Ubenimex
Ubenimex structure
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Common Name | Ubenimex | ||
|---|---|---|---|---|
| CAS Number | 58970-76-6 | Molecular Weight | 308.373 | |
| Density | 1.2±0.1 g/cm3 | Boiling Point | 604.7±55.0 °C at 760 mmHg | |
| Molecular Formula | C16H24N2O4 | Melting Point | 245 °C (dec.)(lit.) | |
| MSDS | Chinese USA | Flash Point | 319.5±31.5 °C | |
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Elastase and tryptase govern TNFα-mediated production of active chemerin by adipocytes.
PLoS ONE 7(12) , e51072, (2012) Chemerin is a leukocyte chemoattractant and adipokine with important immune and metabolic roles. Chemerin, secreted in an inactive form prochemerin, undergoes C-terminal proteolytic cleavage to generate active chemerin, a ligand for the chemokine-like recepto... |
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Gingipain aminopeptidase activities in Porphyromonas gingivalis.
Biol. Chem. 393(12) , 1471-6, (2012) Bestatin, a specific inhibitor of metalloaminopeptidases,inhibits the growth of Porphyromonas gingivalis. To identify its target enzyme, a library of fluorescent substrates was used but no metalloaminopeptidase activity was found. The aminopeptidase activity ... |
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Preparation and evaluation of a new releasable PEGylated tumor necrosis factor-α (TNF-α) conjugate for therapeutic application.
Sci. China Life Sci. 56(1) , 51-8, (2013) To design a releasable PEGylated TNF-α (rPEG-TNF-α), a cathepsin B-sensitive dipeptide (Val-Cit moiety) was inserted into conventional PEG-modified TNF-α (PEG-TNF-α), facilitating its clinical use for anti-tumor therapy. Comparative pharmacokinetic and pharma... |
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The effects of bestatin on humoral response to sheep erythrocytes in non-treated and cyclophosphamide-immunocompromised mice.
Immunopharmacol. Immunotoxicol. 35(1) , 133-8, (2013) The effects of bestatin on humoral immune response to sheep erythrocytes (SRBC) and restoration of the response impaired by a single cyclophosphamide dose (350 mg/kg) were tested on mice. Bestatin (at doses of 10, 1, and 0.1 mg/kg) was administered intraperit... |
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The X-ray crystal structure of human aminopeptidase N reveals a novel dimer and the basis for peptide processing.
J. Biol. Chem. 287(44) , 36804-13, (2012) Human aminopeptidase N (hAPN/hCD13) is a dimeric membrane protein and a member of the M1 family of zinc metallopeptidases. Within the rennin-angiotensin system, its enzymatic activity is responsible for processing peptide hormones angiotensin III and IV. In a... |
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Pain inhibition by blocking leukocytic and neuronal opioid peptidases in peripheral inflamed tissue.
FASEB J. 26(12) , 5161-71, (2012) Inflammatory pain can be controlled by endogenous opioid peptides. Here we blocked the degradation of opioids in peripheral injured tissue to locally augment this physiological system. In rats with hindpaw inflammation, inhibitors of aminopeptidase N (APN; be... |
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Synthesis of a novel series of L-isoserine derivatives as aminopeptidase N inhibitors.
J. Enzyme Inhib. Med. Chem. 27(2) , 302-10, (2012) A series of novel L-isoserine derivatives were synthesised and evaluated for their ability to inhibit aminopeptidase N (APN)/CD13. In our preliminary biological results, some of these compounds possessed a potent inhibitory activity against the APN. Within th... |
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Purification and characterization of porcine skeletal muscle aminopeptidase T, a novel metallopeptidase homologous to leukotriene A4 hydrolase.
Biosci. Biotechnol. Biochem. 75(6) , 1154-9, (2011) A novel aminopeptidase, Aminopeptidase T (APase T), was purified from porcine skeletal muscle following successive column chromatography: twice on DEAE-cellulose, hydroxyapatite, and Sephacryl S-200 HR using Leu-β-naphthylamide (LeuNap) as a substrate. The mo... |
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Comparative biochemical and functional properties of two leucine aminopeptidases of Clonorchis sinensis.
Mol. Biochem. Parasitol. 182(1-2) , 17-26, (2012) Leucine aminopeptidases (LAP; EC 3.4.11.1) are a group of metalloexopeptidases, which catalyze the sequential removal of leucine amino acids from the N-termini of the polypeptides or proteins. In this study, we identified two novel genes that encode LAPs of C... |
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Design, synthesis and preliminary activity evaluation of novel 3-amino-2-hydroxyl-3-phenylpropanoic acid derivatives as aminopeptidase N/CD13 inhibitors.
J. Enzyme Inhib. Med. Chem. 28(3) , 545-51, (2013) Aminopeptidase N (APN/CD13) over expressed on tumour cells, plays a critical role in tumour invasion, metastasis and tumour angiogenesis. In this article, we described the design, synthesis and preliminary activity studies of novel 3-amino-2-hydroxyl-3-phenyl... |