mouse monoclonal IgG1; PLZF Antibody (D-9) is an IgG1 κ mouse monoclonal PLZF antibody (also designated ZBTB16 antibody, or ZNF145 antibody) that detects the PLZF protein of mouse, rat and human origin by WB, IP, IF, IHC(P) and ELISA. PLZF Antibody (D-9) is available as both the non-conjugated anti-PLZF antibody form, as well as multiple conjugated forms of anti-PLZF antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. 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). The expression of HIC-1 is also frequently suppressed in leu-kemia and other 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.