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Explore the potential of our Recombinant Human CCL8 protein, an essential research tool for immunology-focused investigations. This C-C motif chemokine 8, also known as CCL8, is produced in E. coli and encompasses the 24-99aa expression region of the full-length mature protein. The tag-free protein is supplied in lyophilized powder form, allowing for straightforward reconstitution with sterile water or buffer for a wide range of experimental applications.
Committed to quality and performance, our Recombinant Human CCL8 protein exhibits a purity of >96% as determined by SDS-PAGE and HPLC analysis. Furthermore, endotoxin levels are maintained below 1.0 EU/µg, as determined by the LAL method. The protein demonstrates full biological activity, as determined by a chemotaxis bioassay using human peripheral blood monocytes, with an effective concentration range of 10-100 ng/mL.
Significant research has been conducted to understand the function and relevance of CCL8 (C-C motif chemokine 8) in various biological processes and diseases. CCL8, a member of the CC chemokine family, was first characterized by Proost et al. (1996), who elucidated its role as a chemoattractant for monocytes, eosinophils, and basophils. The involvement of CCL8 in the recruitment of leukocytes during inflammation was further supported by Van Coillie et al. (1999), highlighting its role in immune responses. Menten et al. (2002) explored the relationship between CCL8 and HIV-1 infection, demonstrating that CCL8 serves as a potent inhibitor of the R5 strains of HIV-1, thereby suggesting its potential role in controlling HIV-1 infection. CCL8's association with cancer was demonstrated by Negus et al. (1995), who identified the overexpression of CCL8 in human melanoma cell lines, and it has since been implicated in various cancer types. Furthermore, a study by Bandapalli et al. (2014) revealed the involvement of CCL8 in colorectal cancer progression and its potential as a diagnostic and therapeutic target.
1. Proost P, et al. Human and bovine granulocytes express a natural IL-8 inhibitor: characterization of the cDNA coding for the human homolog. Eur J Immunol. 1996;26(10): 2388-93.
2. Van Coillie E, et al. The MCP/eotaxin subfamily of CC chemokines. Cytokine Growth Factor Rev. 1999;10(1): 61-86.
3. Menten P, et al. The LD78beta isoform of MIP-1alpha is the most potent CCR5 agonist and HIV-1-inhibiting chemokine. J Clin Invest. 2002;110(4): 587-94.
4. Negus RP, et al. The detection and localization of monocyte chemoattractant protein-1 (MCP-1) in human ovarian cancer. J Clin Invest. 1995;95(5): 2391-6.
5. Bandapalli OR, et al. Transcriptional activation of CCL8 by TGF-β1-SMAD/SMAD4 and IFN-γ-NF-κB in colorectal cancer stroma. Int J Cancer. 2014;134(3): 517-28.
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