Abstract: A driving substrate, a light-emitting apparatus and a manufacturing method thereof, a splicing display apparatus, the driving substrate includes: a device disposing area, a bending area and a bonding area, the bending area is located between the device disposing area and the bonding area; the driving substrates located in the device disposing area, the bending area, and the bonding area include a buffer layer, a first conductive layer and a flexible dielectric layer that are stacked in sequence; the driving substrates located in the device disposing area and the bonding area further include a base plate disposed at a side of the buffer layer away from the first conductive layer, and a second conductive layer disposed at a side of the flexible dielectric layer away from the first conductive layer; and the driving substrate located in the bending area is configured to be able to bend along a bending axis.

Abstract: Affinity peptide ligands of mouse polyomavirus capsomers and a designed screening method thereof. The affinity peptide ligands can be used for separation and purification of the capsomers.

Abstract: Affinity peptide ligands of mouse polyomavirus capsomers and a designed screening method thereof. The affinity peptide ligands can be used for separation and purification of the capsomers.

Abstract: A method for protein refolding with an ion exchange resin. The method includes (a) choosing an ion exchange resin that having charged groups with the same sign as a net charge of a denatured protein to be refolded; (b) removing heterogeneous ions from the ion exchange resin by washing the ion exchange resin sequentially with saline solution and deionized water, to prepare the ion exchange resin; (c) mixing the ion exchange resin with a refolding buffer thoroughly, then adding the denatured protein to the refolding buffer and allowing the denatured protein to refold; and then (d) collecting the supernatant by centrifugation or settlement, to obtain a solution containing the refolded protein.

Abstract: A method for protein refolding using a like-charged ion exchange resins as an additive to facilitate protein refolding. The ion exchange resins mentioned herein includes charged group with the same sign as the target protein to be refolded and the method for refolding an unfolded protein. The method has some advantages described as below: firstly, no new impurity is introduced into the final product of protein due to ion exchange resins used in the present invention is insoluble and easy to remove by settlement or centrifugation, secondly; the key material used in the present invention, ion exchange resins, is easy to recycle after regeneration; thirdly, compared with the refolding method by chromatographic techniques, the current method requires no expensive chromatograph facilities and is simple to perform at lower cost, which is a desirable character for preparative refolding of therapeutic proteins expressed in bacteria as inclusion bodies.

Abstract: The present invention relates to the method for production, isolation, purification and the uses of recombinant herpes simplex virus vectors loaded with five sero-type adeno-associated virus AAV1, 3, 4, 5 and 6 respectively. The above five sero-type recombinant herpes simplex viruses are HSV-r2c1, HSR-r2c3, HSV-r2c4, HSV-r2c6 respectively. The 1, 3, 4, 5 and 6 sero-type recombinant adeno-associated viruses vectors could be produced by infecting the cells with the recombinant herpes simplex virus vectors.