Recombinant Human CXCL9 protein is a valuable research tool for immunology studies. This C-X-C motif chemokine 9 (CXCL9, also known as CMK, MIG, and SCYB9) is expressed in E. coli and encompasses amino acids 23-125, representing the full-length mature protein. Provided as a tag-free lyophilized powder, it can be readily reconstituted with sterile water or a suitable buffer for diverse experimental applications.
Our Recombinant Human CXCL9 protein exhibits high purity (>97%), confirmed by SDS-PAGE and HPLC analyses. Endotoxin levels are rigorously controlled, consistently remaining below 1.0 EU/μg (LAL method). Bioactivity is demonstrated by its efficacy in a chemotaxis bioassay using human peripheral blood T-lymphocytes, with a functional concentration range of 10-100 ng/ml.
Extensive research highlights CXCL9's importance in immunology. Luster et al. (1988)[1] identified interferon-γ-induced protein 10 (later designated CXCL9) and described its chemoattractant properties for monocytes and T cells. Groom and Luster (2011)[2] further detailed CXCL9's multifaceted roles in immune regulation and infection control. More recently, Hirahara et al. (2020)[3] explored CXCL9's potential as a biomarker and therapeutic target in autoimmune diseases.
References:
[1] Luster AD, Unkeless JC, Ravetch JV. γ-Interferon transcriptionally regulates an early-response gene containing homology to platelet proteins. Nature. 1988;334(6179):265-8.
[2] Groom JR, Luster AD. CXCR3 in T cell function. Exp Cell Res. 2011;317(5):620-31.
[3] Hirahara K, et al. Development of novel immunotherapies targeting type 1 cytokines and CXCR3. Ann Rheum Dis. 2020;79(2):157-8.
Our Recombinant Human CXCL14 protein is a valuable tool for researchers studying immunology. This C-X-C motif chemokine 14, also known as CXCL14, MIP2G, NJAC, and SCYB14, is expressed in E. coli and encompasses the 35-111aa expression region of the full-length mature protein. The tag-free protein is supplied as a lyophilized powder, enabling convenient reconstitution with sterile water or buffer for diverse experimental applications.
Quality and performance are paramount. Our Recombinant Human CXCL14 protein exhibits a purity exceeding 95%, as confirmed by SDS-PAGE and HPLC analysis. Endotoxin levels are rigorously controlled below 1.0 EU/µg, determined by the LAL method. This protein demonstrates biological activity through its ability to induce calcium flux in prostaglandin E2-treated THP1 human acute monocytic leukemia cells, with an ED50 typically in the range of 1-10 ng/mL.
CXCL14 has been extensively researched for its involvement in immune regulation, tumor progression, and cancer.[1] Studies have highlighted its chemotactic properties towards monocytes and dendritic cells[2], as well as its tumor-suppressive effects in various cancer types.[3] This underscores the significance of CXCL14 in immune system research and its potential as a therapeutic target for immune-related diseases and cancer.
References:
1. Hara T, et al. Identification of a chemotactic ligand for CXCR1 and CXCR2 in human osteosarcoma cells. Biochem Biophys Res Commun. 2009;386(4): 694-9.
2. Hromas R, et al. Cloning of BRAK, a novel divergent CXC chemokine preferentially expressed in normal versus malignant cells. Biochem Biophys Res Commun. 1999;255(3): 703-6.
3. Tanegashima K, et al. The Chemokine CXCL14 suppresses the tumorigenicity of hepatocellular carcinoma cells. Int J Cancer. 2013;132(4): 949-60.
Recombinant Human CX3CL1, also known as Fractalkine, is a multifunctional chemokine involved in immune responses. It plays a critical role in the recruitment and activation of leukocytes[1]. Our recombinant human CX3CL1 is a partial protein, encompassing amino acids 25-100, with a molecular weight of 8.6 kDa. Expressed in Escherichia coli, this tag-free recombinant protein is available in liquid or lyophilized powder form, making it suitable for diverse research applications in the field of immunology.
Our Recombinant Human CX3CL1 exhibits a purity exceeding 97%, as determined by SDS-PAGE and HPLC, ensuring high quality for your research endeavors. The endotoxin level is less than 1.0 EU/ug, as established by the LAL method. The biological activity of our CX3CL1 has been validated by a chemotaxis bioassay utilizing human T-lymphocytes, demonstrating activity within a concentration range of 5.0-10 ng/ml.
Extensive studies have demonstrated that CX3CL1 is implicated in a wide array of immune-mediated disorders, including atherosclerosis, multiple sclerosis, rheumatoid arthritis, and inflammatory bowel disease[2]. Furthermore, CX3CL1 has been linked to the regulation of tumor progression and metastasis in specific types of cancer[3].
References:
1. Bazan JF, et al. A new class of membrane-bound chemokine with a CX3C motif. Nature. 1997;385(6617): 640-4.
2. Jones BA, et al. Fractalkine/CX3CL1: A potential new target for inflammatory diseases. Mol Interv. 2010;10(5): 263-70.
3. Park MH, et al. Serum fractalkine levels are elevated in patients with advanced non-small cell lung cancer. Korean J Intern Med. 2010;25(2): 146-52.
The recombinant human CCL1 protein is expressed in *Escherichia coli* and encompasses the partial mature sequence spanning amino acids 23-96. This tag-free protein is supplied as a lyophilized powder, enabling convenient reconstitution with sterile water or buffer. With a purity exceeding 97%, as determined by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) and high-performance liquid chromatography (HPLC), our recombinant CCL1 also exhibits a low endotoxin level of less than 1.0 EU/µg, as measured using the limulus amebocyte lysate (LAL) method. The protein retains full biological activity, evidenced by its efficacy in a chemotaxis bioassay employing human T-lymphocytes, with an activity concentration range of 10-100 ng/ml.
C-C motif chemokine 1 (CCL1) belongs to the CC chemokine family and plays a pivotal role in immune cell trafficking and function. Consequently, a comprehensive understanding of CCL1's functions and mechanisms is crucial for unraveling its contributions to the immune system and the development of potential therapeutic interventions for immune-related diseases.
Recombinant Human CCL3L1 protein is an essential research tool for investigators studying immunology. This C-C motif chemokine 3-like 1 protein, also known as CCL3L1, CCL3L3, D17S1718, G0S19-2, and SCYA3L1, is expressed in *E. coli* and encompasses the full length of the mature protein (amino acids 24-93). This tag-free, lyophilized powder can be conveniently reconstituted with sterile water or an appropriate buffer to meet specific experimental needs.
Our Recombinant Human CCL3L1 protein exhibits high purity, exceeding 97% as determined by SDS-PAGE and HPLC analyses. Endotoxin levels are stringently controlled, remaining below 1.0 EU/µg, as verified by the LAL method. The protein demonstrates full biological activity, comparable to standard, as determined by a chemotaxis bioassay utilizing human monocytes within a concentration range of 1.0-10 ng/ml.