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 2 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

Phosphatidylinositol 3-kinase regulatory subunit alpha; PI3-kinase regulatory subunit alpha; PI3K regulatory subunit alpha; PtdIns-3-kinase regulatory subunit alpha; Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha; PI3-kinase subunit p85-alpha; PtdIns-3-kinase regulatory subunit p85-alpha; PIK3R1; GRB1

p25025

Human,Mouse,Rat

WB

WB 1:500-1:1000

~ 40 kDa

Rabbit

IL-8Rβ pAb detects endogenous levels of IL-8Rβ protein.

Synthetic peptide, corresponding to Human MYLK.

Polyclonal

Rabbit IgG

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

PBS with 0.02% sodium azide, 50% glycerol, pH7.2

1mg/ml

Store at 4℃ short term,and store at -20℃ long term. Avoid freeze-thaw cycles.