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Merck

L5006

Sigma-Aldrich

Leucine Aminopeptidase, microsomal from porcine kidney

Type IV-S, ammonium sulfate suspension, 10-40 units/mg protein (Bradford)

Sinónimos:

Aminopeptidase M, Aminopeptidase N, Cathepsin III, LAP, Leucinamide aminopeptidase, Leucinaminopeptidase

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About This Item

Número de CAS:
Comisión internacional de enzimas:
EC Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54

type

Type IV-S

Quality Level

form

ammonium sulfate suspension

specific activity

10-40 units/mg protein (Bradford)

storage temp.

2-8°C

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General description

Leucine Aminopeptidase belongs to the family of metalloprotease.

Application

Leucine Aminopeptidase, microsomal from porcine kidney has been used in the isolation of neprilysin (NEP) from rodent brain-C5 and for peptide digestion.

Biochem/physiol Actions

Leucine Aminopeptidase possesses broad substrate-specificity. It hydrolyzes peptides up to the proline residue and does not continue to degrade beyond proline.

Unit Definition

One unit will hydrolyze 1.0 μmole of L-leucine-p-nitroanilide to L-leucine and p-nitroaniline per min at pH 7.2 at 37 °C. (At 25 °C, approx. 40% of the activity at 37 °C is obtained.) The activity obtained using L-leucine p-nitroanilide as substrate is 2-5 times that obtained with L-leucinamide as substrate.

Physical form

Suspension in 3.5 M (NH4)2SO4 solution, pH 7.7, containing 10 mM MgCl2

Inhibitor

Referencia del producto
Descripción
Precios

pictograms

Health hazardExclamation mark

signalword

Danger

Hazard Classifications

Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3

target_organs

Respiratory system

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)


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Biochemical identification of the neutral endopeptidase family member responsible for the catabolism of amyloid beta peptide in the brain
Takaki Y, et al.
The Journal of Biological Chemistry, 128(6), 897-902 (2000)
Intestinal digestive resistance of immunodominant gliadin peptides
Hausch F, et al.
American Journal of Physiology: Gastrointestinal and Liver Physiology, 283(4), G996-G1003 (2002)
The most potent organophosphorus inhibitors of leucine aminopeptidase. Structure-based design, chemistry, and activity
Grembecka J, et al.
Journal of medicinal chemistry, 46(13), 2641-2655 (2003)
Debittering of a Tryptic Digest of Bovine p-casein Using Porcine Kidney General Aminopeptidase and X-Prolydipeptidyl Aminopeptidase from Lactococcus lactis subsp. cremoris AM2
Barry CM, et al.
Journal of Food Science, 65(7), 1145-1150 (2000)
Sylvain Debieu et al.
Organic & biomolecular chemistry, 15(12), 2575-2584 (2017-03-08)
We report a reaction-based strategy for the fluorogenic detection of protease activity. Based on the "covalent-assembly" probe design principle recently put forward by the Yang group for detection of Sarin related threats (J. Am. Chem. Soc., 2014, 136, 6594-6597), we

Artículos

Instructions for working with enzymes supplied as ammonium sulfate suspensions

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