RP1008S Recombinant Human Holo-Transferrin (CHO)

Background

Recombinant human transferrin (rhTransferrin) is a single-chain glycoprotein composed of 679 amino acids with a molecular weight of approximately 75–80 kDa, containing two N-glycosylation sites and two Fe³⁺-binding sites, belonging to the iron-binding protein family. Native transferrin is primarily synthesized and secreted by hepatocytes and is present at high concentrations in serum. It mediates iron uptake and transport by binding to the transferrin receptor (TfR1/CD71) and entering cells via receptor-mediated endocytosis. In serum-free media, rhTransferrin can replace animal-derived transferrin to support cell growth, being particularly suitable for hybridoma, CHO cell, and stem cell culture, while also reducing iron toxicity by preventing oxidative stress caused by free iron. Furthermore, rhTransferrin can serve as a drug delivery vehicle, such as transferrin-drug conjugates, targeting tumor cells with high TfR expression, offering potential clinical applications. This product is expressed in CHO cells, featuring high purity, high activity, and freedom from animal-derived contamination.

Product Advantages

• CHO cell expression

• Holo-form, fully iron-saturated, ready to use without additional iron supplementation

• Formulation-free, clean ingredient profile

• Animal-free production system

• Excellent batch-to-batch consistency

• 60-month shelf life

• Suitable for CGT and biopharmaceutical process development

• Supports research and industrial-scale production

Product Specifications

Figure 1： Recombinant Human Transferrin purity test results, left: SDS-PAGE (sample R, reduced ; sample NR, non-reduced); right: SEC-HPLC

Figure 2：Recombinant Human Transferrin biological activity test results, ED50 is 0.3 μg/mL

Directions for Use

Reconstitute with sterile PBS, WFI, or other suitable buffer at room temperature. Recommended stock concentration: 0.5–2.0 mg/mL. After complete dissolution, filter-sterilize using a 0.22 μm sterile membrane filter. Filtered stock solution can be stored under aseptic conditions at 2–8°C for up to 30 days. Dilute further before adding to culture medium as needed.

Transport & Storage

Ice pack transport.

Store at 2–8°C, protected from light, sealed, and moisture-proof. Avoid repeated opening and prolonged exposure to air. Shelf life: 60 months under recommended storage conditions.

Applications

RP1008S Recombinant Human Holo-Transferrin serves as an important iron transport component in serum-free, low-serum, and chemically defined (CD) media, widely applicable to mammalian cell culture and biopharmaceutical process development.

Applicable cell types include but are not limited to:

• Mesenchymal stem cells (MSC)

• Induced pluripotent stem cells (iPSC)

• Embryonic stem cells (ESC)

• NK cells, T cells, and other immune cells

• CHO cells, HEK293 cells, and other engineered cells

• Other mammalian cell culture systems

Produced using a CHO cell expression platform, it contains no animal-derived components or added formulations, meeting the requirements of serum-free and chemically defined media for raw material safety, consistency, and traceability.

Precautions

• This product is intended for research, process development, and biomanufacturing use only. Not for diagnostic, therapeutic, or clinical use in humans or animals.

• Use the product as soon as possible after opening. Unused portions should be promptly sealed and stored under recommended conditions.

• Handle reconstituted solutions under aseptic conditions to avoid microbial contamination.

• Optimal transferrin concentration may vary across different cell types and culture systems. Determine optimal usage conditions through preliminary experiments.

• Read the product technical datasheet carefully before use and follow relevant experimental protocols.

Reference

1.De Jong G, Van Dijk J P, Van Eijk H G. The biology of transferrin[J]. Clinica chimica acta, 1990, 190(1-2): 1-46.

2.Ponka P, Beaumont C, Richardson D R. Function and regulation of transferrin and ferritin[C]. Seminars in hematology. 1998, 35(1): 35-54.

3.Ogun A S, Adeyinka A. Biochemistry, transferrin[J]. 2018.