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Involved in the metabolism of neuropeptides under 20 amino acid residues long.
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Data suggest that three new candidate genes involved in the development of rheumatoid arthritis (RA): ERBB2 (show ERBB2 ELISA Kits), TP53 (show TP53 ELISA Kits) and THOP1.
THOP1 may have clinical potentials to be employed as a promising biomarker to identify individuals with better prognosis and a novel antitumor agent for therapy of patients with NSCLC
Low THOP1 expression levels are associated with recurrence of hepatocellular carcinoma.
TCEP. Data indicate that THIMET-oligopeptidase (TOP) oxidation by H2O2 and high valence states of hemeproteins does not lead to enzyme oligomerization.
The semi-quantitative intracellular peptidome analyses of siRNA-transfected HEK293 cells shows that the levels of specific intracellular peptides are either increased or decreased upon EP24.15 inhibition.
human thimet oligopeptidase crystal structure shows substrate recognition, regulation, and localization
EP24.15 associates with AT1 (show AGTR1 ELISA Kits) and B2 receptors both at the plasma membrane and after receptor internalization
Mutations at only two residues (Glu-469 and Arg-498) are required to swap specificity with neurolysin, a result that is confirmed by testing the two-mutant constructs.
increase in THOP1 expression might be part of a compensatory defense mechanism of the brain against an increased Abeta (show APP ELISA Kits) load.
Over 100 peptides were identified in human embryonic kidney 293 (HEK293) cells that are derived from intracellular proteins; many but not all of these peptides are substrates or products of EP24.15.
the cellular peptidases dipeptidyl peptidase 3 (DPP-3 (show DPP3 ELISA Kits)) and thimet oligopeptidase 1 (TOP-1 (show TOP1 ELISA Kits)), both of which are present in nonimmunogenic necrotic cells, eliminated proteasomal degradation products and blocked Ag cross-presentation
Data show that Thimet oligopeptidase (TOP) is coexpressed with estrogen receptor alpha (show ESR1 ELISA Kits), and estradiol regulates TOP expression in a brain region-specific manner in female mice.
EP24.15 association with lipid rafts on the extracellular surface precedes constitutive release of the peptidase into the extracellular milieu for its action on neuropeptides
Melanoma cells secrete thimet oligopeptidase which have an important role in tumor proliferation/angiogenesis in vitro and in vivo.
Cyclic strain putatively regulates both the mRNA expression and enzymatic function of EP24.15 and EP24.16.
Involved in the metabolism of neuropeptides under 20 amino acid residues long. Involved in cytoplasmic peptide degradation. Able to degrade the beta-amyloid precursor protein and generate amyloidogenic fragments.
thimet oligopeptidase 1
, thimet oligopeptidase-like
, thimet oligopeptidase
, Thimet oligopeptidase
, endopeptidase 24.15
, endo-oligopeptidase A
, soluble metallo-endopeptidase
, endopeptidase EC18.104.22.168