Anti-ID2 Antibody Picoband® Fluoro647 Conjugated

DNA-binding protein inhibitor ID-2 is a protein that in humans is encoded by the ID2 gene. The protein encoded by this gene belongs to the inhibitor of DNA binding family, members of which are transcriptional regulators that contain a helix-loop-helix (HLH) domain but not a basic domain. Members of the inhibitor of DNA binding family inhibit the functions of basic helix-loop-helix transcription factors in a dominant-negative manner by suppressing their heterodimerization partners through the HLH domains. This protein may play a role in negatively regulating cell differentiation. A pseudogene of this gene is located on chromosome 3.

DNA-binding protein inhibitor ID-2; Class B basic helix-loop-helix protein 26; bHLHb26; Inhibitor of DNA binding 2; Inhibitor of differentiation 2; ID2; BHLHB26

A synthetic peptide corresponding to a sequence at the C-terminus of human ID2, identical to the related mouse sequence, and different from the related rat sequence by one amino acid.

Transcriptional regulator (lacking a basic DNA binding domain) which negatively regulates the basic helix-loop-helix (bHLH) transcription factors by forming heterodimers and inhibiting their DNA binding and transcriptional activity. Implicated in regulating a variety of cellular processes, including cellular growth, senescence, differentiation, apoptosis, angiogenesis, and neoplastic transformation. Inhibits skeletal muscle and cardiac myocyte differentiation. Regulates the circadian clock by repressing the transcriptional activator activity of the CLOCK-ARNTL/BMAL1 heterodimer. Restricts the CLOCK and ARNTL/BMAL1 localization to the cytoplasm. Plays a role in both the input and output pathways of the circadian clock: in the input component, is involved in modulating the magnitude of photic entrainment and in the output component, contributes to the regulation of a variety of liver clock-controlled genes involved in lipid metabolism. .

1. Langlands K, Yin X, Anand G, Prochownik EV (Aug 1997) . Differential interactions of Id proteins with basic-helix-loop-helix transcription factors. J. Biol. Chem. 272 (32) : 19785–93. 2. Law SF, Zhang YZ, Fashena SJ, Toby G, Estojak J, Golemis EA (Oct 1999) . Dimerization of the docking/adaptor protein HEF1 via a carboxy-terminal helix-loop-helix domain. Exp. Cell Res. 252 (1) : 224–35.