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IL32 alfa is the shortest of the 4 isotypes of IL32 known, it is 134 amino acids ( kDa) protein, the IL32B (beta) is 188, IL32C is 168 and IL32D is 179 amino acids long proteins. Each subtype has an N-terminal segment and four kringle domains (NK4), that interact with several other proteins including the hepatic growth factor via c-met a tyrosine receptor kinase (5). IL-32 synergized with the intracellular nuclear oligomerization domain receptors (NOD1- and NOD2-specific muropeptides of peptidoglycans for the release of IL-1beta and IL-6. In contrast, IL-32 did not influence the cytokine production induced via TLRs (6). The anti-IL32 selective antibodies were made against an epitope that lies near the C-terminal end of the protein. The antibodies to IL32 are affinity purified on immobilized affinity based chromatography and characterized for applications in ELISA and Western blotting. The antiIL32 antibodies recognize a single band of IL32 in PC-IL32 samples. The IL32 antibodies do not cross react with other pro-inflammatory or anti-inflammatory interleukins, has also produced antibodies to other interleukins, interleukin receptors, cytokines and their receptors.