L1635
L-Leucine β-naphthylamide
Sinonimo/i:
L-Leucine-2-naphthylamide
Autenticatiper visualizzare i prezzi riservati alla tua organizzazione & contrattuali
Scegli un formato
100 MG
CHF 54.20
1 G
CHF 183.00
CHF 54.20
Check Cart for Availability
Scegli un formato
Cambia visualizzazione
100 MG
CHF 54.20
1 G
CHF 183.00
About This Item
Formula empirica (notazione di Hill):
C16H20N2O
Numero CAS:
Peso molecolare:
256.34
Numero CE:
Numero MDL:
Codice UNSPSC:
12352204
ID PubChem:
NACRES:
NA.83
CHF 54.20
Check Cart for Availability
Prodotti consigliati
Saggio
≥98% (TLC)
Livello qualitativo
Stato
powder
Solubilità
H2O: insoluble
Temperatura di conservazione
−20°C
Stringa SMILE
CC(C)C[C@H](N)C(=O)Nc1ccc2ccccc2c1
InChI
1S/C16H20N2O/c1-11(2)9-15(17)16(19)18-14-8-7-12-5-3-4-6-13(12)10-14/h3-8,10-11,15H,9,17H2,1-2H3,(H,18,19)/t15-/m0/s1
JWHURRLUBVMKOT-HNNXBMFYSA-N
Cerchi prodotti simili? Visita Guida al confronto tra prodotti
Applicazioni
L-Leucine β-naphthylamide has been used as a substrate:
- to measure the activity of aminopeptidase in Escherichia coli[1]
- to evaluate the enzyme activity of cathepsin H from rabbit skeletal muscles[2]
- in the proteolytic assay of L-Leucine aminopeptidase[3]
Substrate for leucine aminopeptidase determination in colorimetric and histochemical procedures.
Confezionamento
Bottomless glass bottle. Contents are inside inserted fused cone.
Qualità
Very low free β-naphthylamine.
Substrati
Substrate for aminopeptidase M
Avvertenze
Warning
Indicazioni di pericolo
Consigli di prudenza
Classi di pericolo
Carc. 2
Codice della classe di stoccaggio
11 - Combustible Solids
Classe di pericolosità dell'acqua (WGK)
WGK 3
Punto d’infiammabilità (°F)
Not applicable
Punto d’infiammabilità (°C)
Not applicable
Dispositivi di protezione individuale
Eyeshields, Gloves, type P3 (EN 143) respirator cartridges
Scegli una delle versioni più recenti:
Possiedi già questo prodotto?
I documenti relativi ai prodotti acquistati recentemente sono disponibili nell’Archivio dei documenti.
I clienti hanno visto anche
A M Reisenauer et al.
Science (New York, N.Y.), 227(4682), 70-72 (1985-01-04)
The regulation of amino-oligopeptidase (AOP), an intestinal brush border hydrolase essential for the surface digestion of peptide nutrients, was examined in rats in vivo. Short-term (30-minute) intraintestinal perfusion of a tetrapeptide substrate, Gly-Leu-Gly-Gly, or a synthetic substrate, leucyl-beta-naphthylamide, induced a
T Nishimura et al.
European journal of biochemistry, 137(1-2), 23-27 (1983-12-01)
The mode of action towards oligopeptides and proteins of hydrolase H purified from rabbit skeletal muscle was studied. The presence of protamine or alpha-N-benzoylarginine p-nitroanilide (an endopeptidase substrate) changed both the Km and V values of the enzyme towards Leu-beta-naphthylamide
F Marciano-Cabral et al.
The Journal of protozoology, 34(2), 146-149 (1987-05-01)
An intracellular alpha-aminoacyl-peptide hydrolase (EC 3.4.11.-) from Naegleria fowleri nN68 (ATCC 30894) has been characterized. The enzyme preparation hydrolyzed phenylalanyl-, tyrosyl-, leucyl-, arginyl-, alanyl-, tryptophanyl-, histidyl-, methionyl-, and lysyl-naphthylamide but not benzoylleucyl-, leucylglycyl-, glycylprolylleucyl-, glycyl-, threonyl-, aspartyl-, or glutamyl-naphthylamide. The
Proteolytic activity in the placenta, decidua and postimplantation embryos of the rat.
A Fein et al.
Israel journal of medical sciences, 21(4), 394-396 (1985-04-01)
Masanori Matsuishi et al.
The international journal of biochemistry & cell biology, 35(4), 474-485 (2003-02-05)
Rabbit muscle cathepsin H classified as an aminoendopeptidase was purified and its properties were investigated to clarify its contribution to the proteolysis of postmortem muscle. The purification was performed by ammonium sulfate fractionation and successive chromatographies on Sephadex G-75, phosphocelluose
Active Filters
Il team dei nostri ricercatori vanta grande esperienza in tutte le aree della ricerca quali Life Science, scienza dei materiali, sintesi chimica, cromatografia, discipline analitiche, ecc..
Contatta l'Assistenza Tecnica.
