided is a fusion protein of insulin and an immunoglobulin Fc region. Specifically, the present invention relates to an insulin fusion protein having a prolonged in vivo half-life and stability, a preparation that contains the fusion protein, a preparation method therefor and an application thereof.

Abstract: A highly glycosylated human blood-clotting factor VIII (FVIII) fusion protein, and a manufacturing method and application of same. The fusion protein comprises, from the N-terminus to the C-terminus, a human (FVIII), a flexible peptide connector, at least one rigid unit of a human chorionic gonadotropin ?-subunit carboxyl terminal peptide, and a half-life extending portion (preferentially selected from a human IgG Fc variant). The fusion protein has a similar level of biological activity as a recombinant (FVIII) and an extended in vivo half-life, thereby improving pharmacokinetics and drug efficacy.

Abstract: Provided are a blood coagulation factor IX fusion protein with a prolonged circulation half-life, a conjugate thereof, a pharmaceutical composition containing same and the use of same in treating hemorrhagic diseases (such as hemophilia B).

Abstract: Provided by the present invention are a novel GLP-1 fusion protein and a conjugate thereof, a pharmaceutical composition containing same, and a use thereof in reducing blood sugar or body weight, especially for treating diabetes, in particular type II diabetes.

Abstract: Disclosed are a coagulation factor VIII fusion protein which is conjugated with polyalkylene glycol and which has an extended cyclic half-life, a preparation method therefor and a use thereof, wherein the active moiety of the coagulation factor VIII is directly linked or indirectly linked by a peptide linker to a fusion partner, and the fusion protein is further conjugated to a polyalkylene glycol. The half-life is significantly increased compared to an FVIII fusion protein modified without polyalkylene glycol.

Abstract: A highly glycosylated human blood-clotting factor VIII (FVIII) fusion protein, and a manufacturing method and application of same. The fusion protein comprises, from the N-terminus to the C-terminus, a human (FVIII), a flexible peptide connector, at least one rigid unit of a human chorionic gonadotropin ?-subunit carboxyl terminal peptide, and a half-life extending portion (preferentially selected from a human IgG Fc variant). The fusion protein has a similar level of biological activity as a recombinant (FVIII) and an extended in vivo half-life, thereby improving pharmacokinetics and drug efficacy.

Abstract: Methods for treating an infection in a tissue sample are described. Tissue samples that are harvested from a patient may be infected with either bacteria or a virus. A rhodamine compound is mixed with the infected tissue sample to form a mixture. The mixture is then exposed to radiant energy to inhibit or kill the bacteria. The exposed mixture is then transplanted into the patient. The rhodamine compounds may be 2?-(6-dimethylamino-3-dimethylimino-3H-xanthen-9-yl) 4?, 5?-dichloro-benzoic acid methyl ester hydrochloride.

Abstract: Methods for treating an infection in a tissue sample are described. Tissue samples that are harvested from a patient may be infected with either bacteria or a virus. A rhodamine compound is mixed with the infected tissue sample to form a mixture. The mixture is then exposed to radiant energy to inhibit or kill the bacteria. The exposed mixture is then transplanted into the patient. The rhodamine compounds may be 2?-(6-dimethylamino-3-dimethylimino-3H-xanthen-9-yl)4?,5?-dichloro-benzoic acid methyl ester hydrochloride.

Abstract: Methods for treating a bacterial infection in a tissue sample are described. Tissue samples that are harvested from a patient may be infected with bacteria. A rhodamine compound is mixed with the infected tissue sample to form a mixture. The mixture is then exposed to radiant energy to inhibit or kill the bacteria. The exposed mixture is then transplanted into the patient.

Abstract: Methods for treating a bacterial infection in a tissue sample are described. Tissue samples that are harvested from a patient may be infected with bacteria. A rhodamine compound is mixed with the infected tissue sample to form a mixture. The mixture is then exposed to radiant energy to inhibit or kill the bacteria. The exposed mixture is then transplanted into the patient.

Abstract: Methods for treating a bacterial infection in a tissue sample are described. Tissue samples that are harvested from a patient may be infected with bacteria. A rhodmaine compound is mixed with the infected tissue sample to form a mixture. The mixture is then exposed to radiant energy to inhibit or kill the bacteria. The exposed mixture is then transplanted into the patient.

Abstract: Compounds of formula (I) wherein: one of R1, R2, R3, R4 and (R10)n represents halogen and each remaining R1, R2, R3, R4 and R10 group is independently selected from hydrogen, halogen, amino, acylamino, dialkylamino, cycloalkylamino, azacycloalkyl, alkylcycloalkylamino, aroylamino, diarylamino, arylalkylamino, aralkylamino, alkylaralkylamino, arylaralkylamino, hydroxy, alkoxy, aryloxy, aralkyloxy, mercapto, alkylthio, arylthio, aralkylthio, carboxyl, alkoxycarbonyl, aryloxycarbonyl, aralkoxycarbonyl, carbamoyl, alkylcarbamoyl, dialkylcarbamoyl, cyano, hydroxysulfonyl, amidosulfonyl, dialkylamidosulfonyl, arylalkylamidosulfonyl, formyl, acyl, aroyl, alkyl, alkylene, alkenyl, aryl, aralkyl, vinyl, alkynyl, and corresponding substituted groups; m=0-1; n=1-4, A is nil, O, or NH; R9 is alkylene; -Z is H, amino, dialkylamino, or a trialkylamino salt; X? is an anion; R5, R6, R7 and R8 are independently H or C1-C6 alkyl or R1 in combination with R5 or R6, or R2 in combination with R5 or R6, or R3 in combination wi

Abstract: Compounds of formula I: in which one of R1, R2, R3, R4 and (R10)n represents halogen and each of the remaining R1, R2, R3, R4 and R10 groups is independently selected from hydrogen, halogen, amino, acylamino, dialkylamino, cycloalkylamino, azacycloalkyl, alkylcycloalkylamino, aroylamino, diarylamino, arylalkylamino, aralkylamino, alkylaralkylamino, arylaralkylamino, hydroxyl, alkoxy, aryloxy, aralkyloxy, mercapto, alkylthio, arylthio, aralkylthio, carboxyl, alkoxycarbonyl, aryloxycarbonyl, aralkoxycarbonyl, carbamoyl, alkylcarbamoyl, dialkylcarbamoyl, cyano, hydroxysulfonyl, amidosulfonyl, dialkylamidosulfonyl, arylalkylamido-sulfonyl, formyl, acyl, aroyl, alkyl, alkylene, alkenyl, aryl, aralkyl, vinyl, alkynyl and corresponding substituted groups; m=0-1; n=1-4; A is nil, O or NH; R9 is alkylene, Z is H, amino, dialkylamino or trialkylamino salt; X is an anion; and R5, R6, R7 and R8 are independently selected from H and C1-6 alkyl, or R1 with R5 or R6, or R2 with R5 or R6, or R3 with R7 or R8 represents a

Abstract: Methods for selecting and identifying modified toxins and conjugates thereof are provided. The methods are select for toxins that exhibit reduced toxicity to the host cell in which they are expressed. Methods of increasing production of toxins, such as the modified toxins, or conjugates thereof, also are provided. In particular, in the methods the toxins, or conjugates thereof, are produced in the presence of an inhibitor molecule. Also provided, are modified toxins and conjugates thereof. Such conjugates can be used in the treatment of various disease or disorders associated with proliferation, migration, and physiological activity of cells involved in immune or inflammatory responses.

Abstract: This invention is directed to Flavobacterium heparinum for use as a host cell organism for the expression of homologous and heterologous genes.

Abstract: This invention is directed to Flavobacterium heparinum for use as a host cell organism for the expression of homologous and heterologous genes.

Abstract: Novel compounds of the formula (I) wherein: one of R1, R2, R3, R4, and (R10)n represents an halogen atom and each of the remaining R1, R2, R3, R4, and each of the remaining R10 group is independently selected in the group constituted by hydrogen, halogen atoms, an amino, acylamino, dialkylamino, cycloalkylamino, azacycloalkyl, alkylcycloalkylamino, aroylamino, diarylamino, arylalkylamino, aralkylamino, alkylaralkylamino, arylaralkylamino, hydroxy, alkoxy, aryloxy, aralkyloxy, mercapto, alkylthio, arylthio, aralkylthio, carboxyl, alkoxycarbonyl, aryloxycarbonyl, aralkoxycarbonyl, carbamoyl, alkylcarbamoyl, dialkylcarbamoyl, cyano, hydroxysulfonyl, amidosulfonyl, dialkylamidosulfonyl, arylalkylamidosulfonyl, formyl, acyl, aroyl, alkyl, alkylene, alkenyl, aryl, aralkyl, vinyl, alkynyl group and by the corresponding substituted groups; —m=0-1; n=1-4, A is nil, O, or NH; R9 represents an alkylene group; —Z is H, amino, dialkylamino, or trialkylamino salt; X—is an anion; R5, R6, R7 a

Abstract: The invention relates to the stabilization of enzymes through the formation of matrix stabilized enzyme crystals. A matrix stabilized enzyme crystal is formed through cross-linking a polymer having one or more reactive moieties with an enzyme crystal using a low concentration of a multi-functional cross-linking reagent. The invention includes matrix stabilized enzyme crystals of phenylalanine ammonia lyase and a method of using to treat hyperphenylalaninemia.

Abstract: This invention is directed to Flavobacterium heparinum for use as a host cell organism for the expression of homologous and heterologous genes.

Abstract: The present invention describes the isolation and sequence of genes from Flavobacterium heparinum encoding heparin and heparan sulfate degrading enzymes, heparinase II and heparinase III (EC 4.2.2.8). It further describes a method of expressing and an expression for heparinases I, II and III using a modified ribosome binding region derived from a promoter from glycosaminoglycan lyase genes of F. heparinum. Also, a multi-step protein purification method incorporating cell disruption, cation exchange chromatography, affinity chromatography and hydroxylapatite chromatography is outlined. Antibodies against a post-translational modification moiety common to Flavobacterium heparinum proteins and a method to obtain antibodies specific to these moieties and to the amino acid sequences of heparinases I, II and III are described.