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About This Item
CAS Number:
UNSPSC Code:
12352204
NACRES:
NA.54
EC Number:
232-942-5
MDL number:
Specific activity:
10-40 units/mg protein (Bradford)
Product Name
Leucine Aminopeptidase, microsomal from porcine kidney, Type IV-S, ammonium sulfate suspension, 10-40 units/mg protein (Bradford)
type
Type IV-S
form
ammonium sulfate suspension
specific activity
10-40 units/mg protein (Bradford)
storage temp.
2-8°C
Quality Level
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Related Categories
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.
General description
Leucine Aminopeptidase belongs to the family of metalloprotease.
Other Notes
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
signalword
Danger
hcodes
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
target_organs
Respiratory system
Storage Class
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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)
Rossella Galati et al.
Zeitschrift fur Naturforschung. C, Journal of biosciences, 58(7-8), 558-561 (2003-08-27)
The ability of synthetic protein fragments to survive the degradative action of aminopeptidases and serum proteolytic enzymes can be remarkably enhanced by slight modifications at their N-terminal alpha-amino group. This can be achieved by addition of beta-alanine or amino acids
Intestinal digestive resistance of immunodominant gliadin peptides
Hausch F, et al.
American Journal of Physiology: Gastrointestinal and Liver Physiology, 283(4), G996-G1003 (2002)
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)
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)
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