L6007
Leucine Aminopeptidase, microsomal from porcine kidney
Type VI-S, lyophilized powder, ≥12 units/mg protein (biuret)
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biological source
Porcine kidney
Quality Level
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
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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
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Eye Irrit. 2 - Resp. Sens. 1 - Skin Irrit. 2 - STOT SE 3
Target Organs
Respiratory system
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
动植物源性产品
Certificates of Analysis (COA)
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Novel and highly sensitive fluorescent assay for leucine aminopeptidases
Huang H, et al.
Analytical biochemistry, 391(1), 11-16 (2009)
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)
Leucine aminopeptidases: diversity in structure and function
Matsui M, et al.
Biological Chemistry, 387(12), 1535-1544 (2006)
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)
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)
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