Recombinant Mouse Ccl21c protein

Ccl21c, a splice variant of the CCL21 chemokine, belongs to the CC chemokine family and plays a critical role in immune cell trafficking and lymphoid tissue organization. The full-length CCL21 gene produces multiple isoforms (Ccl21a, Ccl21b, Ccl21c) through alternative splicing, with Ccl21c distinguished by its unique C-terminal sequence. This protein is primarily secreted by stromal cells in lymph nodes and high endothelial venules, where it binds to the CCR7 receptor on dendritic cells, T cells, and B cells, guiding their migration to secondary lymphoid organs. Unlike other isoforms, Ccl21c lacks a heparin-binding domain, altering its tissue distribution and functional interactions.

Recombinant Ccl21c is produced using expression systems like E. coli or mammalian cells, followed by purification via affinity tags (e.g., His-tag) and chromatography. Quality validation typically involves SDS-PAGE, Western blotting, and functional assays to confirm receptor-binding activity. Its production enables controlled studies on CCR7-mediated signaling, lymphocyte homing, and immune responses in vitro and in vivo.

Research applications include investigating immune cell recruitment in inflammation, cancer metastasis (where CCR7-CCL21 axes often promote tumor dissemination), and lymphoid neogenesis. Ccl21c is also explored as a therapeutic target or adjuvant to modulate immune activity in autoimmune diseases or vaccine development. However, functional differences between Ccl21 isoforms and species-specific variations (human vs. murine models) require careful interpretation. Current studies focus on resolving its structural nuances and tissue-specific roles to harness its potential in immunotherapy and diagnostic strategies.