epitope mapping within an extracellular domain of CCRL2 of human origin
Modification Notes
CCRL2 (C-C chemokine receptor-like 2), also known as chemokine receptor X, human chemokine receptor (HCR), CRAM-A or CRAM-B, is a seven pass transmembrane protein expressed by monocytes, neutrophils, and dendritic cells of immunal tissues (predominanly spleen, fetal liver, bone marrow and lymph node). It shares over 40% homology with other C-C chemokine receptors but does not share the conserved DRY motif which is among the important motifs necessary for signalling and ligand-binding. C-C chemokine receptors are G-protein coupled, seven pass transmembrane domain proteins whose major physiological role is to function in the chemotaxis of T cells and phagocytic cells to areas of inflammation. CCRL2 responds to inflammatory chemokines and is upregulated in cells stimulated with lipopolysaccharide (LPS). It may function as a receptor for CCL2, CCL5, CCL7 and CCL8. In addition, CCRL2 may be involved in the pathogenesis of rheumatoid arthritis (RA).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of CCRL2 of human origin by WB, IP, IF and ELISA:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope mapping within an extracellular domain of CCRL2 of human origin
Tissue Specificity
epitope mapping within an extracellular domain of CCRL2 of human origin