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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.

Product List

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Product Features

Sequence Integrity: Protein sequence is complete with the signal peptide and pre-peptide removed.

High Purity: Protein purity is verified to be greater than 95% by SDS-PAGE.

Various Species Available: Human, Mouse, Cynomolgus and Rabbit species.

Bioactivity Validated: FcRn binding activity is validated with protocols available to download.

Verification Data

High purity and structural homogeneity verified by SDS-PAGE and SEC-MALS
High purity and structural homogeneity verified by SDS-PAGE and SEC-MALS

Human Serum Albumin, His Tag (Cat. No. HSA-H5220) on SDS-PAGE under reducing (R) condition. The purity of the protein is greater than 95%. As verified by SEC-MALS, the purity is more than 90% and the molecular weight of this protein is around 60-75 kDa.

High purity and structural homogeneity verified by SDS-PAGE and SEC-MALS

Human Serum Albumin, His Tag (Cat. No. HSA-H522a) on SDS-PAGE under reducing (R) condition. The purity of the protein is greater than 95%. As verified by SEC-MALS, the purity is more than 90% and the molecular weight of this protein is around 60-75 kDa.

High biological activity verified by SPR & BLI

High biological activity verified by SPR & BLI

Human Serum Albumin Protein, His Tag (Cat. No. HSA-H5220) immobilized on CM4 Chip can bind Human FCGRT&B2M Heterodimer Protein, His Tag (Cat. No. FCN-H52W7) with an affinity constant of 0.381 μM as determined in a SPR assay (Biacore T200) (Routinely tested).

High biological activity verified by SPR & BLI

Mouse Serum Albumin, His Tag (Cat. No. MSA-M52H8) immobilized on CM5 Chip can bind Mouse FCGRT&B2M Heterodimer Protein, His Tag (Cat. No. FCM-M52W8) with an affinity constant of 0.165 μM as determined in a SPR assay (Biacore T200) (Routinely tested).

High biological activity verified by SPR & BLI

Loaded Biotinylated Human FCGRT&B2M Heterodimer Protein, His,Avitag (Cat. No. FCM-H82W7) on SA Biosensor, can bind Human Serum Albumin, His Tag (Cat. No. HSA-H5220) with an affinity constant of 0.647 μM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).

High biological activity verified by SPR & BLI

Loaded Biotinylated Human Serum Albumin, His,Avitag (Cat. No. HSA-H82E3) on SA Biosensor, can bind Human FCGRT&B2M Heterodimer Protein, His Tag&Strep II Tag (Cat. No. FCM-H5286) with an affinity constant of 0.641 μM as determined in BLI assay (ForteBio Octet Red96e) (Routinely tested).

FAQ

Q

How can recombinant serum albumin be used in half-life extension studies?

Serum albumin interacts with the neonatal Fc receptor (FcRn) in acidic endosomes and undergoes FcRn-mediated recycling, which contributes to its long circulating half-life. This mechanism can be leveraged in drug development by fusing or conjugating therapeutics to human serum albumin (HSA), or by designing HSA-binding therapeutics, to extend half-life and improve pharmacokinetic properties.
Q

How do I choose the appropriate recombinant serum albumin product for my study?

Product selection depends on your experimental model, assay format, and detection method. Consider the species, tag, and labeling format required for your study. ACROBiosystems offers serum albumin proteins from multiple species in unlabeled, biotinylated, HRP-conjugated, and fluorescently labeled formats to support different experimental needs.
Q

Which serum albumin format should I choose for my assay?

Choose the format based on your assay design and detection method. Unlabeled proteins offer flexibility for general binding studies, while biotinylated proteins are suitable for streptavidin-based capture or detection systems. HRP-conjugated and Alexa Fluor™ 647-labeled HSA provide additional options for enzyme- or fluorescence-based detection.
Q

Can ACROBiosystems' recombinant serum albumin proteins be used for FcRn-binding studies?

Yes. Selected recombinant serum albumin proteins have been validated for FcRn binding using SPR and/or BLI. For example, Human Serum Albumin Protein, His Tag (Cat. No. HSA-H5220) binds Human FCGRT&B2M Heterodimer Protein with an affinity constant of 0.381 μM, as determined by SPR.
Q

Why is FcRn-binding activity important for serum albumin-based half-life extension?

FcRn-mediated recycling helps protect serum albumin from intracellular degradation and contributes to its long circulating half-life. Therefore, FcRn-binding activity is an important functional consideration when evaluating serum albumin for FcRn-mediated half-life extension strategies.
Q

How do I choose the appropriate species of serum albumin for my study?

Species selection should be based on the biological system and experimental model used in your study. ACROBiosystems offers recombinant serum albumin from multiple species, including human, mouse, cynomolgus monkey, rat, rabbit, and domestic pig, providing options for different experimental models and cross-species studies.
Q

Why might the experimentally observed molecular weight of serum albumin differ from the expected value?

Experimentally observed molecular weight can vary depending on the analytical method and protein characteristics. For example, Human Serum Albumin Protein, His Tag (Cat. No. HSA-H5220) shows an experimentally determined molecular weight of approximately 60–75 kDa by SEC-MALS. For accurate interpretation, refer to the characterization data provided for the specific product and analytical method.
Q

Should FcRn assay pH be controlled?

Yes. Albumin–FcRn binding is pH dependent, so maintain defined assay conditions when comparing binding results.
  • Introduction
  • Product List
  • Product Features
  • Verification Data
  • FAQ