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Human serum albumin is the most abundant protein in human plasma. It can transport hormones, lipids and other molecules and maintain osmotic pressure.
OsrHSA is a recombinant human serum albumin derived from rice grains, which
provides an excellent solution for animal free medium. Compared to FBS, pHSA
and BSA, OsrHSA has higher purity and excellent batch consistency. Meanwhile,
OsrHSA is widely used as excipient, stabilizer and embedding agent in
bio-pharmaceutical applications.


  • It is lyophilized with saline (HYC002C01).
  • It is packaged in 50ml with 20% concentration (HYC001C01).


  • Purity: More than 99.99% as determined by SDS-PAGE and HPLC analysis.
  • Endotoxin: Less than 0.01EU/mg

Physical Appearance

  • Off-white to light beige lyophilized powder

Storage and Handling

Stored at temperatures 2-8º for 36 months . For lyophilized powder, it is recommended to reconstitute
the lyophilized OsrHSA in sterile PBS. Upon reconstitution, OsrHSA should be stored below -20º. Use as soon as possible after
opening. Please avoid freeze-thaw cycles.

Quality control tests

1. HPLC analysis

OsrHSA was analyzed by size exclusion chromatography
HPLC (SEC HPLC), showing the purity is more than 99.99%.

2. OsrHSA has equal safety in Vivo to pHSA

The titers of individual immunoglobulins IgG, IgM, IgE, and IgA showed no significant difference among the pHSA,
OsrHSA, and saline groups, and the titers of C4 complement were not significantly different.

3. Performance of OsrHSA in CIK cell therapy

OsrHSA was used in PBMC culture to induce the CIK cells. After 14 days, the total cell amount reach to 6.6X109, and the CD3+CD56+ rate is more than 22.97%. It showed that OsrHSA has effective action in promoting CIK cell growth.

Tested Applications

  • Cell & gene therapy development and optimizing cell therapy performance 

Cell therapies, including immune cell and stem cell-based therapies, are some of the most sophisticated therapeutics in development. Cell therapy offers an alternative approach to more widely used treatment options. However, the area faces challenges on several fronts, such as upscaling, logistics and ensuring consistent performance. Consequently, there is a need to optimize cell performance to achieve a viable cell product and safe therapeutic solution to patients.

  • Recombinant human albumin for stem cell culture, cryopreservation & formulation

Albumin is well known to facilitate growth of many cell types, such as mesenchymal stem cells (MSC’s), embryonic stem cells (ESC’s), induced pluripotent stem cells (iPSC’s) and immune cells.

Today, several of albumin’s biological properties have been proven valuable across the cell therapy value chain, including:

a)Transportation and complexation with metals or other molecular entities, creating an optimal micro-environment for sustained cell viability.

b)Acting as a rich nutrient source ensuring optimal conditions, particularly during cell proliferation.

c)Functioning as a pH buffer to prevent unwanted effects during differentiation.

d)Maintaining cell viability during cryopreservation – driven by the high purity of our recombinant albumin.

e)Acting as a scavenger of toxins and other reactive oxygen species, albumin protects cells against chemical stress all the way from culture to patient.

f)Providing an insulation effect in media due to its propensity to distribute evenly throughout solutions.

= Our recombinant human albumin products has been specifically developed to enhance these functional properties .

g)Vaccine stabilization

  • Maintaining vaccine stability

Vaccines continue to be an important field of pharmaceutical research, offering valuable therapeutic and prophylactic patient benefits.

Like other biologics, vaccines are susceptible to environmental stress, such as temperature changes and physical strain. Therefore, maintaining stability during manufacturing, storage and delivery of vaccines to patients can be a difficult task.

The ability to maintain stability in such conditions lead to reduction in cost and more effective vaccination programs to people worldwide. Even when freeze-drying is chosen as a formulation option, reduction of cell viability and vaccine efficacy can occur for temperature sensitive vaccines.

Overcoming vaccine challenges using albumin 

a)Protection from sheer stress: Recombinant human albumin provides an insulating effect on viral vector vaccines, protecting against physical damage during manufacturing and handling, ultimately maintaining potency and efficacy.

b)Prevention of surface adsorption: Loss of vaccine particles on surfaces during downstream processing can cause significant loss of yield. Furthermore, adsorption to final vaccine containers may result in inadequate dose control. By coating surfaces with our recombinant HSA, these issues may be prevented.

c)Thermal stability: Thermally sensitive vaccines can lose viability and efficacy during freeze-thaw and/or fluctuating temperatures under transportation. Driven by albumin’s high thermal stability, our recombinant HSA has shown to extend this quality to co-formulated vaccines.

These properties have been shown to be applicable across a broad range of vaccine constructs, such as live attenuated vaccines, whole-inactivated, sub-unit vaccines, viral vector vaccines, virus like particles (VLP’s) and enveloped vaccines.

  • Protein & peptide formulation

Given the instable nature of proteins and peptides, optimizing the stability of such therapeutics is a critical yet challenging objective of any drug development program. Resolution of such challenges enables their full therapeutic potential to be exploited, thereby ensuring optimal treatment options.

Formulation challenges

Safety and activity can be impaired by loss of “integrity” of the formulated product. Proteins and peptides indeed are only marginally stable and can undergo degradation via several mechanisms:

a)Hydrophobic interactions and peptide fibrillation may lead to aggregatesand sub-visible particles, resulting in reduced efficacy and increased immunogenicity.

b)Binding to surfacescan cause structural changes resulting in self-association and/or aggregation. Further to this, non-specific adsorption to drug containers may cause material loss and incorrect dosing.

c)Chemical stress, such as degradation by oxidative species, can result in a range of functional changes such as altered binding activities, increased susceptibility to aggregation and proteolysis, and increased or decreased uptake by cells, as well as altered immunogenicity.

Choosing the right formulation strategy

Companies often work within a standard toolbox of excipients for formulation development. Although many of these agents are effective stabilizers, their use requires careful consideration in terms of local toxicity and potential immunogenicity. Often the outcome is a cocktail of excipients. In some instances, it is quite difficult to combine the various “ingredients” to reach the levels of stabilization needed. As formulation becomes increasingly complicated to achieve, there is an equally increased need for advanced solutions.

Albumin is nature’s own stabilizer, with in vivo functions to transport and protect vital molecules. Our recombinant human albumin exploits albumin’s multifunctional properties as an effective, versatile stabilizer. It is particularly suited as a leaner formulation approach of biological drugs, such as proteins or peptides, not readily stabilized using traditional formulation strategies.

  • Medical device coating

Biocompatible medical device coating using recombinant human albumin

Innovation in medical devices continues to create novel treatment options. However, medical device developers are facing challenges in ensuring safe and biocompatible products. Biocompatibility is crucial when using medical devices to ensure they do not elicit an adverse response by the patient.

Due to its natural propensities, albumin is widely utilized in the medical device industry for coating of stents and tubing, for instance in dialysis, to improve their biocompatibility.

Albumin’s natural surface coating ability

Albumin has been demonstrated to cover both hydrophobic and hydrophilic surfaces in nearly a single molecule layer. This means that even small amounts of albumin can effectively cover large areas of surface.

By coating with albumin, a biological interface is created, thereby limiting the exposure of the otherwise incompatible surface to the patient, increasing product safety.

The improved purity and defined nature of our product consistently produces the same surface coverage. This makes our product especially suited to the medical devices industry as it minimizes the need for elaborate release procedures and product performance monitoring. Additionally, due to its recombinant nature, is free of risk with respect to human derived pathogens and viruses, further warranting a safe product.




Additional information


1g, 10g