Cytokines
Product List
Recombinant Human C-C motif chemokine 21 protein (CCL21)
Our recombinant human CCL21 protein, expressed in E. coli, encompasses the full-length mature protein sequence, spanning from amino acids 24 to 134. This tag-free protein is supplied as a lyophilized powder that can be readily reconstituted with sterile water or buffer. The purity of our recombinant CCL21 exceeds 97%, as confirmed by SDS-PAGE and HPLC analysis. The endotoxin content remains below 1.0 EU/µg, as determined using the LAL method. The protein exhibits full biological activity, as demonstrated in a chemotaxis bioassay with human lymphocytes, eliciting activity within a concentration range of 10-100 ng/ml.
As a member of the CC chemokine family, C-C motif chemokine 21 (CCL21) plays a significant role in immune cell migration and function. Comprehensive understanding of CCL21's functions and mechanisms is crucial for elucidating its role within the immune system and its potential as a therapeutic target for immune-related diseases.
Recombinant Human C-C motif chemokine 22 protein (CCL22) (Active)
Our recombinant human CCL22 protein is produced in *Escherichia coli* and encompasses the mature protein sequence from amino acids 25-93. This tag-free protein is supplied as a lyophilized powder for convenient reconstitution using sterile water or buffer. It exhibits a purity exceeding 97%, confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and high-performance liquid chromatography (HPLC). The endotoxin level is less than 1.0 EU/µg, as determined by the limulus amebocyte lysate (LAL) method. The protein is fully biologically active, as demonstrated in a chemotaxis bioassay using human T-lymphocytes, where it displays activity within a concentration range of 10-100 ng/ml.
C-C motif chemokine 22 (CCL22), belonging to the CC chemokine family, plays a crucial role in regulating immune cell trafficking and function. Investigating the functions and mechanisms of CCL22 is essential for understanding its impact on the immune system and for identifying potential therapeutic targets for immune-related conditions.
Recombinant Human C-C motif chemokine 24 protein (CCL24), partial (Active)
This Recombinant Human CCL24 protein is a high-quality reagent for immunological research. Expressed in E. coli, it comprises amino acids 27-104. Supplied as a tag-free, lyophilized powder for convenient reconstitution with sterile water or buffer.
Rigorous quality control ensures >97% purity (SDS-PAGE and HPLC), with endotoxin levels consistently below 1.0 EU/µg (LAL method). Bioactivity is confirmed via a chemotaxis assay using human peripheral blood eosinophils, exhibiting activity within the 50-100 ng/ml concentration range.
CCL24 plays a crucial role in immunoregulation. Kitaura et al. (1999)[1] demonstrated its function as a selective eosinophil chemoattractant, vital in allergic disorder pathogenesis. Furthermore, Yuan et al. (2016)[2] implicated CCL24 in atopic dermatitis development, highlighting its therapeutic potential. These studies underscore CCL24's importance in the immune system and its potential as a target for immune-related disease interventions.
References:
[1] Kitaura M, et al. Molecular cloning of human eotaxin, an eosinophil-selective CC chemokine, and identification of a specific eosinophil eotaxin receptor, CC chemokine receptor 3. J Biol Chem. 1999;274(39):27975-80.
[2] Yuan Y, et al. Serum eotaxin-1 is a potential biomarker for atopic dermatitis in an Asian population. Int J Dermatol. 2016;55(2):e86-92.
Recombinant Human C-C motif chemokine 26 protein (CCL26) (Active)
Recombinant Human CCL26 protein is an indispensable research tool for immunology investigations. This C-C motif chemokine 26, also known as CCL26, is produced in *E. coli*, encompassing the 24-94 amino acid expression region of the full-length mature protein. The tag-free protein is supplied as a lyophilized powder, facilitating easy reconstitution with sterile water or buffer for diverse experimental applications.
We prioritize quality and performance. Our Recombinant Human CCL26 protein exhibits a purity exceeding 97%, as confirmed by SDS-PAGE and HPLC analyses. Endotoxin levels are meticulously maintained below 1.0 EU/µg, as determined by the LAL method. The protein demonstrates robust biological activity in a chemotaxis bioassay utilizing human CCR3 transfected HEK293 cells, with an effective concentration range of 0.5-2.0 µg/ml.
Extensive research has delved into the role of CCL26 in immune regulation. Garcia-Zepeda *et al*. (1996)[1] initially identified CCL26 as an eosinophil-selective chemoattractant. Komiya *et al*. (2003)[2] subsequently elucidated its role in allergic inflammation. Abonyo *et al*. (2010)[3] further demonstrated CCL26's contribution to eosinophil trafficking within the airways. Ying *et al*. (2012)[4] established a link between CCL26 and asthma pathogenesis. These studies collectively underscore the pivotal role of CCL26 in the immune system and its potential as a therapeutic target for immune-related diseases.
References:
1. Garcia-Zepeda EA, *et al*. Human eotaxin is a specific chemoattractant for eosinophil cells and provides a new mechanism to explain tissue eosinophilia. *Nat Med*. 1996;2(4): 449-56.
2. Komiya A, *et al*. CCL26/eotaxin-3 is more effective to induce the migration of eosinophils of asthmatics than CCL11/eotaxin-1 and CCL24/eotaxin-2. *J Leukoc Biol*. 2003;74(4): 611-7.
3. Abonyo BO, *et al*. Human eotaxin-3/CCL26 gene expression is regulated by DNA demethylation. *Clin Exp Allergy*. 2010;40(8): 1254-63.
4. Ying S, *et al*. Expression and cellular provenance of thymic stromal lymphopoietin and chemokines in patients with severe asthma and chronic obstructive pulmonary disease. *J Immunol*. 2012;181(4): 2790-8.
