Recombinant Human CCR1 protein

CCR1 (C-C chemokine receptor type 1) is a G protein-coupled receptor (GPCR) that plays a pivotal role in immune regulation and inflammatory responses. It belongs to the chemokine receptor family and primarily binds to C-C motif ligands such as CCL3 (MIP-1α), CCL5 (RANTES), and CCL7 (MCP-3). Expressed on various immune cells, including monocytes, neutrophils, T cells, and dendritic cells, CCR1 mediates chemotaxis and cellular activation in response to inflammatory signals. Its activation triggers intracellular signaling pathways, such as calcium mobilization and MAP kinase activation, which are critical for leukocyte recruitment to infection or injury sites.

Recombinant CCR1 protein is engineered for in vitro studies to elucidate its structural and functional properties. Produced using heterologous expression systems (e.g., mammalian, insect, or bacterial cells), the recombinant form typically retains key domains, such as the seven transmembrane helices and ligand-binding regions, enabling interaction studies with chemokines or potential therapeutic inhibitors. Purification tags (e.g., His-tag) are often incorporated to facilitate isolation and characterization.

Research on recombinant CCR1 is driven by its implication in chronic inflammatory diseases (e.g., rheumatoid arthritis, multiple sclerosis) and cancer metastasis. It serves as a target for drug discovery, with efforts focused on developing antagonists to block pathogenic leukocyte migration. Additionally, recombinant CCR1 is used in ligand-receptor binding assays, signaling pathway analysis, and high-throughput screening platforms. Challenges remain in maintaining its native conformation and post-translational modifications during production, which are essential for functional studies. Understanding CCR1's role through recombinant models continues to advance therapeutic strategies for immune-related disorders.