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In stock & estimated to ship in 1-2 days by July 22, 2026

Description 

Recombinant human erythropoietin (EPO) is a glycosylated cytokine essential for erythropoiesis, specifically promoting the proliferation and differentiation of erythroid progenitor cells (CFU-E) into mature erythrocytes.

While renal production maintains physiological EPO levels in adults, hepatic synthesis predominates during fetal and neonatal development.

Beyond its canonical role in hematopoiesis, EPO exhibits pleiotropic bioactivities, including angiogenic stimulation via vascular smooth muscle cell proliferation, neuroprotective effects under hypoxic conditions, and modulation of B-cell function.

The recombinant protein retains native conformational integrity, ensuring targeted activation of the EPO receptor (EPOR) to orchestrate tissue-specific responses without off-target interactions, making it invaluable for therapeutic applications in anemia treatment and regenerative medicine.

Specifications

Specification Acceptance Criteria TL-636-0050 TL-636-0100
Appearance Freeze-dried preparation, the form should be white loose body Compliance Compliance
Identity The electrophoretic bands should be consistent with the molecular weight of the product Compliance Compliance
Visible Particle Should be no visible particle Compliance Compliance
Moisture ≤4.0% 2.0% 2.9%
pH 6.5~7.5 7.3 7.3
Purity >90% / SDS-PAGE Compliance Compliance
Endotoxin <0.1EU/μg <0.1EU/μg <0.1EU/μg
Mycoplasma Should be negative Negative Negative
Sterility No growth No growth No growth
Biological Activity Cell proliferation assay with TF-1 cells, specific activity ≥1×106 IU/mg 3.08×106 IU/mg

Features

  • Glycosylated, Mammalian-Derived EPO

    HEK293 expression preserves native glycosylation and EPOR-specific signaling fidelity.

  • Validated High Biological Activity

    Demonstrated potency in TF-1 cell proliferation assay (≥1.0 × 10⁶ IU/mg).

  • High Purity with Stringent QC

    90% purity by SDS-PAGE with confirmed sterility, mycoplasma negativity, and low endotoxin.

  • Consistent Lot-to-Lot Performance

    Controlled moisture, pH, and activity ensure reproducibility in hematopoietic research workflows.

Applications

Erythropoiesis Research

Promotes proliferation and differentiation of erythroid progenitors (CFU-E).

T Cell-Related Studies

Applied as a functional cytokine component in immune cell research systems.

CIK Cell Research

Used in cytokine-induced killer (CIK) cell culture and functional modulation studies.

Regenerative & Angiogenesis Research

Explored for non-hematopoietic roles including angiogenesis and tissue protection under hypoxia.

Stability & Storage

  • Lyophilized powder: Stable for 12 months at −80 °C or 6 months at −20 °C when stored in the original sealed container under desiccant.
  • Reconstitution: Dissolve in sterile Water for Injection, 0.9% NaCl, or PBS (pH 7.4), maintaining a final concentration ≥100 µg/mL to prevent adsorption.
  • Handling: Aliquot to avoid repeated freeze–thaw cycles.

Cautions

• Research Use Only: This product is not intended for diagnostic or therapeutic use.

• Handling: Prepare solutions using sterile technique. Avoid microbial contamination to maintain activity.

• Storage: Follow recommended storage conditions. Repeated freeze–thaw cycles may reduce performance.

Documents

FAQ

What is Recombinant Human EPO Protein?

Recombinant Human EPO Protein is a recombinant form of human erythropoietin (EPO), a glycosylated cytokine involved in erythropoiesis. It promotes the proliferation and differentiation of erythroid progenitor cells (CFU-E) into mature erythrocytes and is supplied for research applications involving EPO biology.

How is Recombinant Human EPO Protein produced?

This Recombinant Human EPO Protein is produced using a HEK293 mammalian expression system. The protein corresponds to the human EPO expressed region Ala28-Arg193 and contains a C-terminal 6×His tag.

What applications can Recombinant Human EPO Protein be used for?

Recombinant Human EPO Protein can be used for erythropoiesis research, erythroid progenitor cell differentiation studies, and EPO-related research applications. EPO has also been studied for additional biological activities including angiogenesis, hypoxia-related responses, and B-cell function.

How is the biological activity of Recombinant EPO Protein validated?

The biological activity of Recombinant Human EPO Protein is evaluated using a TF-1 cell proliferation assay. The product specification requires a specific activity of ≥1.0×10⁶ IU/mg.

What quality controls are performed for this Recombinant Human EPO Protein?

Quality testing includes appearance, identity, visible particle inspection, moisture analysis, pH testing, purity evaluation by SDS-PAGE, endotoxin testing, mycoplasma testing, sterility testing, and biological activity analysis.

The product specification includes purity greater than 90% by SDS-PAGE and endotoxin below 0.1 EU/μg.

What expression system is used for Recombinant Human EPO Protein?

Recombinant Human EPO Protein is produced using HEK293 cells as the mammalian expression system.

How should Recombinant Human EPO Protein be stored?

The lyophilized protein is stable for 12 months at −80°C or 6 months at −20°C when stored in the original sealed container under desiccant. Repeated freeze–thaw cycles should be avoided after reconstitution.

How should Recombinant Human EPO Protein be reconstituted?

The lyophilized protein can be dissolved in sterile Water for Injection, 0.9% NaCl, or PBS (pH 7.4). A final concentration of ≥100 µg/mL is recommended during reconstitution.

Is Recombinant Human EPO Protein for therapeutic or clinical use?

No. This product is supplied for Research Use Only (RUO). It is not intended for human, animal, diagnostic, or therapeutic applications.

When can I expect my order to ship?

Most orders are filled and shipped within 2-3 business days from the time they are received.

Our standard shipping usually take 2-5 days.

We also provide express shippping for time-sensitive deliveries. 

Email contact@biofargo.com if you have any requirements.

 

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