Provided is an African swine fever virus chimeric protein. The chimeric protein comprises: (1) an African swine fever virus p72 domain I; (2) an African swine fever virus p72 domain II; (3) an African swine fever virus p72 domain III; and (4) an African swine fever virus antigenic protein. By using African swine fever virus p72 protein as a skeleton, the chimeric protein provided in the present invention will exhibit antigenic epitopes of African swine fever virus antigenic proteins p54, p30, CD2v, and p12, achieve a good immune effect, and can produce significant humoral and cell-mediated immune response.

The invention refers to an anti-oxMIF/anti-CD3 antibody comprising at least one binding site specifically recognizing oxMIF and one binding site specifically recognizing CD3, which is an IgG wherein a scFv is fused to only one of the two heavy IgG chains, an IgG wherein one Fab arm is replaced by a bispecific-T-cell-engager (BiTE), or an IgG wherein both Fab arms are replaced by scFvs with different binding specificities, and its use in the treatment of hyperproliferative diseases, specifically in the treatment of cancer.

Alpha-sheet polypeptide multimers, and polypeptides for making multimers, compositions and medical devices including them, and their use for treating and diagnosing amyloid diseases or amyloid-associated diseases are disclosed.

Described are peptides and peptide conjugates comprising CN binding motifs (CNBM) which inhibit the CN-NFAT interaction. In some embodiments, the peptides comprise: (i) CNBM; (ii) a hydrophobic, non-peptidic moiety (RH) which interacts with the hydrophobic pocket on a CN protein; (iii) a sequence -AAU1-AAU2-AAU3-AAU4-AAU5-AAU6-, wherein each of AAU2, AAU3, AAU4, AAU5, and AAU6, is, independently, optional, and each of AAU1, AAU2, AAU3, AAU4, AAU5, and AAU6 when present is independently an amino acid as defined herein; or (iv) combinations thereof. In some embodiments, RH is conjugated to the N- or C-terminus of the CNBM. In some embodiments, the sequence -AAU1-AAU2-AAU3-AAU4-AAU5-AAU6- is conjugated to the N- or C terminus of the CNBM. In some embodiments, the peptides comprise: CNBM and RH. In some embodiments. In some embodiments, the peptides comprise: CNBM and AAU1-AAU2-AAU3-AAU4-AAU5-AAU6-. In some embodiments, the peptides of the disclosure CNBM and RH.

Provided is an antibody, which is capable of specifically binding to a B-cell maturation antigen (BCMA). The provided BCMA antibody is capable of specifically binding to an extracellular fragment of the BCMA and has excellent affinity and specificity; and the antibody is a functional antibody and has the activity blocking binding of the BCMA with its ligand APRIL. Immune cells constructed based on the antibody has an excellent specific killing function for a BCMA-positive tumor cell.

A pharmaceutical composition is described, which comprises proteins and an immune checkpoint inhibitor, wherein the proteins comprise a fusion protein, and the fusion protein comprises cytokines IL12, IL2, and GMCSF. A reagent kit is also described, which comprises the pharmaceutical composition. The pharmaceutical composition or the reagent kit may be used in preparing a medicament for treating a tumor.

The preparation method of a starch-based double-loaded functional nanoparticle includes: performing restrictive hydrolysis treatment on egg high-density lipoprotein using proteases to obtain the polypeptide; performing self-assembling on a mixed system containing the polypeptide and quercetin under the alkaline condition to form a micelle nanoparticle; performing covalent grafting reaction on a mixed system containing the micelle nanoparticle and anthocyanin under the alkaline condition to form a graft; and electrostatically compounding carboxymethyl dextrin with the graft to obtain the starch-based double-loaded functional nanoparticle. In the preparation method, raw materials derived from natural sources are used, and the self-assembled colloid nanoparticle with good properties can be obtained by adjusting the pH without any organic reagents. The obtained product has a nanoparticle size, has high antioxidant activity and stability against environmental stress, and can be widely applied to the fields of delivery of nutrients, stabilization of biologically active substances and the like.

The preparation method of a starch-based double-loaded functional nanoparticle includes: performing restrictive hydrolysis treatment on egg high-density lipoprotein using proteases to obtain the polypeptide; performing self-assembling on a mixed system containing the polypeptide and quercetin under the alkaline condition to form a micelle nanoparticle; performing covalent grafting reaction on a mixed system containing the micelle nanoparticle and anthocyanin under the alkaline condition to form a graft; and electrostatically compounding carboxymethyl dextrin with the graft to obtain the starch-based double-loaded functional nanoparticle. In the preparation method, raw materials derived from natural sources are used, and the self-assembled colloid nanoparticle with good properties can be obtained by adjusting the pH without any organic reagents. The obtained product has a nanoparticle size, has high antioxidant activity and stability against environmental stress, and can be widely applied to the fields of delivery of nutrients, stabilization of biologically active substances and the like.

The present disclosure relates to a fusion protein of Z-domain and calsequestrin having improved reactivity, stability, and antibody recovery, and a method of isolating and purifying antibodies using the same. Specifically, the present disclosure relates to: a nucleic acid encoding a fusion protein of Z-domain and calsequestrin having improved reactivity, stability, and antibody recovery; a recombinant expression vector including the nucleic acid; a host cell transformed with the recombinant expression vector; and a method of isolating and purifying antibodies by using the fusion protein of Z-domain and calsequestrin having improved reactivity, stability, antibody recovery, and purity.

The present disclosure relates to a fusion protein of Z-domain and calsequestrin having improved reactivity, stability, and antibody recovery, and a method of isolating and purifying antibodies using the same. Specifically, the present disclosure relates to: a nucleic acid encoding a fusion protein of Z-domain and calsequestrin having improved reactivity, stability, and antibody recovery; a recombinant expression vector including the nucleic acid; a host cell transformed with the recombinant expression vector; and a method of isolating and purifying antibodies by using the fusion protein of Z-domain and calsequestrin having improved reactivity, stability, antibody recovery, and purity.