Use your antibodies-online credentials, if available.
Keine Produkte auf Ihrer Vergleichsliste.
Ihr Warenkorb ist leer.
The protein encoded by DNPEP is an aminopeptidase which prefers acidic amino acids, and specifically favors aspartic acid over glutamic acid.
Showing 3 out of 3 products:
aspartyl aminopeptidase was upregulated in colorectal cancer tissues, and greater activity correlated significantly with the absence of lymph node metastases and with better overall survival
The crystal structure of human DNPEP complexed with zinc and a substrate analogue aspartate-beta-hydroxamate reveals a dodecameric machinery built by domain-swapped dimers.
Identification of histidine residues important in the catalysis and structure of aspartyl aminopeptidase
Study shows that in the absence of aspartyl aminopeptidase (DNPEP), the kidney lysates retain their ability to cleave STE20 (zeige STK24 ELISA Kits)/SPS1-related proline/alanine-rich kinase(SPAK (zeige STK39 ELISA Kits)), indicating that DNPEP might have been misidentified as the protease behind the kidney lysate activity, or that the aspartyl aminopeptidase might not be the only protease cleaving SPAK (zeige STK39 ELISA Kits) in kidney.
Results demonstrate that Mir140 is essential for normal endochondral bone development and suggest that the reduced BMP signaling caused by Dnpep upregulation plays a causal role in the skeletal defects of Mir140-null mice.
DNPEP assembles into a functionally relevant tetrahedral complex that restricts access of peptide substrates to the active site.
The protein encoded by this gene is an aminopeptidase which prefers acidic amino acids, and specifically favors aspartic acid over glutamic acid. It is thought to be a cytosolic protein involved in general metabolism of intracellular proteins.
, Aspartyl aminopeptidase