Cytokines
Product List
Recombinant Human C-C motif chemokine 5 protein (CCL5)
Our Recombinant Human CCL5 protein is a versatile tool for advancing immunological research. Produced in E. coli, this full-length mature protein encompasses amino acids 24-91 and is tag-free for optimal compatibility with your experiments. Supplied as a lyophilized powder, the product can be conveniently reconstituted according to your specific requirements.
Our commitment to quality ensures a purity of >98% for the Recombinant Human CCL5 protein, as verified by SDS-PAGE and HPLC analysis. Endotoxin levels are meticulously controlled below 1.0 EU/µg using the LAL method. Furthermore, the protein's biological activity is demonstrated through a chemotaxis bioassay utilizing human peripheral blood monocytes, with an effective concentration range of 1.0-10 ng/ml.
CCL5 plays a pivotal role in the recruitment and activation of immune cells, with research highlighting its involvement in diverse immune responses and inflammatory processes[1]. Consequently, our Recombinant Human CCL5 protein serves as a valuable tool in elucidating the molecular mechanisms underlying immune function and developing novel therapeutics for immune-related disorders[2].
References:
1. Appay V, Rowland-Jones SL. RANTES: a versatile and controversial chemokine. Trends Immunol. 2001;22(2): 83-87.
2. Proost P, Struyf S, Van Damme J. Natural post-translational modifications of chemokines. Biochem Soc Trans. 2006;34(Pt 6): 997-1001.
Recombinant Human C-C motif chemokine 7 protein (CCL7) (Active)
Our Recombinant Human CCL7 protein offers a valuable tool for researchers in immunology. This C-C motif chemokine 7, also known as CCL7, MCP3, SCYA6, and SCYA7, is expressed in E. coli and encompasses the 24-99aa expression region of the full-length mature protein. The tag-free protein is supplied as a lyophilized powder, ensuring convenient reconstitution with sterile water or buffer for diverse experimental applications.
We prioritize quality, and our Recombinant Human CCL7 protein exhibits a purity exceeding 97%, as verified by SDS-PAGE and HPLC analysis. Endotoxin levels are rigorously maintained below 1.0 EU/µg, as determined by the LAL method. The protein demonstrates full biological activity in a chemotaxis bioassay using human monocytes, with an effective concentration range of 10-100 ng/ml.
Recent studies have illuminated the role of CCL7 in immune system regulation and its implication in various pathologies, including inflammatory diseases[1], autoimmune diseases[2], and cancer[3]. The multifaceted functions of CCL7 within the immune system underscore its significance as a research target and its potential for therapeutic applications.
References:
1. Proost P, et al. Posttranslational modifications affect the activity of the human monocyte chemotactic proteins MCP-1 and MCP-2: identification of MCP-2(6-76) as a natural chemokine inhibitor. J Immunol. 1996;156(6): 2079-85.
2. Weber C, et al. MCP-3 (CCL7) delivered by parvovirus MVMp reduces tumorigenicity of mouse melanoma cells through activation of T lymphocytes and NK cells. Int J Cancer. 2002;99(6): 923-7.
3. Wang L, et al. The C-C motif chemokine ligand 7 and interferon γ play an important role in the development of focal and segmental glomerulosclerosis. Ann Transl Med. 2020;8(6): 388.
Recombinant Human C-C motif chemokine 8 protein (CCL8) (Active)
Recombinant Human CCL8 protein, a critical research tool for immunology studies, offers valuable insights into the intricacies of immune system function. 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, enabling straightforward reconstitution with sterile water or buffer for a wide array of experimental applications.
We are committed to providing high-quality and high-performance products. Our Recombinant Human CCL8 protein exhibits a purity of >96%, as determined by SDS-PAGE and HPLC analysis. 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.
Extensive research has been conducted to elucidate 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)[1], who established 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)[2], highlighting its role in immune responses. Menten et al. (2002)[3] investigated the relationship between CCL8 and HIV-1 infection, demonstrating that CCL8 serves as a potent inhibitor of the R5 strains of HIV-1, suggesting its potential role in controlling HIV-1 infection. CCL8's association with cancer was demonstrated by Negus et al. (1995)[4], 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)[5] revealed the involvement of CCL8 in colorectal cancer progression and its potential as a diagnostic and therapeutic target.
References:
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.
Recombinant Human C-C motif chemokine 14 protein (CCL14), partial (Active)
This recombinant human CCL14 protein, expressed in E. coli, comprises amino acids 22-93 of the human CCL14 sequence. Supplied as a tag-free lyophilized powder, it is readily reconstituted with sterile water or buffer. Purity exceeds 96%, as verified by SDS-PAGE and HPLC. Endotoxin levels are below 1.0 EU/µg (LAL method). Bioactivity is comparable to the standard, exhibiting a chemotactic activity range of 5.0-20 ng/ml in a human monocyte assay.
C-C motif chemokine 14 (CCL14) is a member of the CC chemokine family, playing a crucial role in immune system regulation by modulating immune cell trafficking and function. Research into CCL14 is vital for understanding immune responses and developing potential therapeutics for immune-related diseases.
Recombinant Human C-C motif chemokine 13 protein (CCL13), partial (Active)
This recombinant human CCL13 protein is expressed in E. coli and encompasses an amino acid sequence corresponding to residues 24-98 of the human CCL13 protein. The product is tag-free and supplied as a lyophilized powder, which can be reconstituted in sterile water or buffer prior to use. The protein exhibits a purity exceeding 96%, as determined by SDS-PAGE and HPLC, and the endotoxin level is less than 1.0 EU/µg, as measured by the LAL method. The recombinant CCL13 demonstrates full biological activity in comparison to the standard, with its activity confirmed through a chemotaxis bioassay utilizing human monocytes at a concentration range of 10-100 ng/ml.
C-C motif chemokine 13 (CCL13), a small secreted protein belonging to the CC chemokine family, plays a crucial role in immune and inflammatory responses. CCL13 is involved in the recruitment and activation of immune cells, particularly monocytes, and its function and regulation have been extensively studied in the field of immunology.
Recombinant Human C-C motif chemokine 16 protein (CCL16) (Active)
Our Recombinant Human CCL16 (C-C motif chemokine 16) is expressed in *E. coli* and encompasses the full length of the mature protein (amino acids 24-120). This product is supplied as a lyophilized powder with a purity exceeding 97%, as confirmed by SDS-PAGE and HPLC. The endotoxin level is less than 1.0 EU/µg as determined by the LAL method. The recombinant CCL16 is tag-free for enhanced versatility in various applications.
CCL16 is a chemokine that plays a critical role in the trafficking and activation of leukocytes[1]. It has been implicated in various inflammatory diseases, including rheumatoid arthritis and atherosclerosis[2,3]. CCL16 exhibits chemotactic activity for monocytes, lymphocytes, and eosinophils[4]. Additionally, CCL16 has been shown to have a potential role in angiogenesis and tumor progression[5].
Demonstrating full biological activity, the recombinant human CCL16 exhibits a concentration range of 10-100 ng/ml in chemotaxis bioassays using human monocytes, when compared to a standard reference.
References:
1. Mantovani, A. *et al*. The chemokine system in diverse forms of macrophage activation and polarization. Trends Immunol. 2000; 21(6): 303-307.
2. Hosaka, S. *et al*. Predominant expression of the human LIM and SH3 domain protein, hILINCK in activated monocyte lineage. FEBS Lett. 2000; 481(2): 93-98.
3. Van Coillie, E. *et al*. Human monocyte chemotactic proteins-2 and -3: structural and functional comparison with MCP-1. J. Immunol. 1999; 162(7): 4349-4359.
4. Hieshima, K. *et al*. Molecular cloning of a novel human CC chemokine liver and activation-regulated chemokine (LARC) expressed in liver. Chemotactic activity for lymphocytes and gene localization on chromosome 2. J. Biol. Chem. 1997; 272(38): 23913-23921.
5. Müller, G. and Lipp, M. Signal transduction by the chemokine receptor CXCR5: Structural requirements for G protein activation analyzed by chimeric CXCR1/CXCR5 molecules. J. Exp. Med. 2001; 194(2): 181-192.
Recombinant Human C-X-C motif chemokine 2 protein (CXCL2)
Our Recombinant Human CXCL2 protein is a valuable research tool for immunology researchers. This C-X-C motif chemokine 2 protein, also known as CXCL2, GRO2, GROB, MIP2A, and SCYB2, is produced in *E. coli* and encompasses the full length of the mature protein (amino acids 35-107). This tag-free, lyophilized powder can be readily reconstituted with sterile water or a suitable buffer to meet various experimental needs.
Our Recombinant Human CXCL2 protein exhibits high purity, exceeding 97% as confirmed by both SDS-PAGE and HPLC analyses. Endotoxin levels are rigorously controlled, ensuring they remain below 1.0 EU/µg, as verified by the LAL method. The protein demonstrates full biological activity when compared to a standard, with its biological activity determined by a chemotaxis bioassay using human CXCR2 transfected human 293 cells within a concentration range of 10-100 ng/ml.
The significance of CXCL2 in immunology research is well-established. For example, Zhou *et al*. (2001)[1] highlighted the crucial role of CXCL2 in neutrophil infiltration and activation during acute inflammation, suggesting its potential therapeutic applications. In another study, Sugimoto *et al*. (2012)[2] reported the potential anti-inflammatory effects of CXCL2 inhibition in experimental autoimmune encephalomyelitis, an animal model of multiple sclerosis, further underscoring the protein's relevance in understanding immune system function and developing potential treatments for immune-related disorders.
References:
1. Zhou H, *et al*. Neutrophil infiltration and activation in bronchoalveolar lavage fluid from patients with acute respiratory distress syndrome: a role for C-X-C chemokine. Chin Med J (Engl). 2001;114(2):174-8.
2. Sugimoto K, *et al*. Inhibition of C-X-C chemokine receptor 2 (CXCR2) suppresses EAE development by suppressing accumulation of neutrophils and macrophages in the CNS, and subsequent demyelination. Nihon Rinsho Meneki Gakkai Kaishi. 2012;35(5):424-33.
Recombinant Human C-C motif chemokine 23 protein (CCL23), partial (Active)
This recombinant human CCL23 protein is produced in *E. coli* and encompasses a partial sequence (22-120aa) of the NM_145898 isoform. Supplied as a lyophilized powder, this tag-free protein facilitates convenient reconstitution with sterile water or buffer. With a purity exceeding 97%, as confirmed by SDS-PAGE and HPLC, our recombinant CCL23 maintains a low endotoxin level below 1.0 EU/µg, as determined by the LAL method. This protein demonstrates full biological activity, evidenced by its efficacy in a chemotaxis bioassay using human T-lymphocytes, with an activity concentration range of 10-50 ng/ml.
As a member of the CC chemokine family, C-C motif chemokine 23 (CCL23) plays a crucial role in regulating immune cell trafficking and function. Understanding CCL23's functions and mechanisms is essential for comprehending its impact on the immune system and developing potential therapeutic strategies for immune-related disorders.
Recombinant Human C-C motif chemokine 25 protein (CCL25)
This recombinant Human CCL25 protein is a high-quality research tool designed for a wide array of immunology applications. Also known as C-C motif chemokine 25, this full-length mature protein is expressed in E. coli, encompassing the 24-150aa expression region. The tag-free, lyophilized powder can be readily reconstituted with sterile water or buffer, ensuring ease of use.
The quality of our Recombinant Human CCL25 protein is rigorously assured, exhibiting a purity exceeding 97%, as determined by SDS-PAGE and HPLC analysis. Additionally, endotoxin levels are stringently maintained below 1.0 EU/µg, as confirmed by the LAL method. Our CCL25 protein demonstrates robust biological activity in a chemotaxis bioassay utilizing human monocytes, with an effective concentration range spanning 1.0-10 ng/ml.
CCL25 has been the subject of extensive research exploring its crucial role in the immune system. For instance, Zaballos et al. (1999)[1] elucidated that CCL25 is a potent chemoattractant for lymphocytes, particularly T cells. Subsequently, Bowman et al. (2006)[2] emphasized the integral involvement of CCL25 in the development and functionality of the small intestine's immune system. Most recently, research conducted by Kim et al. (2017)[3] revealed a significant correlation between CCL25 and rheumatoid arthritis, suggesting promising therapeutic potential in this disease. Collectively, these findings underscore the profound importance of CCL25 in immune regulation and its potential as a target for future therapeutic interventions.
References:
1. Zaballos A, et al. Identification of a novel CC chemokine, human eotaxin-2, that is specific for CCR3 and displays high eosinophil chemotactic activity. J Immunol. 1999;162(11): 6798-801.
2. Bowman EP, et al. The intestinal chemokine thymus-expressed chemokine (CCL25) attracts IgA antibody-secreting cells. J Exp Med. 2006;203(3): 507-13.
3. Kim HR, et al. Chemokine CC motif ligand 25 enhances resistance to apoptosis in CD4+ T cells from patients with rheumatoid arthritis by increasing the activation of the PI3K/Akt and STAT3 pathways. Front Immunol. 2017;8: 820.
