Skip to Content
Merck
All Photos(1)

Key Documents

View All Documentation

Safety Information

L6007

Sigma-Aldrich

Leucine Aminopeptidase, microsomal from porcine kidney

Type VI-S, lyophilized powder, ≥12 units/mg protein (biuret)

Synonym(s):

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

Sign Into View Organizational & Contract Pricing
All Photos(1)

About This Item

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

biological source

Porcine kidney

type

Type VI-S

form

lyophilized powder

specific activity

≥12 units/mg protein (biuret)

mol wt

320 kDa

composition

Protein, 30-70%

storage temp.

−20°C

Looking for similar products? Visit Product Comparison Guide

General description

Leucine Aminopeptidase (LAP) from porcine is a 320-kDa exopeptidase present in cytosol. It contains zinc in its structure and belongs to the M1 and M17 peptidase families. LAP display bi-lobed structure and has the catalytic domain at the C-terminus and a variable N-terminal domain.

Application

Leucine Aminopeptidase, microsomal from porcine kidney has been used in aminopeptidase N (APN) inhibitor screening assay in adenocarcinoma cell line ES-2 and in the inhibition kinetic studies with APN inhibitor.

Biochem/physiol Actions

Leucine Aminopeptidase (LAP) catalyzes protein hydrolysis at the leucine residue at N-terminal. An altered level of LAP is implicated in tumor proliferation and progression. LAP is a potential biomarker for ovarian epithelial cancer therapy. Porcine LAP hydrolyzes glycine and arginine substrates.

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

Contains primarily phosphate buffer salts, pH 7.0

inhibitor

Product No.
Description
Pricing

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 Listings

Regulatory Listings are mainly provided for chemical products. Only limited information can be provided here for non-chemical products. No entry means none of the components are listed. It is the user’s obligation to ensure the safe and legal use of the product.

JAN Code

L6007-BULK:
L6007-50UN:
L6007-VAR:
L6007-25UN:
L6007-100UN:

Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Novel and highly sensitive fluorescent assay for leucine aminopeptidases
Huang H, et al.
Analytical biochemistry, 391(1), 11-16 (2009)
Leucine aminopeptidases: diversity in structure and function
Matsui M, et al.
Biological Chemistry, 387(12), 1535-1544 (2006)
The effect of different species Aminopeptidase N Structure on the activity screening of Aminopeptidase N Inhibitor
Wang X, et al.
Biological & Pharmaceutical Bulletin, 33(10), 1658-1665 (2010)
Activity screening and structure-activity relationship of the hit compounds targeting APN/CD13
Wang X, et al.
Fundamental & Clinical Pharmacology, 25(2), 217-228 (2011)
Refolding of hexameric porcine leucine aminopeptidase using a cationic detergent and dextrin-10 as artificial chaperones
Laslo AC, et al.
Journal of Biotechnology, 140(3-4), 162-168 (2009)
View All Related Papers

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service