Int J Biochem Cell Biol. 2005 Apr;37(4):715-9. doi: 10.1016/j.biocel.2004.08.010.


Prominin-1, originally found on neuroepithelial stem cells in mice, is a five transmembrane domain cell-surface glycoprotein that localizes to membrane protrusions. Its homologue human Prominin-1 was first isolated from hematopoietic stem cells by a monoclonal antibody recognizing a specific epitope designated as AC133 (CD133). Transcription of Prominin-1 is driven by five tissue-specific alternative promoters resulting in the formation of differentially spliced mRNA isoforms. Prominin-1 is expressed on different types of stem cells, but it is not known if it plays a significant role in key stem cell functional features. Although the biological function of Prominin-1 is not well understood, the AC133 epitope currently serves as a useful marker for the isolation of hematopoietic and endothelial progenitor cells.

Publication types

  • Review

MeSH terms

  • AC133 Antigen
  • Alternative Splicing
  • Antigens, CD
  • Glycoproteins / genetics
  • Glycoproteins / metabolism*
  • Hydrolysis
  • Peptides / genetics
  • Peptides / metabolism*
  • RNA, Messenger / genetics


  • AC133 Antigen
  • Antigens, CD
  • Glycoproteins
  • PROM1 protein, human
  • Peptides
  • Prom1 protein, mouse
  • RNA, Messenger