Cytokines

Recombinant Human CXCL11 protein is a valuable research tool for immunology studies. This C-X-C motif chemokine 11, also known as CXCL11, ITAC, SCYB11, and SCYB9B, is produced in *E. coli* and represents the 22-94aa expression region of the full-length mature protein. The tag-free protein is supplied as a lyophilized powder, facilitating reconstitution with sterile water or a suitable buffer for diverse experimental applications.

Our Recombinant Human CXCL11 protein exhibits high purity, exceeding 97%, as confirmed by SDS-PAGE and HPLC analysis. The endotoxin level is meticulously controlled, measuring less than 1.0 EU/µg, as determined by the LAL method. This protein demonstrates full biological activity, as evidenced by its efficacy in a chemotaxis bioassay using IL-2-activated human T-lymphocytes, with an effective concentration range of 0.1-10 ng/ml.

CXCL11 chemokine has been extensively studied. Loetscher *et al*. (1998)^[1] first characterized CXCL11 as a selective ligand for CXCR3, attracting activated T cells. In 2001, Farber (2001)^[2] reviewed CXCL11's role in T-cell trafficking regulation and its involvement in inflammatory diseases. More recently, Teng *et al*. (2018)^[3] investigated the potential of CXCL11 as a biomarker for human colorectal cancer. These studies emphasize CXCL11's crucial role in immune system function and its potential as a therapeutic target for various immune-related disorders.

References:
1. Loetscher M, *et al*. CXC chemokine IP-10 and Mig: Regulation of chemotactic activity *in vitro* and expression *in vivo*. *J Immunol*. 1998;160(6): 2557-65.
2. Farber JM. Mig and IP-10: CXC chemokines that target lymphocytes. *J Leukoc Biol*. 1997;61(3): 246-57.
3. Teng KY, *et al*. Plasma CXCL10 is a potential biomarker for colorectal cancer. *Oncol Lett*. 2018;15(4): 4205-10.

Recombinant Human CXCL13 protein is a valuable research tool for immunology studies. This C-X-C motif chemokine 13, also known as CXCL13, BCA1, BLC, and SCYB13, is expressed in E. coli and encompasses the 23-109 amino acid region, encompassing the full length of the mature protein. Supplied as a tag-free, lyophilized powder, this protein is easily reconstituted with sterile water or a suitable buffer, accommodating various experimental needs.

Our Recombinant Human CXCL13 protein demonstrates high purity, exceeding 97%, as validated by both SDS-PAGE and HPLC analyses. Endotoxin levels are meticulously controlled, remaining below 1.0 EU/µg, confirmed by the LAL method. The protein exhibits full biological activity when compared to the standard, with its biological activity determined by a chemotaxis bioassay using human B cells within a concentration range of 1.0-10 ng/ml.

Numerous studies have underscored the significance of CXCL13 in immunology research. For instance, Ansel *et al*. (2000)^[1] investigated the role of CXCL13 in organizing B cell follicles within secondary lymphoid tissues. Moreover, Allen *et al*. (2004)^[2] demonstrated the involvement of CXCL13 in regulating the homeostatic trafficking of B and T cells. More recently, Förster *et al*. (2021)^[3] explored the potential of CXCL13 as a biomarker in inflammatory diseases, highlighting the importance of CXCL13 in comprehending immune system function and potential therapeutic applications in immune-related disorders.

References:
1. Ansel KM, *et al*. A chemokine-driven positive feedback loop organizes lymphoid follicles. Nature. 2000;406(6793):309-14.
2. Allen CD, *et al*. Germinal center dark and light zone organization is mediated by CXCR4 and CXCR5. Nat Immunol. 2004;5(9):943-52.
3. Förster Y, *et al*. CXCL13: A novel biomarker for inflammation? Int J Mol Sci. 2021;22(11):6039.

Recombinant Human CCL2 protein is a valuable research tool for immunology investigations. This C-C motif chemokine 2, also known as CCL2, MCP1, and SCYA2, is produced in E. coli and encompasses the 24-99aa expression region, representing the full-length mature protein. The tag-free protein is supplied as a lyophilized powder, allowing for convenient reconstitution using sterile water or a suitable buffer to accommodate diverse experimental needs.

Our Recombinant Human CCL2 protein exhibits a high purity level, exceeding 96%, as confirmed by both SDS-PAGE and HPLC analyses. Endotoxin levels are rigorously controlled to remain below 1.0 EU/µg, as verified through the LAL method. This protein demonstrates full biological activity, as evidenced by its efficacy in a chemotaxis bioassay with human monocytes, displaying a functional concentration range of 10-100 ng/ml.

The CCL2 chemokine has been extensively studied in scientific research. Matsushima and Oppenheim (1989)^[1] initially reported the identification and purification of the monocyte chemotactic and activating factor, subsequently known as CCL2. In 2013, Deshmane et al.^[2] provided a comprehensive review of the multifaceted roles of CCL2 in inflammation and disease pathogenesis, including its implications in cancer progression. More recently, Yang et al. (2018)^[3] highlighted the potential use of CCL2 as a diagnostic biomarker for rheumatoid arthritis. These studies underscore the significance of CCL2 in immune system function and suggest its potential therapeutic value in treating various immune-related diseases.

References:
1. Matsushima K, Oppenheim JJ. Interleukin 8 and MCAF: novel inflammatory cytokines inducible by IL 1 and TNF. Cytokine. 1989;1(1):2-13.
2. Deshmane SL, et al. Monocyte Chemoattractant Protein-1 (MCP-1): An Overview. J Interferon Cytokine Res. 2009;29(6):313-26.
3. Yang M, et al. The diagnostic value of serum CCL2/MCP-1 levels in patients with rheumatoid arthritis. Ann Palliat Med. 2018;7(3):312-8.

Our recombinant human CCL11 protein, also known as Eotaxin, is expressed in E. coli and encompasses the full length of the mature 24-97 amino acid sequence. This tag-free protein is supplied as a lyophilized powder, facilitating convenient reconstitution with sterile water or buffer. With a purity exceeding 97%, as determined by SDS-PAGE and HPLC, our recombinant CCL11 also exhibits a low endotoxin level of less than 1.0 EU/µg, as measured by the LAL method. The protein is fully biologically active, as confirmed by its efficacy in a chemotaxis bioassay using human peripheral blood eosinophils, with an activity concentration range of 0.1-10.0 ng/ml.

C-C motif chemokine 11 (CCL11), or Eotaxin, is a crucial protein involved in the recruitment and activation of eosinophils in response to allergens and other stimuli. CCL11 plays a pivotal role in allergic diseases, including asthma, atopic dermatitis, and allergic rhinitis. Consequently, investigating the functions and mechanisms of CCL11 is essential for developing potential therapeutic interventions for these immune-related diseases.

Extensive research has been conducted to elucidate the role of CCL11 in immune regulation. For instance, Ponath et al. (1996)^[1] first identified CCL11 as a potent eosinophil chemoattractant. Subsequently, Ying et al. (1999)^[2] demonstrated that CCL11 was significantly upregulated in bronchial biopsies from asthmatic patients compared to non-asthmatic subjects. More recent studies have uncovered the involvement of CCL11 in other pathological conditions, such as neuroinflammation and cognitive decline in Alzheimer's disease (Villeda et al. (2011)^[3]). Moreover, CCL11 has been implicated in cancer progression and metastasis, as shown in the study by Chen et al. (2019)^[4], which revealed that CCL11 could promote colorectal cancer cell migration and invasion. Additionally, a study by Choi et al. (2021)^[5] suggested that CCL11 may serve as a therapeutic target for treating eosinophilic esophagitis.

References:
1. Ponath PD, et al. Cloning of the human eosinophil chemoattractant, eotaxin. Expression, receptor binding, and functional properties suggest a mechanism for the selective recruitment of eosinophils. J Clin Invest. 1996;97(3): 604-12.
2. Ying S, et al. Enhanced expression of eotaxin and CCR3 mRNA and protein in atopic asthma. Association with airway hyperresponsiveness and predominant co-localization of eotaxin mRNA to bronchial epithelial and endothelial cells. Eur J Immunol. 1999;29(12): 3847-56.
3. Villeda SA, et al. The ageing systemic milieu negatively regulates neurogenesis and cognitive function. Nature. 2011;477(7362): 90-4.
4. Chen W, et al. CCL11 promotes migration and proliferation of mouse neural progenitor cells. Stem Cell Res Ther. 2019;10(1): 395.
5. Choi J, et al. Increased expression of C-C motif chemokine ligand 11 and its specific receptor, C-C motif chemokine receptor 3, in eosinophilic esophagitis: the potential role of CCL11 in eosinophilic esophagitis pathogenesis. J Allergy Clin Immunol Pract. 2021;9(4): 1584-1594.e4.