epitope mapping at the C-terminus of NF-E2 p18 of mouse origin
Modification Notes
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.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISAGSChIP
recommended for detection of NF-E2 p18 (also designated MafK) of mouse, rat and human origin by WB, IP, IF and ELISA:
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope mapping at the C-terminus of NF-E2 p18 of mouse origin
Tissue Specificity
epitope mapping at the C-terminus of NF-E2 p18 of mouse origin