Olink

Olink®
Part of Thermo Fisher Scientific

Explore HT

Gene
SESTD1

Uniprot
Q86VW0

Protein
SEC14 domain and spectrin repeat-containing protein 1

See alternative names Huntingtin-interacting protein-like protein,
Protein Solo

Uniprot Function Description

May act as the primary docking protein directing membrane turnover and assembly of the transient receptor potential channels TRPC4 and TRPC5. Binds phospholipids such as phosphatidylinositol monophosphates, phosphatidylinositol diphosphates (PIP2s) and phosphatidic acid, but not less polar lipids including phosphatidylcholine, phosphatidylserine, and phosphatidylinositol. The binding to PIP2s is calcium dependent. Might be involved in the plasma membrane localization of CTNNB1.

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)
N/A

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)
2.5
Hooked
No
Hook (NPX)
8.2

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
1:1

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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