epitope mapping at the N-terminus of HIC-1 of human origin
recommended for detection of HIC-1 of mouse, rat and human origin by WB, IF and ELISA; also reactive with additional species, including canine and porcine
blocking peptide, sc-10317 P
TransCruz reagent for Gel Supershift and ChIP applications, sc-10317 X, 200 µg/0.1 ml
HIC-1 Background Information Hypermethylated in cancer (HIC-1) was originally identified as a target of p53-induced gene expression. HIC-1 is deleted in the genetic disorder Miller-Dieker syndrome (MDS), and the expression of HIC-1 is also frequently suppressed in leukemia and various cancers due to the hypermethylation of specific DNA regions and the resulting transcriptional silencing. These and other studies indicate that HIC-1 acts as a putative tumor suppressor protein that mediates transcriptional repression . HIC-1 is ubiquitously expressed in adult tissues and its structure is defined by five zinc fingers and an N-terminal broad complex POZ (or BTB) domain. The BTB/POZ domain mediates homomeric and heteromeric POZ-POZ interactions and is common to transcriptional regulators involved in chromatin modeling. In several BTB/POZ containing proteins, including BCL-6 and the promyelocytic leukemia zinc-finger (PLZF) oncoprotein, this domain interacts with the SMRT/N-CoR-mSin3A HDAC complex and is directly involved in repressing and silencing gene transcription. When this domain is deleted, as with the oncogenic PLZF-RAR chimera of promyelocytic leukemias, this transcriptional repression is attenuated. Conversely, HIC-1 does not interact with components of the HDAC complex, suggesting that HIC-1-induced transcriptional repression is unassociated with the POZ/BTB domain.
HIC-1 (N-19)
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HIC-1 (N-19): sc-10317. Western blot analysis of HIC-1 expression in KNRK whole cell lysate.