Abcam, ab234627, Leucine Aminopeptidase (LAP) Activity Assay Kit (Fluorometric)

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Leucine Aminopeptidase (LAP) Activity Assay Kit (Fluorometric) (ab234627) provides a quick, sensitive and easy way for measuring total LAP activity in various samples such as animal tissues or cell cultures. Individual kit components also available for purchase with a minimum order of 20 units. Contact us to discuss your needs.
Key facts
Detection method:Fluorescent,
Sample types:Suspension cells, Tissue Homogenate, Adherent cells,
Assay type:Enzyme activity,
Sensitivity:= 0.1 mU/well,
Assay Platform:Microplate reader

Product details:
Leucine Aminopeptidase (LAP) Activity Assay Kit (Fluorometric) (ab234627) provides a quick, sensitive and easy way for measuring total LAP activity in various samples such as animal tissues or cell cultures.
In this assay, LAPs hydrolyze leucine from the fluorescent probe and the amount of fluorescent probe detected at Ex/Em 368/460 nm is used to determine the total activity of the LAP enzymes. The assay is simple to perform, high-throughput adaptable and can detect less than 0.1 mU of LAP activity.
Other Notes
This product was previously called K534 Biovision Leucine Aminopeptidase (LAP) Activity Assay Kit (Fluorometric). Biovision was acquired by Abcam in 2021.
Leucine aminopeptidases (EC 3.4.11.1) (LAPs) are a diverse set of exopeptidases that catalyze the hydrolysis of leucine residues from the amino-termini of proteins or peptides. LAPs are ubiquitous enzymes present among animals, plants and prokaryotes. Previously, they were thought to typically play important roles in cell maintenance, growth and development. However, research in the recent years has identified multiple secondary functions for these enzymes in animals and microbes including transcriptional regulation and vesicle transport. Studies have implicated LAP enzymes in tumor cell proliferation, invasion and angiogenesis. Placental LAP is used as a biomarker in ovarian epithelial cancer while adipocyte-derived LAP is used as a marker of endometrial cancer cell proliferation and differentiation.
The Safety Datasheet for this product has been updated for certain countries. Please check the current version in the Support and downloads section.

Properties and Storage Information:
Shipped at conditions-Blue Ice, Appropriate short-term storage conditions--20°C, Appropriate long-term storage conditions--20°C, Storage information--20°C

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
Leucine Aminopeptidase (LAP) also known as aminopeptidase or aminopeptidase N is an enzyme that catalyzes the cleavage of amino acids from the N-terminus of peptide substrates. It has a molecular mass of around 100 kDa. LAP is expressed in many tissues including liver kidney and small intestine. It plays a significant enzymatic role in protein metabolism by regulating the availability of free amino acids which are important for various cellular processes.
Biological function summary
This enzyme is involved in several physiological processes beyond general protein metabolism. It participates in antigen processing and presentation which is important for immune response. LAP does not function within a large protein complex but works effectively as a monomer. Its enzymatic activity influences the regulation and modulation of key physiological activities by controlling the peptide and amino acid pools.
Pathways
LAP is a vital player in both the renin-angiotensin system and the gastrointestinal protein digestion pathway. In the renin-angiotensin system LAP regulates the levels of certain peptides which in turn contribute to blood pressure control. In protein digestion LAP aids in breaking down dietary proteins into amino acids for absorption. LAP's enzymatic activity impacts interactions with proteins like angiotensin-converting enzyme (ACE) and other peptidases.
LAP is linked to conditions such as hypertension and various types of cancers. Hypertension is associated with its activity in the renin-angiotensin system affecting blood pressure regulation. In cancers altered LAP activity can affect tumor progression and immune evasion. Additionally LAP works together with proteins like matrix metalloproteinases which are relevant in cancer metastasis. These associations make LAP a target of interest for therapeutics in related diseases.