4results about How to "Efficient secretion" patented technology

The application belongs to the technical field of biology, and discloses a hybridoma cell strain 2F8 secreting a calmodulin 2 monoclonal antibody, a specific monoclonal antibody, and preparation and application. The hybridoma cell strain 2F8 secreting the calmodulin 2 monoclonal antibody is classified and named as 2F8, and is preserved in the China General Microbiological Culture Collection Center on April 9, 2025, with a preservation number of CGMCC No.46343. The application also provides the calmodulin 2 monoclonal antibody secreted by the hybridoma cell strain 2F8 and a polynucleotide encoding the calmodulin 2 monoclonal antibody. The antibody has specific recognition ability for the calmodulin 2, and is suitable for immunological detection, in particular, Western-blot and immunohistochemical detection. The antibody can be used for preparing a reagent, a kit or other immunological detection product for detecting the calmodulin 2, and has practical application value.

This invention relates to the fields of microbial fermentation and genetic engineering technology, specifically disclosing a method for preparing human type III collagen fragments. Based on Pichia pastoris, this invention constructs a multidimensional synergistic expression system of "molecular chaperone co-expression - precursor supply - osmotic pressure adaptation regulation," reducing the structural instability of collagen fragments during secretion and post-processing, and constructing an expression system suitable for stable and efficient secretion of collagen fragments. The method described in this invention can achieve efficient extracellular secretory expression of human type III collagen fragments, and the obtained protein has high structural uniformity and stability, with a protein yield of up to 6.55 g / L under 5 L fermenter conditions. The method described in this invention is suitable for the large-scale preparation of human type III collagen fragments and provides a new technical solution for obtaining collagen products with high structural uniformity and good functional activity.

The application discloses a recombinant plasmid for expressing salt-tolerant protease, a yeast engineering bacterium, a fermentation medium thereof and application. Key elements for heterologous expression of the salt-tolerant protease are confirmed, and the recombinant plasmid for expressing the salt-tolerant protease and the yeast engineering bacterium are constructed. The long-term salt-tolerance level and SDS tolerance of the salt-tolerant protease expressed by the yeast engineering bacterium are significantly improved, and the salt-tolerant protease can effectively and significantly degrade soybean protein isolate under high-temperature and high-salt conditions, so that the salt-tolerant protease has important application value for efficient catalysis of protein substrates in traditional high-salt fermentation industry. The application also realizes efficient secretion of the salt-tolerant protease by optimizing the concentration of enzyme cofactors. Furthermore, electrophoretically pure grade recombinant salt-tolerant protease is obtained through one-step separation and purification, and the purification process is simple and efficient.

The application belongs to the technical field of biocatalytic synthesis of steroid drugs, and particularly relates to a dehydrogenase, a gene, an engineering bacterium and application, the amino acid sequence of the dehydrogenase is SEQ ID NO. 1 or SEQ ID NO. 2, the dehydrogenase has high dehydrogenation activity, high stereoselectivity and strong regioselectivity, and no other conformation impurities are generated; the engineering bacterium can efficiently secrete the dehydrogenase, and effectively improves the conversion efficiency of a substrate, especially for a substrate 6-methy format (11beta, 17alpha-dihydroxy-6alpha-methylpregna-1, 4-diene-3, 20-diketone), which is low in cost and has significant industrialization potential; the dehydrogenase mutant has clear physicochemical properties, and the method of whole cell catalysis is used, so that the cumbersome step of enzyme purification is omitted, and the cost is reduced and the operation is simple.