NF-E2 p18 Background Information The nuclear DNA binding protein NF-E2 regulates expression of globulin genes in developing erythroid cells through interaction with upstream AP-1-like recognition sites. More specifically, NF-E2 recognizes a site containing an intact AP-1 binding motif, preceded by a G residue two base pairs upstream. NF-E2 is an obligate heterodimer composed of NF-E2 p45 and NF-E2 p18. NF-E2 p18, also known as NF-E2U or MafK, is a ubiquitously expressed component that is related to the v-Maf oncogene. It contains a basic-leucine zipper domain that functions in DNA binding and dimerization. In addition, NF-E2 p18 may play a role in erythroid differentiation. The major component of NF-E2 is a polypeptide, designated NF-E2 p45, that belongs to the basic region-leucine zipper family of transcription factors. This subunit of NF-E2 is specifically expressed at low level in hematopoietic progenitor cells and differentiated cells of the erythroid, megakaryocyte and mast cell lineages.
NF-E2 p18 (C-16) Product Citations
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NF-E2 p18 (C-16)
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NF-E2 p18 (C-16): sc-477. Western blot analysis of NF-E2 p18 expression in non-transfected: sc-117752 (A) and mouse NF-E2 p18 transfected: sc-122032 (B) 293T whole cell lysates.
NF-E2 p18 (C-16): sc-477. Immunofluorescence staining of methanol-fixed HeLa cells showing nuclear localization.
