Rabbit polyclonal primary
DDIT4 Rabbit Polyclonal Antibody (ER1706-76)
Synthetic peptide within human ddit4 aa 183-232 / 232.
Hela and K562 cell lysates, rat epididymis tissue, human tonsil tissue, human colon cancer tissue, human breast tissue, mouse colon tissue, A549.
Store at +4C after thawing. Aliquot store at -20C or -80C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Peptide affinity purified
25 kDa (Predicted band size)
DDIT4 antibody; DDIT4_HUMAN antibody; Dig2 antibody; DNA damage inducible transcript 4 antibody; DNA damage inducible transcript 4 protein antibody; DNA damage-inducible transcript 4 protein antibody; FLJ20500 antibody; HIF 1 responsive protein RTP801 antibody; HIF 1 responsive RTP801 antibody; HIF-1 responsive protein RTP801 antibody; Protein regulated in development and DNA damage response 1 antibody; REDD-1 antibody; REDD1 antibody; RTP801 antibody
Belongs to the DDIT4 family.
Broadly expressed, with lowest levels in brain, skeletal muscle and intestine. Up-regulated in substantia nigra neurons from Parkinson disease patients (at protein level).
Phosphorylated by GSK3B; this promotes proteasomal degradation.; Polyubiquitinated by a DCX (DDB1-CUL4A-RBX1) E3 ubiquitin-protein ligase complex with BTRC as substrate-recognition component, leading to its proteasomal degradation.
REDD-1, also designated DNA-damage-inducible transcript 4, dig2 or RTP801, is thought to function in the regulation of reactive oxygen species (ROS). REDD-1 expression has also been linked to apoptosis, Ab toxicity and the pathogenesis of ischemic diseases. As an HIF-1-responsive gene, REDD-1 exhibits strong hypoxia-dependent upregulation in ischemic cells of neuronal origin. In response to stress due to DNA damage and glucocorticoid treatment, REDD-1 is upregulated at the transcriptional level. REDD-1 negatively regulates the mammalian target of Rapamycin (mTOR), a serine/threonine kinase often referred to as FRAP. It is crucial in the coupling of extra- and intracellular cues to FRAP regulation. The absence of REDD-1 is associated with the development of retinopathy, a major cause of blindness.