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Merck
CN

L5006

Leucine Aminopeptidase, microsomal from porcine kidney

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

Synonym(s):

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

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About This Item

CAS Number:
9054-63-1
EC Number:
3.4.11.2 (BRENDA, IUBMB)
EC Number:
232-942-5
MDL number:
MFCD00131501
UNSPSC Code:
12352204
NACRES:
NA.54

Key Documents

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type

Type IV-S

Quality Level

200

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.

Physical form

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

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.

Pictograms

Health hazardExclamation mark
GHS08,GHS07

Signal Word

Danger

Hazard Statements

H315,H319,H334,H335

Hazard Classifications

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

Target Organs

Respiratory system

Storage Class Code

11 - Combustible Solids

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Personal Protective Equipment

dust mask type N95 (US), Eyeshields, Gloves

Regulatory Information

低风险生物材料
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Certificates of Analysis (COA)

Lot/Batch Number
0000398273
0000398272
0000363828
0000377176
0000353156

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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)
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)
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
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
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