Mouse IL-11 R alpha Biotinylated Antibody

Mouse interleukin 11 receptor alpha (IL-11 R alpha), originally designated NR1, is a member of the hematopoietic cytokine receptor family that was cloned on the basis of its conserved WSXWS motif. IL-11 R alpha cDNA encodes a 432 amino acid (aa) residue precursor type I membrane protein with a 23 aa residue signal peptide, a 344 aa residue extracellular domain containing two potential glycosylation sites, a 26 aa residue transmembrane region and a short (39 aa residue) cytoplasmic domain. In comparison with other hematopoietic cytokine receptors, the extracellular domain of IL-11 R alpha is closely related to that of IL-6 R alpha, CNTF R alpha and the p40 subunit of IL‑12, exhibiting 24%, 22% and 16% amino acid sequence identity, respectively. By itself, IL-11 R alpha binds IL-11 with low affinity. IL-11 R alpha, together with gp130, forms a functional high-affinity receptor complex for IL-11. The expression of IL-11 R alpha has been detected in all adult tissues examined (lung, stomach, intestine), during embryonic development and in totipotent and differentiating embryonic stem cells. Recombinant soluble IL-11 R alpha has been shown to mediate IL-11 responsiveness in cells expressing the gp130 molecule. In cells expressing transmembrane IL-11 R alpha and gp130, soluble IL-11 R alpha has been shown to act as an IL-11 antagonist.