ACKR2 (E9J8U) Rabbit mAb recognizes endogenous levels of total ACKR2 protein.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human ACKR2 protein.

Chemokines are small, secreted proteins that regulate immune and inflammatory responses, controlling leukocyte migration and localization (1,4,6). Chemokine signaling is typically regulated through G protein-coupled chemokine receptors (CCRs). However, chemokines can also bind to a small family of atypical chemokine receptors (ACKRs) (2,6). ACKR2 has been shown to act as a scavenger for most inflammatory chemokines and to negatively regulate inflammation (4,5). By scavenging chemokines in tissues and on surfaces of lymphatic vessels, ACKR2 plays a vital role in the dissolution of inflammatory responses, regulating adaptive immune response, and autoimmunity (3,5,7). ACKR2 can act as a mediator of signaling between inflammatory leukocytes and lymphatic endothelial cells and has been implicated in dendritic cell maturation (4,5). ACKR2 is expressed in hematopoietic precursors and downregulated during myeloid differentiation (5). Loss of ACKR2 in mouse models has been shown to increase inflammation and tumor growth (2,4). ACKRs are emerging as crucial regulatory components of chemokine networks in a wide range of developmental, physiological, and pathological contexts.