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Cat. No.: RHSAY-1 (for 1g)

Cat. No.: RHSAY-5 (for 5g)

Cat. No.: RHSAY-20 (for 20g)

Description

Human Serum Albumin (HSA) is a protein composed of 585 amino acids, with a molecular weight of approximately 66.5 kDa. Its secondary structure is predominantly α-helical, and it carries a net negative charge on its surface. HSA exhibits high conformational flexibility, enabling it to bind a diverse range of molecules.

Structurally, the protein comprises three homologous domains (I, II, and III), each capable of binding different classes of ligands. HSA demonstrates excellent binding affinity for water, calcium (Ca²⁺), sodium (Na⁺), potassium (K⁺), fatty acids, hormones, bilirubin, and various pharmaceutical compounds.

Its primary biological role is to regulate colloidal osmotic pressure in the bloodstream. As the major zinc-binding protein in plasma, HSA typically carries around 80% of circulating zinc.

Key physiological functions of HSA include:

1. Maintaining osmotic pressure: By retaining water within blood vessels, HSA prevents fluid leakage, playing a critical role in treating edema.

2. Transport of substances: It binds and transports hydrophobic molecules (e.g., bilirubin, fatty acids), hormones (e.g., thyroxine), and drugs (e.g., antibiotics, anticancer agents), thereby influencing drug distribution and metabolism.

3. Antioxidant properties: Its free thiol (-SH) group scavenges reactive oxygen species, protecting cells from oxidative damage.

4. Modulation of inflammation: By binding pro-inflammatory molecules such as endotoxins, HSA helps mitigate systemic inflammatory responses.

Our company’s recombinant HSA (rHSA) is expressed in yeast and purified through multiple steps. The recombinant protein includes a His tag for purification, and its amino acid sequence matches the native full-length version, with only the signal peptide and propeptide removed. The molecular weight remains approximately 66.5 kDa, and its biological functions are equivalent to those of plasma-derived HSA.

Compared to native HSA, rHSA avoids the risk of blood-borne pathogen transmission. However, potential differences in glycosylation patterns should be noted, and its immunogenicity requires long-term observation—some studies suggest it may trigger mild allergic responses in rare cases.

Concentration

5 mg/mL

Key Features

• Recombinantly expressed; non-human origin to eliminate the risk of blood-borne disease transmission
• Glycosylation pattern highly similar to plasma-derived HSA
• Optional lyophilized formulation available

Applications

• Widely used as a component in pharmaceutical formulations and medical devices due to its high purity and uniformity
• Applied in tissue engineering and regenerative medicine for its excellent biocompatibility and low immunogenicity
• Serves as a primary reference calibrator for urinary albumin in diagnostic testing

Quality Control

• Purity: >95% as determined by SDS-PAGE under reducing conditions
• Host Nucleic Acid Residue: Low residual levels confirmed via PCR (Ct value >38)

Precautions

Glycosylation pattern may differ slightly from plasma-derived HSA

Storage

• Lyophilized at –20°C to –70°C: stable for 12 months
• Reconstituted under sterile conditions: stable at –70°C for up to 3 months
• Avoid repeated freeze–thaw cycles to preserve protein activity

Related:

• Recombinant Human Serum Albumin from Rice (rHSA from Rice, ≥90%)
• Recombinant Human Serum Albumin from Rice (rHSA from Rice, ≥99%)
• Recombinant Human Serum Albumin from Rice (rHSA from Rice, ≥99%, Ultralow-Endotoxin & Enzyme-Free)
• Recombinant Human Serum Albumin from Yeast (rHSA from Yeast, ≥95%)