Recombinant Serum Albumin

Serum albumin (SA) is one of the most abundant and stable proteins in blood. As such, fusion proteins for biopharmaceutics have mostly focused on developing albumin-based constructs due to its high stability, easy construction, and stable formulation. Albumin fusion proteins result in a function protein that prolongs the half-life of drugs through the recycling mechanism mediated by neonatal Fc receptor (FcRn). FcRn is responsible for the transport of albumin across endothelial barriers, such as the blood-brain barrier and the placenta and is also involved in the uptake and recycling of IgG antibodies. The interaction between FcRn and albumin occurs primarily in the acidic environment of the endosome, where the low pH triggers a conformational change in FcRn that allows it to bind to albumin and IgG. Many drugs take advantage of the protection mechanism of FcRn against IgG and human SA (HSA) by fusing/coupling with IgG Fc or HSA to extend their half-life and improve pharmacokinetics. In addition to using HSA as a fusion partner, many pharmaceutical companies are targeting HSA using bispecific or multiple antibodies to bind to HSA and prolong the half-life of drugs.

To facilitate the development of HSA antibody drugs and HSA fusion protein drugs, ACROBiosystems is offering a series of recombinant Serum Albumin products that have been validated in binding to FcRn proteins and can be used as antibody drug targets and fusion protein drug isotype controls.

Serum albumin (SA) is one of the most abundant and stable proteins in blood. As such, fusion proteins for biopharmaceutics have mostly focused on developing albumin-based constructs due to its high stability, easy construction, and stable formulation. Albumin fusion proteins result in a function protein that prolongs the half-life of drugs through the recycling mechanism mediated by neonatal Fc receptor (FcRn). FcRn is responsible for the transport of albumin across endothelial barriers, such as the blood-brain barrier and the placenta and is also involved in the uptake and recycling of IgG antibodies. The interaction between FcRn and albumin occurs primarily in the acidic environment of the endosome, where the low pH triggers a conformational change in FcRn that allows it to bind to albumin and IgG. Many drugs take advantage of the protection mechanism of FcRn against IgG and human SA (HSA) by fusing/coupling with IgG Fc or HSA to extend their half-life and improve pharmacokinetics. In addition to using HSA as a fusion partner, many pharmaceutical companies are targeting HSA using bispecific or multiple antibodies to bind to HSA and prolong the half-life of drugs.

To facilitate the development of HSA antibody drugs and HSA fusion protein drugs, ACROBiosystems is offering a series of recombinant Serum Albumin products that have been validated in binding to FcRn proteins and can be used as antibody drug targets and fusion protein drug isotype controls.

Serum albumin (SA) is one of the most abundant and stable proteins in blood. As such, fusion proteins for biopharmaceutics have mostly focused on developing albumin-based constructs due to its high stability, easy construction, and stable formulation. Albumin fusion proteins result in a function protein that prolongs the half-life of drugs through the recycling mechanism mediated by neonatal Fc receptor (FcRn). FcRn is responsible for the transport of albumin across endothelial barriers, such as the blood-brain barrier and the placenta and is also involved in the uptake and recycling of IgG antibodies. The interaction between FcRn and albumin occurs primarily in the acidic environment of the endosome, where the low pH triggers a conformational change in FcRn that allows it to bind to albumin and IgG. Many drugs take advantage of the protection mechanism of FcRn against IgG and human SA (HSA) by fusing/coupling with IgG Fc or HSA to extend their half-life and improve pharmacokinetics. In addition to using HSA as a fusion partner, many pharmaceutical companies are targeting HSA using bispecific or multiple antibodies to bind to HSA and prolong the half-life of drugs.

To facilitate the development of HSA antibody drugs and HSA fusion protein drugs, ACROBiosystems is offering a series of recombinant Serum Albumin products that have been validated in binding to FcRn proteins and can be used as antibody drug targets and fusion protein drug isotype controls.

Serum albumin (SA) is one of the most abundant and stable proteins in blood. As such, fusion proteins for biopharmaceutics have mostly focused on developing albumin-based constructs due to its high stability, easy construction, and stable formulation. Albumin fusion proteins result in a function protein that prolongs the half-life of drugs through the recycling mechanism mediated by neonatal Fc receptor (FcRn). FcRn is responsible for the transport of albumin across endothelial barriers, such as the blood-brain barrier and the placenta and is also involved in the uptake and recycling of IgG antibodies. The interaction between FcRn and albumin occurs primarily in the acidic environment of the endosome, where the low pH triggers a conformational change in FcRn that allows it to bind to albumin and IgG. Many drugs take advantage of the protection mechanism of FcRn against IgG and human SA (HSA) by fusing/coupling with IgG Fc or HSA to extend their half-life and improve pharmacokinetics. In addition to using HSA as a fusion partner, many pharmaceutical companies are targeting HSA using bispecific or multiple antibodies to bind to HSA and prolong the half-life of drugs.

To facilitate the development of HSA antibody drugs and HSA fusion protein drugs, ACROBiosystems is offering a series of recombinant Serum Albumin products that have been validated in binding to FcRn proteins and can be used as antibody drug targets and fusion protein drug isotype controls.

Serum albumin (SA) is one of the most abundant and stable proteins in blood. As such, fusion proteins for biopharmaceutics have mostly focused on developing albumin-based constructs due to its high stability, easy construction, and stable formulation. Albumin fusion proteins result in a function protein that prolongs the half-life of drugs through the recycling mechanism mediated by neonatal Fc receptor (FcRn). FcRn is responsible for the transport of albumin across endothelial barriers, such as the blood-brain barrier and the placenta and is also involved in the uptake and recycling of IgG antibodies. The interaction between FcRn and albumin occurs primarily in the acidic environment of the endosome, where the low pH triggers a conformational change in FcRn that allows it to bind to albumin and IgG. Many drugs take advantage of the protection mechanism of FcRn against IgG and human SA (HSA) by fusing/coupling with IgG Fc or HSA to extend their half-life and improve pharmacokinetics. In addition to using HSA as a fusion partner, many pharmaceutical companies are targeting HSA using bispecific or multiple antibodies to bind to HSA and prolong the half-life of drugs.

To facilitate the development of HSA antibody drugs and HSA fusion protein drugs, ACROBiosystems is offering a series of recombinant Serum Albumin products that have been validated in binding to FcRn proteins and can be used as antibody drug targets and fusion protein drug isotype controls.