epitope mapping at the C-terminus of IL-8RA of human origin
Modification Notes
IL-8 has been shown to function as a potent neutrophil chemostatic and activating peptide and is an important mediator of inflammatory diseases. Two distinct human IL-8 receptors, designated IL-8RA and IL-8RB have been characterized. Both are expressed at a high level on neutrophils and to a lesser extent on monocytes and myeloid cell lines. In addition, the IL-8RA subunit is expressed in T cells such as the Jurkat cell line. Both IL-8Rs are members of the seven-transmembrane domain rhodopsin superfamily of receptors and as such, couple G proteins for signal transduction. The two receptors share 77% amino acid identity. IL-8RA exhibits high-affinity binding for IL-8 and low-affinity MGSA binding, whereas IL-8RB has high-affinity binding for both IL-8 and MGSA.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of IL-8RA of human origin by WB, IP, IF and ELISA:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope mapping at the C-terminus of IL-8RA of human origin
Tissue Specificity
epitope mapping at the C-terminus of IL-8RA of human origin