Abstract: Disclosed is a method for efficiently separating and purifying recombinant human coagulate factor VIII Fc fusion protein. The method comprises steps of affinity chromatography and anion exchange chromatography; and the sample captured by means of the affinity chromatography is eluted with a salt ion buffer containing 5%-20% polyol organic solvents under the condition of pH 4.0 to 8.0, and the protein sample can be separated and purified to 85% or more by further ProteinA affinity chromatography. The purification method is simple to operate, naturally connects each step of chromatography, has a high recovery rate and low cost, and easily increases production.

Abstract: Provided is a tetravalent homodimeric bispecific antibody molecule simultaneously targeting an immune effector cell antigen CD3 and a tumor-associated antigen, wherein the bispecific antibody molecule contains, in order from N-terminus to C-terminus, a first single chain Fv, a second single chain Fv and a Fc fragment; wherein the first single chain Fv can specifically bind to the tumor-associated antigen, the second single chain Fv can specifically bind to CD3, and the first and the second single chain Fvs are connected by a linker peptide, while the second single chain Fv and the Fc fragment are directly connected or connected by a linker peptide; and the Fc fragment does not have effector functions such as CDC, ADCC and ADCP.