Abstract: This disclosure relates to dimeric immunotherapeutics that comprise an IgG that is crosslinked with a disulfide bond. The IgG may include two heavy chains including a cysteine mutation that forms the disulfide bond. The dimeric immunotherapeutics are formed by increasing the concentration of the IgG such that spontaneous dimerization via the formation of disulfide bonds between the IgG molecules occurs over time.

Abstract: This disclosure describes proteins that specifically bind human sperm protein 17 (Sp17) with nanomolar affinity and high specificity. These proteins include a recombinant human anti-Sp17 IgG that is suitable for use as a therapeutic antibody to treat cancers that ectopically express Sp17. Other Sp17-binding proteins are described including antibody fragments, antibody conjugates, and fusion proteins.

Abstract: This disclosure describes proteins that specifically bind human sperm protein 17 (Sp17) with nanomolar affinity and high specificity. These proteins include a recombinant human anti-Sp17 IgG that is suitable for use as a therapeutic antibody to treat cancers that ectopically express Sp17. Other Sp17-binding proteins are described including antibody fragments, antibody conjugates, and fusion proteins.

Abstract: This disclosure relates to dimeric immunotherapeutics that comprise two IgGs that are crosslinked with a disulfide bond. The two IgGs may be chimeras of two different heavy chains, in which one heavy chain includes a cysteine mutation that forms the disulfide bond, and the other heavy chain lacks the cysteine mutation. The presence of a cysteine mutation in only one of the heavy chains of an IgG avoids two disulfide bonds between the two IgGs, which increases the accessible orientations between the two crosslinked IgGs, and also avoids the formation of trimers and higher-order oligomers.

Abstract: This disclosure relates to dimeric immunotherapeutics that comprise an IgG that is crosslinked with a disulfide bond. The IgG may include two heavy chains including a cysteine mutation that forms the disulfide bond. The dimeric immunotherapeutics are formed by increasing the concentration of the IgG such that spontaneous dimerization via the formation of disulfide bonds between the IgG molecules occurs over time.

Abstract: This disclosure relates to dimeric immunotherapeutics that comprise an IgG that is crosslinked with a disulfide bond. The IgG may include two heavy chains including a cysteine mutation that forms the disulfide bond. The dimeric immunotherapeutics are formed by increasing the concentration of the IgG such that spontaneous dimerization via the formation of disulfide bonds between the IgG molecules occurs over time.

Abstract: This disclosure describes methods and drug therapies for treating or preventing various health conditions, including cancer. The methods and therapies of the present disclosure comprise antibody-based therapies that functionally increase antibody binding to target antigens. Specifically, the antibody-based therapies increase the copy number of an antigen by utilizing at least a pair of differing antibodies directed at non-overlapping epitopes of the same antigen for effectively delivering payloads to a target cell. Each differing antibody may be conjugated to the same or a differing payload. The antibody-based therapy may use proteins that specifically bind human folate receptor alpha (FRalpha) with high affinity. These proteins include a human anti-FRalpha IgG1 that is suitable for use as a therapeutic antibody to treat conditions, such as cancers that express FRalpha. Other FRalpha-binding proteins are also described including antibody fragments, antibody conjugates, and fusion proteins.

Abstract: This disclosure relates to dimeric immunoconjugates for use in treating cancer generally and to dimeric immunoconjugates that bind human sperm protein 17 (Sp17) specifically. A dimeric immunoconjugate of this disclosure generally comprises a first monomeric antibody that carries a first payload and a second monomeric antibody that carries a second payload, wherein the first payload and the second payload are different. Such dimeric immunoconjugates advantageously allow the simultaneous delivery of two chemotherapeutics to a cancer cell, which allows for synergistic antineoplastic activity.

Abstract: This disclosure describes proteins that specifically bind human folate receptor alpha (FRalpha) with high affinity. These proteins include a recombinant human anti-FRalpha IgG1 that is suitable for use as a therapeutic antibody to treat cancers that express FRalpha. Other FRalpha-binding proteins are also described including antibody fragments, antibody conjugates, and fusion proteins.

Abstract: This disclosure describes proteins that specifically bind human folate receptor alpha (FRalpha) with high affinity. These proteins include a recombinant human anti-FRalpha IgG1 that is suitable for use as a therapeutic antibody to treat cancers that express FRalpha. Other FRalpha-binding proteins are also described including antibody fragments, antibody conjugates, and fusion proteins.

Abstract: This disclosure relates to dimeric immunotherapeutics that comprise two IgGs that are crosslinked with a disulfide bond. The two IgGs may be chimeras of two different heavy chains, in which one heavy chain includes a cysteine mutation that forms the disulfide bond, and the other heavy chain lacks the cysteine mutation. The presence of a cysteine mutation in only one of the heavy chains of an IgG avoids two disulfide bonds between the two IgGs, which increases the accessible orientations between the two crosslinked IgGs, and also avoids the formation of trimers and higher-order oligomers.

Abstract: This disclosure relates to homodimeric antibodies for use in treating cancer generally and to both homodimeric antibodies that bind human sperm protein 17 (Sp17) and homodimeric antibody immunoconjugates specifically. Such homodimeric antibodies display improved properties relative to monomeric antibodies, for example, because they can crosslink cells, improve cellular uptake, and/or carry greater payloads.

Abstract: This disclosure relates to dimeric immunotherapeutics that comprise two IgGs that are crosslinked with a disulfide bond. The two IgGs may be chimeras of two different heavy chains, in which one heavy chain includes a cysteine mutation that forms the disulfide bond, and the other heavy chain lacks the cysteine mutation. The presence of a cysteine mutation in only one of the heavy chains of an IgG avoids two disulfide bonds between the two IgGs, which increases the accessible orientations between the two crosslinked IgGs, and also avoids the formation of trimers and higher-order oligomers.

Abstract: This disclosure relates to dimeric immunotherapeutics that comprise two IgGs that are crosslinked with a disulfide bond. The two IgGs may be chimeras of two different heavy chains, in which one heavy chain includes a cysteine mutation that forms the disulfide bond, and the other heavy chain lacks the cysteine mutation. The presence of a cysteine mutation in only one of the heavy chains of an IgG avoids two disulfide bonds between the two IgGs, which increases the accessible orientations between the two crosslinked IgGs, and also avoids the formation of trimers and higher-order oligomers.

Abstract: This disclosure relates to dimeric immunotherapeutics that comprise an IgG that is crosslinked with a disulfide bond. The IgG may include two heavy chains including a cysteine mutation that forms the disulfide bond. The dimeric immunotherapeutics are formed by increasing the concentration of the IgG such that spontaneous dimerization via the formation of disulfide bonds between the IgG molecules occurs over time.

Abstract: This disclosure relates to dimeric immunotherapeutics that comprise two IgGs that are crosslinked with a disulfide bond. The two IgGs may be chimeras of two different heavy chains, in which one heavy chain includes a cysteine mutation that forms the disulfide bond, and the other heavy chain lacks the cysteine mutation. The presence of a cysteine mutation in only one of the heavy chains of an IgG avoids two disulfide bonds between the two IgGs, which increases the accessible orientations between the two crosslinked IgGs, and also avoids the formation of trimers and higher-order oligomers.

Abstract: This disclosure relates to dimeric immunotherapeutics that comprise an IgG that is crosslinked with a disulfide bond. The IgG may include two heavy chains including a cysteine mutation that forms the disulfide bond. The dimeric immunotherapeutics are formed by increasing the concentration of the IgG such that spontaneous dimerization via the formation of disulfide bonds between the IgG molecules occurs over time.

Abstract: This disclosure describes proteins that specifically bind human sperm protein 17 (Sp17) with nanomolar affinity and high specificity. These proteins include a recombinant human anti-Sp17 IgG that is suitable for use as a therapeutic antibody to treat cancers that ectopically express Sp17. Other Sp17-binding proteins are described including antibody fragments, antibody conjugates, and fusion proteins.

Abstract: This disclosure relates to homodimeric antibodies for use in treating cancer generally and to both homodimeric antibodies that bind human sperm protein 17 (Sp17) and homodimeric antibody immunoconjugates specifically. Such homodimeric antibodies display improved properties relative to monomeric antibodies, for example, because they can crosslink cells, improve cellular uptake, and/or carry greater payloads.

Abstract: This disclosure describes methods of using proteins that specifically bind human folate receptor alpha (FRalpha) with high affinity. These proteins include a recombinant human anti-FRalpha IgG1 that is suitable for use as a therapeutic antibody to treat cancers that express FRalpha. Other FRalpha-binding proteins are also described including antibody fragments, antibody conjugates, and fusion proteins.