EPO a Fc Human

Erythropoietin-Alpha Fc-Chimera Human Recombinant
Cat. No.
BT4933
Source
Chinese Hamster Ovary Cells(CHO).
Synonyms
EPO-a, EPO-alpha, Epoetin, EP, MGC138142.
Appearance
Sterile Filtered White lyophilized (freeze-dried) powder.
Purity
Greater than 98.0% as determined by:
(a) Analysis by RP-HPLC.
(b) Analysis by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Erythropoietin-alpha Fc-Chimera Human Recombinant is produced in Chinese hamster ovary (CHO) cells by recombinant DNA technology is a dimeric, glycosilated, polypeptide chain consisting of two mature human EPO molecules linked to the Fc portion of human IgG1. The Fc component contains the CH2 domain, the CH3 domain and hinge region, but not the CH1 domain of IgG1. As a result of glycosylation, the recombinant protein migrates with an apparent molecular mass of 140 kDa in non-reducing SDS-PAGE.

Product Specs

Introduction
As a member of the EPO/TPO family, this gene encodes a secreted, glycosylated cytokine composed of four alpha helical bundles. This protein is present in the plasma and plays a crucial role in regulating red blood cell production. It achieves this by promoting erythroid differentiation and initiating hemoglobin synthesis. Additionally, this protein exhibits neuroprotective properties against various potential brain injuries and demonstrates antiapoptotic functions in several tissue types.
Description
Erythropoietin-alpha Fc-Chimera Human Recombinant, produced in Chinese hamster ovary (CHO) cells using recombinant DNA technology, is a dimeric, glycosylated polypeptide chain. It consists of two mature human EPO molecules linked to the Fc portion of human IgG1. The Fc component includes the CH2 domain, the CH3 domain, and the hinge region, but excludes the CH1 domain of IgG1. Due to glycosylation, the recombinant protein exhibits an apparent molecular mass of 140 kDa in non-reducing SDS-PAGE.
Physical Appearance
Sterile Filtered White lyophilized powder.
Formulation
The lyophilized powder is formulated with 1x PBS pH-7.4 at a concentration of 1 mg per mg of powder.
Solubility
To reconstitute the lyophilized Erythropoietin, it is recommended to dissolve it in sterile 18MΩ-cm H2O at a concentration of not less than 100 µg/ml. This solution can then be further diluted in other aqueous solutions as needed.
Stability
Lyophilized Erythropoietin-a, although stable at room temperature for 3 weeks, should be stored in a dry environment below -18°C. Once reconstituted, EPO-alpha should be stored at 4°C for short-term use (2-7 days) and below -18°C for future use. To ensure long-term stability, adding a carrier protein (0.1% HSA or BSA) is recommended. Avoid repeated freeze-thaw cycles.
Purity
The purity is determined using two methods and exceeds 98.0%: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.
Biological Activity
The ED50, determined by the dose-dependent stimulation of human megakaryoblastic leukemia cells, is less than 2.0 ng/ml. This corresponds to a Specific Activity of 5.0 x 105 IU/mg.
Synonyms
EPO-a, EPO-alpha, Epoetin, EP, MGC138142.
Source
Chinese Hamster Ovary Cells(CHO).

Product Science Overview

Structure and Function

Erythropoietin-Alpha Fc-Chimera (Human Recombinant), often abbreviated as EPO-α/Fc, is a recombinant form of EPO that has been engineered to include the Fc region of human IgG1. This fusion enhances the stability and half-life of the protein in the bloodstream . The Fc component contains the CH2 domain, the CH3 domain, and the hinge region, which contribute to the extended half-life by interacting with the neonatal Fc receptor (FcRn) and protecting the protein from lysosomal degradation .

The recombinant EPO-α/Fc is produced in Chinese hamster ovary (CHO) cells, which are commonly used in biotechnology for the production of therapeutic proteins due to their ability to perform complex post-translational modifications, including glycosylation . Glycosylation is essential for the biological activity and stability of EPO, as it affects the protein’s solubility, resistance to proteolysis, and receptor binding affinity .

Therapeutic Applications

Recombinant human EPO and its analogs, including EPO-α/Fc, are widely used as erythropoiesis-stimulating agents (ESAs) in the treatment of anemia associated with chronic kidney disease (CKD), cancer, and other conditions . By stimulating erythropoiesis, these agents help to increase red blood cell counts and improve oxygen delivery to tissues, thereby alleviating the symptoms of anemia .

In addition to its role in erythropoiesis, EPO has been found to have neuroprotective and anti-apoptotic effects in various tissues . These properties have sparked interest in the potential use of EPO and its derivatives in the treatment of neurological disorders and other conditions involving cell death and tissue damage .

Production and Purification

The production of recombinant EPO-α/Fc involves the transfection of CHO cells with the human EPO gene or cDNA linked to an expression vector . The transfected cells are then cultured, and the recombinant protein is secreted into the culture medium. The protein is subsequently purified using techniques such as affinity chromatography, which exploits the Fc region’s affinity for protein A or protein G, commonly used ligands in purification processes .

The purified EPO-α/Fc is typically lyophilized (freeze-dried) for stability and ease of storage. It is recommended to reconstitute the lyophilized protein in sterile water and store it at low temperatures to maintain its stability and biological activity .

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2024 Thebiotek. All Rights Reserved.