Combining with interleukin-6 to initiate a change in cell activity.

Combining with a biogenic amine to initiate a change in cell activity.

The formation from simpler components of a cuticle, the outer layer of some animals and plants, which acts to prevent water loss.

The process by which a microorganism (or other particulate material) is rendered more susceptible to phagocytosis by coating with an opsonin, a blood serum protein such as a complement component or antibody.

cuticle biosynthesis during molting (sensu Protostomia and Nematoda)

cuticle synthesis during molting (sensu Protostomia and Nematoda)

Synthesis and deposition of a noncellular, hardened, or membranous secretion from an epithelial sheet, occurring as part of the molting cycle. As in, but not restricted to, the taxon Protostomia (Protostomia, ncbi_taxonomy_id:33317), and the roundworms (Nematoda, ncbi_taxonomy_id:6231).

Combining with interleukin-7 to initiate a change in cell activity.

cuticle biosynthesis during molting (sensu Insecta)

cuticle synthesis during molting (sensu Insecta)

The synthesis and deposition of a noncellular, hardened, or membranous secretion from an epithelial sheet, occurring as part of the molting cycle. As in, but not restricted to, the true insects (Insecta, ncbi_taxonomy_id:50557).

Combining with interleukin-8 to initiate a change in cell activity.

cuticle biosynthesis during molting (sensu Nematoda)

cuticle synthesis during molting (sensu Nematoda)

Synthesis and deposition of a noncellular, hardened, or membranous secretion from an epithelial sheet, occurring as part of the molting cycle, as in, but not restricted to, the roundworms (Nematoda, ncbi_taxonomy_id:6231).

Combining with interleukin-9 to initiate a change in cell activity.

The chemical reactions involving keratan sulfate, a glycosaminoglycan with repeat units consisting of beta-1,4-linked D-galactopyranosyl-beta-(1,4)-N-acetyl-D-glucosamine 6-sulfate and with variable amounts of fucose, sialic acid and mannose units; keratan sulfate chains are covalently linked by a glycosidic attachment through the trisaccharide galactosyl-galactosyl-xylose to peptidyl-threonine or serine residues.