Use your antibodies-online credentials, if available.
抗Human DDIT4 抗体:
抗Mouse (Murine) DDIT4 抗体:
抗Rat (Rattus) DDIT4 抗体:
Human Polyclonal DDIT4 Primary Antibody for ELISA, WB - ABIN1003102
Ellisen, Ramsayer, Johannessen, Yang, Beppu, Minda, Oliner, McKeon, Haber: REDD1, a developmentally regulated transcriptional target of p63 and p53, links p63 to regulation of reactive oxygen species. in Molecular cell 2002
Show all 4 Pubmed References
Human Polyclonal DDIT4 Primary Antibody for IHC, ELISA - ABIN1003101
Shoshani, Faerman, Mett, Zelin, Tenne, Gorodin, Moshel, Elbaz, Budanov, Chajut, Kalinski, Kamer, Rozen, Mor, Keshet, Leshkowitz, Einat, Skaliter, Feinstein: Identification of a novel hypoxia-inducible factor 1-responsive gene, RTP801, involved in apoptosis. in Molecular and cellular biology 2002
Show all 4 Pubmed References
Human Polyclonal DDIT4 Primary Antibody for IHC (p), WB - ABIN541689
Sofer, Lei, Johannessen, Ellisen: Regulation of mTOR and cell growth in response to energy stress by REDD1. in Molecular and cellular biology 2005
Show all 4 Pubmed References
Human Polyclonal DDIT4 Primary Antibody for WB - ABIN541692
Seimetz, Parajuli, Pichl, Veit, Kwapiszewska, Weisel, Milger, Egemnazarov, Turowska, Fuchs, Nikam, Roth, Sydykov, Medebach, Klepetko, Jaksch, Dumitrascu, Garn, Voswinckel, Kostin, Seeger, Schermuly et al.: Inducible NOS inhibition reverses tobacco-smoke-induced emphysema and pulmonary hypertension in mice. ... in Cell 2011
Show all 4 Pubmed References
Human Polyclonal DDIT4 Primary Antibody for ICC, IF - ABIN439647
Potts, McMillan, Rosales, Kim, Ou, Toombs, Brekken, Minden, MacMillan, White: Mode of action and pharmacogenomic biomarkers for exceptional responders to didemnin B. in Nature chemical biology 2015
Show all 2 Pubmed References
Human Polyclonal DDIT4 Primary Antibody for ICC, IF - ABIN4304577
Stadler, Rexhepaj, Singan, Murphy, Pepperkok, Uhlén, Simpson, Lundberg: Immunofluorescence and fluorescent-protein tagging show high correlation for protein localization in mammalian cells. in Nature methods 2013
Human Polyclonal DDIT4 Primary Antibody for ELISA, IHC - ABIN4304576
Chen, Ma, Zhuo, Zhang, Zou, Yang, Gao, Li: 1,25-Dihydroxyvitamin D3 inhibits the proliferation of rat mesangial cells induced by high glucose via DDIT4. in Oncotarget 2018
REDD1 expression, as a mediator linking inflammation, autophagy, and NET release, was also specifically associated with the inflammatory response of UC.
REDD1 is an independent unfavorable prognostic factor in ovarian carcinoma and may promote ovarian cancer metastasis.
These findings indicate that miR221 might play an important role in human placental development by precisely regulating the DDIT4 expression.
Data show that DNA damage-inducible transcript 4 (DDIT4) was upregulated in gastric cancer (GC) cells and tissue, and that the mitogen-activated protein kinase and p53 signaling pathways were involved in the suppression of proliferation.
Silencing lncDDIT4 in naive CD4(+) T cells enhanced Th17 differentiation through increased activation of the DDIT4/mTOR pathway.
DDIT4 might serve as a novel prognostic biomarker in several malignancies.
Cellular metabolism constrains innate immune responses in preterm infants due to perturbations in the expression of PPARgamma, MALT1, DDIT4, and most of the cytokines.
these findings uncover a novel mechanism by which PML loss may contribute to mTOR activation and cancer progression via dysregulation of basal DDIT4 gene expression.
A microarray analysis revealed that in A3G-transduced Vero cells, several cellular transcripts were differentially expressed, suggesting that A3G regulates the expression of host factors. One of the most upregulated host cell factors, REDD1 (regulated in development and DNA damage response-1, also called DDIT4), reduced MV replication approximately 10-fold upon overexpression in Vero cells.
This is concurrent with an increase in the expression level of DDIT4, which is an inhibitor of the mammalian target of rapamycin (mTOR) signaling pathway. these results provided a novel insight on miR1243p involvement in the biological alterations of male patients with major depressive disorder and suggested that this miRNA may also serve as a malespeci fi c target for antidepressant treatment
DDIT4 activity is directly linked to regulation of mTOR signalling
The HIF-1alpha-REDD1-mTOR pathway was involved in the response to hypoxia in BeWo cells. Hypoxia-induced REDD1 upregulation is mediated by a HIF-1alpha-dependent pathway. Disruption of REDD1 blocked the effects of hypoxia on suppressing mTOR and resulted in additional accumulation of HIF-1alpha in BeWo cells.
REDD1 is overexpressed during Familial Mediterranean fever inflammatory attacks induced by physical or psychological stress
Expression of key autophagy markers (microtubule-associated protein 1A/1B light chain 3 and autophagy protein 5) was markedly reduced in cultured human chondrocytes with REDD1 depletion.
The production of superoxide anion in nockout-Rtp801 mouse lung fibroblasts (MLF) was lower than that in Rtp801 Wt cells after cigarette smoke extract treatment, and it was inhibited in Wt MLF by silencing nicotinamide adenine dinucleotide phosphate oxidase-4 (Nox4) expression with small interfering Nox4 RNA.
Changes in REDD1 mRNA and protein have been observed in skeletal muscle under various physiological conditions (e.g., nutrient consumption and resistance exercise) and pathological conditions (e.g., sepsis, alcoholism, diabetes, obesity) suggesting a role for REDD1 in regulating mTORC1-dependent skeletal muscle protein metabolism. [Review]
a novel STAT3-dependent mechanism of both IL-6-induced activation of mTOR and IL-6-dependent reversion of stress-induced inhibition of mTOR activity, is reported.
findings implicate REDD1 as a crucial regulator of mTORC1 activity in iron-depleted cells
C/EBPbeta promotes autophagy in PC3 cells by augmenting REDD1 expression.
These data highlight the central role of REDD1 in regulating both protein synthesis and autophagy in skeletal muscle during sepsis.
REDD1 is a crucial negative regulator of energy expenditure that is necessary for muscle adaptation during energetic stresses.
Altogether, REDD1 appears to be a key player in the control of inflammation.
REDD-1 exacerbates endotoxemic inflammation via atypical NF-kappaB activation.
RTP801 plays a essential role in the progression of restraint stress induced neurodegenerative disease.
Findings suggest that REDD1 in cacna1c heterozygous mice may influence depression-related behavior via regulation of the FoxO3a pathway. Study identified the prefrontal cortex as a key brain region in which cacna1c mechanisms through previously unidentified, novel molecular pathways contribute to depression-related behavior.
Diabetic wild-type mice exhibited functional deficiencies in visual acuity and contrast sensitivity, whereas diabetic REDD1-deficient mice had no visual dysfunction. The results support a role for REDD1 in diabetes-induced retinal neurodegeneration.
these data show that REDD1 induction regulates the exercise-mediated change in a distinct set of genes within skeletal muscle.
Findings suggest that REDD1 is a key mediator of cartilage homeostasis through regulation of autophagy and mitochondrial biogenesis and that REDD1 deficiency exacerbates the severity of injury-induced osteoarthritis.
These data suggest that loss of REDD1 augments the rate of the OV-induced increase in muscle mass by altering multiple protein balance pathways.
REDD1 is required for normal insulin-stimulated signaling, and a subtle balance exists between MEK1/2, REDD1, and mTOR
study suggests that VDR regulates Ddit4 expression during epidermal homeostasis and the wound healing process, while elevated Ddit4 represents an early growth-arresting stress response within VDR(-/-) follicles.
REDD1 knockout T cells exhibit a defect in proliferation and cell survival, although markers of activation appear normal. These findings demonstrate a previously unappreciated role for REDD1 in T cell function.
Reactive oxygen species regulation through REDD1/TXNIP is physiological rheostat controlling stress-induced autophagy.
LPS induces REDD1 expression by two distinct CREB-mediated mechanisms
Glucocorticoids induce skin atrophy and activate REDD1 expression.
REDD1 expression limits the nutrient-induced stimulation of protein synthesis and activation of mTORC1 signaling during periods of feed deprivation.
REDD1 is necessary for hyperglycemia mediated effects on VEGF expression in the retina of diabetic mice.
These data suggest that epithelial mTORC1 activity plays a protective role against lung injury, and its inhibition by Rtp801 exacerbates alveolar injury caused by endotoxin.
The REDD1 KO mouse muscle displayed blunted mTORC1 signaling responses.
Redd1 alters dorsoventral patterning by antagonizing the Wnt/beta-catenin signaling pathway.
HIF-1-responsive gene that may protect some types of cells from hypoxia and H(2)O(2)-triggered apoptosis
DNA damage-inducible transcript 4 protein
, DNA-damage-inducible transcript 4 protein
, protein regulated in development and DNA damage response 1
, DNA-damage-inducible transcript 4
, HIF-1 responsive protein RTP801
, HIF-1 responsive RTP801
, dexamethasone-induced gene 2 protein
, regulated in development and DNA damage response 1