Olink

Olink®
Part of Thermo Fisher Scientific

Explore HT

Gene
QPCT

Uniprot
Q16769

Protein
Glutaminyl-peptide cyclotransferase

See alternative names Glutaminyl cyclase,
Glutaminyl-tRNA cyclotransferase,
Glutamyl cyclase

Uniprot Function Description

Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue. Also catalyzes N-terminal pyroglutamate formation. In vitro, catalyzes pyroglutamate formation of N-terminally truncated form of APP amyloid-beta peptides [Glu-3]-amyloid-beta. May be involved in the N-terminal pyroglutamate formation of several amyloid-related plaque-forming peptides.

Sample type

Recommended sample types are human plasma and serum. For other sample types e.g cerebrospinal fluid, (CSF), tissue or cell lysate, please contact support@olink.com for more information. Please note that protein expression levels are expected to vary in different sample types and certain assays may be affected by interfering substances such as hemolysate.

Precision

Precision (repeatability) is calculated from linearized NPX values over LOD.

Within run precision Coefficient of Variation (CV)
7%

Analytical measuring range

The technical data reported below refers to the measured value in the in vitro validation assays run using known concentrations of recombinant antigen.

LOD (NPX)
-5.4
Hooked
No
Hook (NPX)
0.8

Dilution factor

For optimal assay readout, Olink assays are run using different dilutions of the original samples e.g. undiluted, 1:10, or higher. The dilution factor for this assay is noted below and should be taken into account when estimating the appropriate addressable biological concentration of the protein based on the in vitro validation data.

Dilution factor
1:100

Biomarker Validation Data

Additional validation data, as well as a more detailed description of how the Olink panels are quality controlled can be found in our Data Validation documents – go to Document download center

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