Eotaxin 3 Human
Sterile Filtered White lyophilized (freeze-dried) powder.
Greater than 97.0% as determined by:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
Description
Eotaxin-3 Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 71 amino acids and having a molecular mass of 8.4kDa.
The Eotaxin-3 is purified by proprietary chromatographic techniques.
Product Specs
Recombinant Human Eotaxin-3, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 71 amino acids. It has a molecular weight of 8.4 kDa. The purification of Eotaxin-3 is achieved using proprietary chromatographic techniques.
Sterile Filtered White lyophilized (freeze-dried) powder.
Lyophilized from a 0.2 μm filtered concentrated solution in phosphate-buffered saline (PBS) at pH 7.4.
To reconstitute the lyophilized Eotaxin-3, it is recommended to dissolve it in sterile 18 MΩ-cm H2O at a concentration of at least 100 µg/ml. This solution can then be further diluted in other aqueous solutions as needed.
Lyophilized Eotaxin-3, while stable at room temperature for up to 3 weeks, should be stored desiccated at a temperature below -18°C. Upon reconstitution, CCL26 should be stored at 4°C for 2-7 days. For long-term storage, it is recommended to store it at a temperature below -18°C. To ensure optimal stability during long-term storage, the addition of a carrier protein (0.1% HSA or BSA) is recommended. It is important to avoid repeated freeze-thaw cycles.
The purity of Eotaxin-3 is determined using the following methods: (a) Analysis by RP-HPLC and (b) Analysis by SDS-PAGE. The purity is greater than 97.0%.
The biological activity of Eotaxin-3 is assessed based on its ability to chemoattract BaF3 mouse pro-B cells transfected with mouse CCR3. The ED50 for this effect typically falls within the range of 0.1-1.0 μg/ml.
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Product Science Overview
Eotaxin-3, also known as CCL26 or SCYA26, is a member of the CC chemokine family. Chemokines are small cytokines that play a crucial role in immune responses by directing the migration of immune cells to sites of inflammation or injury. Eotaxin-3 is particularly known for its role in attracting eosinophils, a type of white blood cell involved in allergic reactions and asthma.
Eotaxin-3 is constitutively expressed in various tissues, including the heart and ovary . It is also expressed in endothelial cells, which line blood vessels, and can be upregulated by cytokines such as interleukin-4 (IL-4) and interleukin-13 (IL-13) . Eotaxin-3 binds to the CC chemokine receptor 3 (CCR3), which is highly expressed on eosinophils, basophils, and Th2 lymphocytes . This interaction induces chemotaxis, the directed movement of cells towards the chemokine source, and plays a significant role in allergic inflammation .
Recombinant Eotaxin-3 is typically produced in Escherichia coli (E. coli) using recombinant DNA technology . The protein is expressed as a single, non-glycosylated polypeptide chain and purified using high-performance liquid chromatography (HPLC) and other chromatographic techniques . The final product is lyophilized and can be reconstituted in sterile phosphate-buffered saline (PBS) for use in various applications .
The synthetic route for producing recombinant Eotaxin-3 involves cloning the gene encoding Eotaxin-3 into an expression vector, which is then introduced into E. coli cells . The bacteria are cultured, and the recombinant protein is expressed and accumulated within the cells. The cells are then lysed, and the protein is purified from the cell lysate using chromatographic methods .
The biological activity of recombinant Eotaxin-3 is measured by its ability to chemoattract cells expressing CCR3 . The effective dose (ED50) for this activity is typically in the range of 0.3-1.5 µg/mL . The protein is stable when stored at -20 to -70°C and should be reconstituted in sterile PBS containing at least 0.1% human or bovine serum albumin to maintain its stability .
Industrial production of recombinant Eotaxin-3 involves large-scale fermentation of E. coli cultures expressing the protein . The process includes several steps: fermentation, cell lysis, protein purification, and lyophilization. The purified protein is subjected to rigorous quality control tests, including SDS-PAGE to confirm purity and endotoxin testing to ensure safety .
