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ActoFactor™ Recombinant Human Chemokine (C-C motif) ligand 26

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Cat.No.
CSC-CTK0441
Description
Eotaxin-3 is a CC chemokine that signals through the CCR3 receptor. It is produced by endothelial cells stimulated with IL-4 or IL-13. Eotaxin-3 selectively targets cells expressing CCR3, including eosinophils, basophils, T cells and monocytes. Eotaxin-3 has similar activity to Eotaxin and Eotaxin-2, but the three Eotaxins share only a low degree of sequence homology. Recombinant human Eotaxin-3 is an 8.4 kDa protein containing 71 amino acid residues, including the four highly conserved cysteine residues present in CC chemokines.
Species
Human
Product Overview
Human CCL26 expressed in E.coli
Molecular Mass
8.4 kDa
Size
CAT# CSC-CTK0441-20 (20 μg); CAT# CSC-CTK0441-100 (100 μg)
Expression System
E.coli
Purity
Greater than 98% as determined by SDS-PAGE and HPLC analysis.
Activity
Determined by its ability to chemoattract human CCR3/HEK 293 cells. The maximum activity was achieved at 2ug/ml.
Endotoxin Level
Less than 1 EU/μg.
Formulation
Lyophilized from a sterile-filtered solution with no additives.
Reconstitution
Please centrifuge product before opening vial. The lyophilized protein should be reconstituted with distilled, sterile water to a concentration of 0.1-1.0 mg/ml. For further dilution, carrier protein (0.1% BSA or HSA) should be added to avoid loss of bioactivity.
Storage & Stability
The lyophilized protein, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted protein should be used immediately or stored long-term in undiluted working aliquots at -20°C. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
Citation Guidance
If you use this products in your scientific publication, it should be cited in the publication as: Creative Bioarray cat no. If your paper has been published, please click here to submit the PubMed ID of your paper to get a coupon.

For research use only. Not for any other purpose.

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