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
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human AP-Q protein (AB165911)
ab165911 on a 12.5% SDS-PAGE stained with Coomassie Blue.
Reactivity data
Product details
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
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.
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.
Target data
Publications (1)
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International journal of colorectal disease 39:205 PubMed39702605
2024
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
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