Anti-IL17RA (Ixekizumab)-SMCC-DM1 ADC (ADC-W-1322)

 ADC Target

  • Name
  • IL17RA
  • Alternative Names
  • IL17RA; interleukin 17 receptor A; IL17R, interleukin 17 receptor; interleukin-17 receptor A; CD217; CDw217; hIL 17R; IL 17RA; IL-17 receptor A; IL17R; CANDF5; IL-17RA; hIL-17R; FLJ32274; FLJ36453; MGC10262;
  • Target Entrez Gene ID
  • 23765
  • Overview
  • Interleukin 17A (IL17A) is a proinflammatory cytokine secreted by activated T-lymphocytes. It is a potent inducer of the maturation of CD34-positive hematopoietic precursors into neutrophils. The transmembrane protein encoded by this gene (interleukin 17A receptor; IL17RA) is a ubiquitous type I membrane glycoprotein that binds with low affinity to interleukin 17A. Interleukin 17A and its receptor play a pathogenic role in many inflammatory and autoimmune diseases such as rheumatoid arthritis. Like other cytokine receptors, this receptor likely has a multimeric structure. Alternative splicing results in multiple transcript variants encoding different isoforms.

 ADC Antibody

  • Overview
  • Humanized Anti-IL17RA IgG4-kappa antibody, Ixekizumab
  • Generic name
  • Ixekizumab
  • Host animal
  • Mus musculus

 ADC Linker

  • Name
  • SMCC (N-succinimidyl 4-(Nmaleimidomethyl)cyclohexane-1-carboxylate)
  • Description
  • Disulfide Linkers, are extensively exploited as a chemically labile linkage. Since the release of disulfide-linked drugs requires a cytoplasmic thiol cofactor, such as glutathione (GSH). Disulfides maintain stable at physiological pH and only when ADCs are internalized inside cells, the cytosol provides reducing environment including intracellular enzyme protein disulfide isomerase, or similar enzymes, drugs can be released.

 ADC payload drug

  • Name
  • DM1 (N2'-Deacetyl-N2'-(3-mercapto-1-oxopropyl)maytansine)
  • Description
  • Derived from Maytansinoid,a group of cytotoxins structurally similar to rifamycin, geldanamycin, and ansatrienin. The eponymous natural cytotoxic agent maytansine is a 19-member lactam (ansa macrolide) structure originally isolated from the Ethiopian shrub Maytenus ovatus. Maytansinoids can bind to tubulin at or near the vinblastine-binding site, which interfere the formation of microtubules and depolymerize already formed microtubules, inducing mitotic arrest in the intoxicated cells.

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