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AB202613

Recombinant Human LAP3 protein (His tag N-Terminus)

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(1 Publication)

Recombinant Human LAP3 protein (His tag N-Terminus) is a Human Full Length protein, in the 1 to 519 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.

View Alternative Names

LAPEP, PEPS, LAP3, Cytosol aminopeptidase, Cysteinylglycine-S-conjugate dipeptidase, Leucine aminopeptidase 3, Leucyl aminopeptidase, Peptidase S, Proline aminopeptidase, Prolyl aminopeptidase, LAP-3

1 Images
SDS-PAGE - Recombinant Human LAP3 protein (AB202613)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human LAP3 protein (AB202613)

15% SDS-PAGE analysis of ab202613 (3μg).

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

His tag N-Terminus

Applications

SDS-PAGE

applications

Biologically active

No

Accession

P28838

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8.5 Constituents: 50% Glycerol (glycerin, glycerine), 0.32% Tris HCl, 0.08% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.03% EDTA

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"MGSSHHHHHHSSGLVPRGSHMFLLPLPAAGRVVVRRLAVRRFGSRSLSTADMTKGLVLGIYSKEKEDDVPQFTSAGENFDKLLAGKLRETLNISGPPLKAGKTRTFYGLHQDFPSVVLVGLGKKAAGIDEQENWHEGKENIRAAVAAGCRQIQDLELSSVEVDPCGDAQAAAEGAVLGLYEYDDLKQKKKMAVSAKLYGSGDQEAWQKGVLFASGQNLARQLMETPANEMTPTRFAEIIEKNLKSASSKTEVHIRPKSWIEEQAMGSFLSVAKGSDEPPVFLEIHYKGSPNANEPPLVFVGKGITFDSGGISIKASANMDLMRADMGGAATICSAIVSAAKLNLPINIIGLAPLCENMPSGKANKPGDVVRAKNGKTIQVDNTDAEGRLILADALCYAHTFNPKVILNAATLTGAMDVALGSGATGVFTNSSWLWNKLFEASIETGDRVWRMPLFEHYTRQVVDCQLADVNNIGKYRSAGACTAAAFLKEFVTHPKWAHLDIAGVMTNKDEVPYLRKGMTGRPTRTLIEFLLRFSQDNA","proteinLength":"Full Length","predictedMolecularWeight":"58.3 kDa","actualMolecularWeight":null,"aminoAcidEnd":519,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Escherichia coli","accessionNumber":"P28838","tags":[{"tag":"His","terminus":"N-Terminus"}]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage duration
1-2 weeks
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

LAP3 also known as leukotriene A4 hydrolase has a molecular weight of approximately 53 kDa. This enzyme functions as an aminopeptidase which is a type of enzyme that removes amino acids from the amino terminus of proteins and peptides. It is expressed in many tissues with significant levels found in the liver and kidney. LAP3 also shows activity in the cellular cytoplasm indicating it plays a role in cellular metabolic processes.
Biological function summary

LAP3 participates in protein maturation and degradation. It plays a role in processing peptides that are destined for further degradation or cellular signaling. The LAP3 protein is not known to be part of a larger complex but it works alongside other enzymes involved in peptide metabolism. This activity contributes to the regulation of intracellular peptide concentrations and supports cellular homeostasis.

Pathways

LAP3 is linked to important biological processes such as protein catabolism and the regulation of blood pressure. It interacts within the peptide processing pathways to influence the generation of bioactive peptides. LAP3 works in conjunction with other proteolytic enzymes such as aminopeptidases and endopeptidases which are essential for various cellular functions. Through these pathways LAP3 indirectly impacts the regulation of physiological processes.

LAP3 is associated with hypertension and certain metabolic disorders. It influences conditions like high blood pressure through its role in generating peptides that can modulate vascular functions. LAP3 has connections with proteins involved in these conditions such as angiotensin-converting enzyme (ACE) which also plays a part in blood pressure regulation. Understanding the functions of LAP3 aids in delineating its potential as a therapeutic target for these diseases.
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Specifications

Form

Liquid

Additional notes

ab202613 was purified using conventional chromatography.

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General info

Function

Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme. For instance, in the presence of Mn(2+), it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates. Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status.

Sequence similarities

Belongs to the peptidase M17 family.

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Product protocols

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Target data

Cytosolic metallopeptidase that catalyzes the removal of unsubstituted N-terminal hydrophobic amino acids from various peptides. The presence of Zn(2+) ions is essential for the peptidase activity, and the association with other cofactors can modulate the substrate spectificity of the enzyme. For instance, in the presence of Mn(2+), it displays a specific Cys-Gly hydrolyzing activity of Cys-Gly-S-conjugates. Involved in the metabolism of glutathione and in the degradation of glutathione S-conjugates, which may play a role in the control of the cell redox status.
See full target information LAP3
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Publications (1)

Recent publications for all applications. Explore the full list and refine your search

Liver cancer 12:590-602 PubMed38058421

2023

Real-Time Fluorescence Imaging to Identify Cholangiocarcinoma in the Extrahepatic Biliary Tree Using an Enzyme-Activatable Probe.

Applications

Unspecified application

Species

Unspecified reactive species

Ryugen Takahashi,Takeaki Ishizawa,Yoshinori Inagaki,Mariko Tanaka,Akira Ogasawara,Yugo Kuriki,Kyohhei Fujita,Mako Kamiya,Tetsuo Ushiku,Yasuteru Urano,Kiyoshi Hasegawa
View all publications
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