Abstract: Aspart modified proinsulin sequences that have a modified C-peptide amino acid and/or nucleic acid modification for producing aspart insulin analogs are provided. Highly efficient processes for preparing the aspart insulin analogs and improved preparations containing the aspart insulin analogs prepared according to the methods described herein are also provided.

Abstract: Lis-Pro modified proinsulin sequences that have a modified C-peptide amino acid and/or nucleic acid modification are presented. Methods for producing Lis-Pro insulin analogs are also disclosed. Highly efficient processes for preparing the Lis-Pro insulin analogs and improved preparations containing the Lis-Pro insulin analogs prepared according to the methods described herein are also provided.

Abstract: Glargine proinsulin sconstructs that have a modified C-peptide amino acid and/or nucleic acid sequence for producing glargine insulin analogs are provided. Highly efficient processes for preparing the glargine insulin analogs and improved preparations containing the glargine insulin analogs prepared according to the methods described herein are also provided.

Abstract: Disclosed herein are novel and improved preparations and methods for manufacturing substantially liquid preparations of recombinant human insulin API. The purified recombinant human insulin Active Pharmaceutical Ingredient (API) preparations are substantially free of by-products associated with the lyophilization and/or crystallization. The methods for manufacturing the substantially liquid recombinant human insulin API preparations are provided with optional steps for subjecting the recombinant insulin preparation to lyophilization and/or crystallization. Enhanced yield of recombinant insulin of greater purity are thereby provided according to the present invention. Highly purified formulations of recombinant human insulin of the API insulin preparations disclosed herein are also provided. Stably transformed E. coli cell banks (WCB) capable of expressing the recombinant human insulin are also provided.

Abstract: Preparations of recombinant human growth hormone (hGH) are provided having a purity that comprises 2% or less of a peptide other than native human growth hormone (e.g., essentially free of multimeric forms) are disclosed. Active pharmaceutical ingredient (API) preparations of recombinant hGH suitable for commercial production of formulation grade recombinant hGH are provided. A stable Master Cell Bank of transformed E. coli is also disclosed, as well as methods for creating a transformed E. coli preparation that includes a Met-AsphGH encoding sequence. Improved manufacturing methods are also presented that are suitable for large scale production of highly purified preparations of recombinant human growth hormone.

Abstract: Novel pro-insulin having specific amino acid and/or nucleic acid modifications suitable for improved methods of insulin production are provided. Novel and highly efficient processes for preparing the pro-insulin preparations and preparations containing them are also disclosed. The novel pro-insulin preparations may be converted into human insulin useful in therapeutic preparations. Novel peptides of the C-peptide, and N terminus, including RREAEALQVGQVELGGGPGAGSLQPLALEGSLQAR (SEQ ID NO: 32), and MHHHHHHGGR (SEQ ID NO: 2) respectively are provided, as well as the unique nucleic acid molecules encoding them.

Abstract: Novel pro-insulin having specific amino acid and/or nucleic acid modifications suitable for improved methods of insulin production are provided. Novel and highly efficient processes for preparing the pro-insulin preparations and preparations containing them are also disclosed. The novel pro-insulin preparations may be converted into human insulin useful in therapeutic preparations. Novel peptides of the C-peptide, and N terminus, including RREAEALQVGQVELGGGPGAGSLQPLALEGSLQAR (SEQ ID NO:32), and MHHHHHHGGR (SEQ ID NO:36) respectively are provided, as well as the unique nucleic acid molecules encoding them.