Összes fotó(3)
Fontos dokumentumok
A8200
Aminopeptidase from Aeromonas proteolytica
lyophilized powder, 50-150 units/mg protein
Szinonimák:
AAP, Aminopeptidase from Vibrio proteolyticus, bacterial leucyl aminopeptidase
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(3)
About This Item
CAS-szám:
EC-szám:
MDL-szám:
UNSPSC kód:
12352204
NACRES:
NA.54
Javasolt termékek
grade
Proteomics Grade
Minőségi szint
form
lyophilized powder
specifikus aktivitás
50-150 units/mg protein
molekulatömeg
29.5 kDa
összetétel
Protein, ~40% biuret
oldhatóság
H2O: soluble 0.9-1.1 mg/mL, clear, colorless
idegen aktivitás
endopeptidase, essentially free
tárolási hőmérséklet
−20°C
Általános leírás
A zinc-containing enzyme.
Egyediség
Catalyzes the release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
Alkalmazás
Aminopeptidases are a family of widely distributed proteases, which may be used to study many significant biological processes such as protein maturation, hormone production, and peptide digestion. The enzyme has been used to measure the kinetic rate constant for the binding of bestatin, a general protease inhibitor, to aminopeptidase.
Biokémiai/fiziológiai hatások
Aminopeptidase from Aeromonas proteolytica is a metalloenzyme, which contains 2 atoms of Zn2+ in a single polypeptide with an approximate molecular weight of 29.5 kDa as determined by sedimentation. This enzyme has a high degree of stability, being stable even at temperatures of 70 °C for several hours. Partial inactivation occurs in 8 M urea. Maximum stability and activity are between pH 8.0-8.5. Aminopeptidase from Aeromonas proteolytica can function as an esterase.
Aminopeptidase from Aeromonas proteolytica is involved in protein maturation, hormone production and peptide digestion.
Egység definíció
One unit will hydrolyze 1.0 μmole of L-leucine p-nitroanilide to L-leucine and p-nitroaniline per min at pH 8.0 at 25 °C.
Fizikai forma
Lyophilized powder containing tricine buffer, pH 8.0, zinc chloride and stabilizer.
Elkészítési megjegyzés
Dissolves in water at 0.9-1.1 mg/mL concentration to form a clear, colorless solution.
Figyelmeztetés
Danger
Figyelmeztető mondatok
Óvintézkedésre vonatkozó mondatok
Veszélyességi osztályok
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Célzott szervek
Respiratory system
Tárolási osztály kódja
11 - Combustible Solids
WGK
WGK 1
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
Egyéni védőeszköz
Eyeshields, Gloves, type N95 (US)
Analitikai tanúsítványok (COA)
Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.
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Az ügyfelek ezeket is megtekintették
James Kahn et al.
Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular Biology, 38(4), 238-241 (2011-05-14)
We have recently designed a biochemistry laboratory experiment for the purpose of providing students an advanced experience with enzyme kinetics and the kinetics of binding. Bestatin, a well-known and commercially available general protease inhibitor, is a slow-binding inhibitor of aminopeptidase
G Van Heeke et al.
Biochimica et biophysica acta, 1131(3), 337-340 (1992-07-15)
The gene encoding the Vibrio proteolyticus aminopeptidase was cloned and sequenced and its amino acid sequence was deduced. The gene encodes a 54 kDa protein, larger than the previously reported size of 30 kDa for the purified aminopeptidase. Sequence alignments
L Ustynyuk et al.
Biochemistry, 38(35), 11433-11439 (1999-09-02)
Seven aliphatic and two aromatic alcohols were tested as reporters of the substrate selectivity of the aminopeptidase from Aeromonas proteolytica (AAP). This series of alcohols was chosen to systematically probe the effect of carbon chain length, steric bulk, and inhibitor
Gudrun Schürer et al.
Biochemistry, 43(18), 5414-5427 (2004-05-05)
The aminopeptidase of Aeromonas proteolytica (AAP) belongs to the group of metallo-hydrolases that require two divalent cations for full activity. Such binuclear metal centers are found in several aminopeptidases, raising the question whether a common mechanism, at least partly, is
Carin C Stamper et al.
Biochemistry, 43(30), 9620-9628 (2004-07-28)
Binding of the competitive, slow-binding inhibitor bestatin ([(2S,3R)-3-amino-2-hydroxy-4-phenylbutanoy]-leucine) to the aminopeptidase from Aeromonas proteolytica (AAP) was examined by both spectroscopic and crystallographic methods. Electronic absorption spectra of the catalytically competent [Co_(AAP)], [CoCo(AAP)], and [ZnCo(AAP)] enzymes recorded in the presence of
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