ACKR1 Protein, Human (Cell-Free, His)

ACKR3, an atypical chemokine receptor, serves as a key regulator of chemokine levels and localization through high-affinity binding to chemokines, leading to chemokine sequestration, degradation, or transcytosis. Also referred to as an interceptor, chemokine-scavenging receptor, or chemokine decoy receptor, ACKR3 functions as a receptor for chemokines such as CXCL11 and CXCL12/SDF1. Unlike traditional ligand-driven signal transduction, chemokine binding to ACKR3 does not activate G-protein-mediated pathways but induces beta-arrestin recruitment, resulting in ligand internalization and activation of the MAPK signaling pathway. ACKR3 plays a crucial role in regulating CXCR4 protein levels in migrating interneurons, adapting their chemokine responsiveness. In glioma cells, it transduces signals through the MEK/ERK pathway, contributing to cell growth and survival. While not involved in normal hematopoietic progenitor cell functions, ACKR3 is activated by CXCL11 in malignant hematopoietic cells, leading to ERK1/2 phosphorylation, enhanced cell adhesion, and migration. Additionally, ACKR3 acts as a coreceptor with CXCR4 for a limited subset of HIV isolates, highlighting its involvement in microbial infection.