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AB165911

Recombinant Human AP-Q protein

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(1 Publication)

Recombinant Human AP-Q protein is a Human Full Length protein, in the 1 to 198 aa range, expressed in Wheat germ, suitable for ELISA, WB.

View Alternative Names

AQPEP, LVRN, Aminopeptidase Q, AP-Q, APQ, CHL2 antigen, Laeverin

1 Images
SDS-PAGE - Recombinant Human AP-Q protein (AB165911)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant Human AP-Q protein (AB165911)

ab165911 on a 12.5% SDS-PAGE stained with Coomassie Blue.

Key facts

Expression system

Wheat germ

Tags

GST tag N-Terminus

Applications

ELISA, WB

applications

Biologically active

No

Accession

Q6Q4G3

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 0.79% Tris HCl, 0.31% Glutathione

storage-buffer

Reactivity data

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

Product details

This product was previously labelled as Laeverin.

Sequence info

[{"sequence":"MKVENFKTSEIQELFDIFTYSKGASMARMLSCFLNEHLFVSALKSYLKTFSYSNAEQDDLWRHFQMAIDDQSTVILPATIKNIMDSWTHQSGFPVITLNVSTGVMKQEPFYLENIKNRTLLTSNDTWIVPILWIKNGTTQPLVWLDQSSKVFPEMQVSDSDHDWVILNLNMTGYYRVNYDKLGWKKLNQQLEKDPKMR","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":198,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"Wheat germ","accessionNumber":"Q6Q4G3","tags":[{"tag":"GST","terminus":"N-Terminus"}]}]

Properties and storage information

Shipped at conditions
Dry Ice
Appropriate short-term storage conditions
-80°C
Appropriate long-term storage conditions
-80°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False

Supplementary information

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

AP-Q also known as aminopeptidase Q is a metallopeptidase enzyme involved in the trimming of peptides at the amino terminus. Its molecular mass approximates 110 kDa. This protein is part of the M1 family of aminopeptidases and exhibits specificity for certain peptide substrates. AP-Q expression occurs in various tissues including the kidneys liver and small intestine where it plays a role in protein digestion and metabolism.
Biological function summary

AP-Q is important for regulating peptide hormone activity by processing signaling peptides. It exists as part of a larger peptide-hydrolyzing complex in cellular environments interacting with other enzymes to modulate peptide chains' length and activity. By breaking down bioactive peptides AP-Q influences physiologic processes like blood pressure regulation and immune responses. Its enzymatic activity contributes to maintaining homeostasis through controlled degradation of functional peptides.

Pathways

AP-Q integrates into critical biological processes such as the renin-angiotensin system and antigen processing pathways. In the renin-angiotensin system AP-Q helps regulate blood pressure by controlling the generation of active angiotensin peptides. Related proteins in these pathways include angiotensin-converting enzyme (ACE) which similarly processes peptide substrates to maintain cardiovascular function and fluid balance. By operating within these pathways AP-Q ensures that peptide levels are balanced to sustain normal physiological conditions.

Researchers have linked AP-Q to hypertension and immune system dysfunctions. Anomalies in its enzyme activity may contribute to hypertension through improper regulation of peptide hormones that control vascular resistance. AP-Q also affects immune responses by manipulating antigen presentation processes which can relate to autoimmune disorders or immune deficiencies. Proteins like ACE already known for their role in hypertension often connect with AP-Q in these pathological contexts thereby contributing to or mitigating disease outcomes.

Specifications

Form

Liquid

General info

Function

Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C.

Sequence similarities

Belongs to the peptidase M1 family.

Post-translational modifications

N-glycosylated.

Product protocols

Target data

Metalloprotease which may be important for placentation by regulating biological activity of key peptides at the embryo-maternal interface. On synthetic substrates it shows a marked preference for Leu-4-methylcoumaryl-7-amide (Leu-MCA) over Met-MCA, Arg-LCA and Lys-LCA. Cleaves the N-terminal amino acid of several peptides such as angiotensin-3, kisspeptin-10 and endokinin C.
See full target information LVRN

Publications (1)

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

International journal of colorectal disease 39:205 PubMed39702605

2024

AQP3 mediates autophagy through SIRT1/p62 signal to alleviate intestinal epithelial cell damage caused by sepsis.

Applications

Unspecified application

Species

Unspecified reactive species

Canmin Wang,Yingfang Hu,Yunfeng Song,Xinyi Hu
View all publications

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