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anti-Human NRD1 Antibodies:
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NRDC expression was reduced in infarcted regions in autopsy samples from acute myocardial ischemia patients.
Gene expression level of NRD1 is significantly higher in AD patients when compared to normal controls.
MRNA expression of NRD1 was upregulated in 56% of ESCC tissue samples.
This study demonistrated that alcohol-dependent reduction of nardilysin in cell culture and nervous tissue points to an implication of the enzyme in the pathophysiology of alcoholism.
possible roles of nardilysin in Alzheimer disease, Down syndrome, schizophrenia, mood disorders, alcohol abuse, heroin addiction and cancer; show that nardilysin is a Janus-faced enzyme with regard to brain pathology-- probably neuropathogenic in some diseases, but neuroprotective in others [review]
SH-SY5Y cells, stably transfected with green fluorescent protein-tagged-p42(IP4) show enhanced NRD protein expression already at an earlier time point after retinoic acid stimulation.
NRD1 interacts with p53 mutant R273H
These results demonstrate that gastric cancer cell growth is maintained by autonomous TNF-alpha-NF-kappaB and IL-6-STAT3 signalling, and that NRDc and ADAM proteases turn on these signalling cascades by stimulating ectodomain shedding of TNF-alpha.
Identification and characterization of nardilysin as a novel dimethyl H3K4-binding protein involved in transcriptional regulation.
Several flanking SNPs of the top hits in the meta-analysis demonstrated borderline associations with alcohol dependence in the family sample for KIAA0040, NRD1 and THSD7B, respectively.
Tubulin potentiates the interaction of the metalloendopeptidase nardilysin with the neuronal scaffold protein p42IP4/centaurin-alpha1 (ADAP1).
mediates antigen processing that generates cytotoxic T cell epitopes
nardilysin (NRDc) is potently inhibited by heparin-binding epidermal growth factor-like growth factor (HB-EGF)
Nardilysin has an essential role in HB-EGF ectodomain shedding, which is regulated by the modulation of sheddase activity
We found high staining intensity in the hypothalamus, neocortex and brain stem nuclei. The cellular localization is almost exclusively confined to neurons. In pre- and perinatal human brain cortex, most neurons express the enzyme.
These results indicate the involvement of NRDc in ectodomain shedding of TNF-alpha.
Nardilysin convertase regulates the function of the maxi-K channel isoform mK44 in human myometrium.
N-arginine dibasic convertase is a specific receptor for heparin-binding EGF-like growth factor (HB-EGF) that modulates HB-EGF-induced cell migration.
The acidic stretch of nardilysin, expressed as a fusion protein with glutathione S-transferase and compared to the native enzyme with respect to spermine binding, functions as an autonomous domain.
Here, the authors have demonstrated that nardilysin regulates gastric inflammation caused by Helicobacter felis infection or forced expression of prostaglandin. Metaplastic changes following gastric inflammation were suppressed by the deletion of nardilysin. Furthremore, the deletion of nardilysin significantly suppressed N-methyl-N-nitrosourea (MNU)-induced gastric tumorigenesis in the murine stomach.
Nardilysin Is Required for Maintaining Pancreatic beta-Cell Function
critical regulator of body temperature homoeostasis
deletion of nardilysin prevents the development of diet-induced steatohepatitis and liver fibrogenesis
It controls Amyloid beta plaque formation through the regulation of a-secretase.
It plays a critical role in axonal maturation and myelination. (review)
The use of proteolysis to study the structure of nardilysin.
Studies extend the range of potential substrates for nardilysin and further substantiate that nardilysin is a true peptidase.
miniglucagon-generating endopeptidase is composed of NRDc and aminopeptidase B acting sequentially
role for nardilysin in oocyte meiosis through its dynamic translocation from cytosol to nucleus, and then to the spindle apparatus
NRDc regulates axonal maturation and myelination in the nervous system, in part, through the modulation of NRG1 shedding
This gene encodes a zinc-dependent endopeptidase that cleaves peptide substrates at the N-terminus of arginine residues in dibasic moieties and is a member of the peptidase M16 family. This protein interacts with heparin-binding EGF-like growth factor and plays a role in cell migration and proliferation. Multiple transcript variants encoding different isoforms have been found for this gene.
, N-arginine dibasic convertase 1
, nardilysin 1 (N-arginine dibasic convertase)
, nardilysin, N-arginine dibasic convertase 1
, nardilysin, N-arginine dibasic convertase, NRD convertase 1
, N-arginine dibasic convertase
, nardilysin (N-arginine dibasic convertase)
, Nardilysin-like protein