epitope mapping at the N-terminus of c-Maf of human origin
recommended for detection of c-Maf of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including bovine and avian
blocking peptide, sc-10017 P
TransCruz reagent for Gel Supershift and ChIP applications, sc-10017 X, 200 µg/0.1 ml
c-Maf Background Information Members of the Maf family of basic region/leucine zipper (bZIP) transcription factors affect transcription in either a positive or negative fashion, depending on their particular protein partner and the context of the target promoter. c-Maf (Maf-2) and the closely related family members, neural retina leucine zipper (Nrl), L-Maf and Krml1/MafB (Maf-1), all bind to T-MARE sites and have been implicated in a wide variety of developmental and physiologic roles. The three small Maf family proteins (MafF, MafG and MafK) are components of NF-E2 that function as heterodimers with the large tissue-restricted subunit of NF-E2, called p45, and they are implicated in the transcriptional regulation of many erythroid-specific genes. MafB is expressed in a wide variety of tissues and encodes a protein containing a typical bZIP motif in its carboxy-terminal region. As a transcriptional activator, MafB plays a pivotal role in regulating lineage-specific gene expression during hematopoiesis by repressing Ets-1-mediated transcription of key erythroid-specific genes in myeloid cells. c-Maf interacts with the c-Myb DNA binding domain and forms Myb-Maf complexes, which, in turn, mediate the cooperative interactions between c-Myb and Ets-1 during early myeloid cell differentiation.
c-Maf (N-15) Product Citations
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