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Related Experiment Video

Updated: Jun 25, 2026

Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation

Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation

Published on: September 29, 2019

Calcium-binding S100 protein expression in pterygium.

Andri K Riau¹, Tina T Wong, Roger W Beuerman

¹Singapore Eye Research Institute, Singapore.

Molecular Vision

|February 19, 2009

Summary

This study found higher levels of S100A6, S100A8, and S100A9 proteins in pterygium tissue compared to normal conjunctiva. Altered S100A11 localization also suggests these proteins may contribute to pterygium formation.

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The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...

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Area of Science:

Ophthalmology
Molecular Biology
Cell Biology

Background:

Pterygium is an ocular surface disease characterized by fibrovascular growth onto the cornea.
The exact cause of pterygium remains unknown.
S100 proteins are involved in cell migration, proliferation, and differentiation.

Purpose of the Study:

To investigate the presence and distribution of specific S100 proteins in pterygium tissue.
To compare S100 protein expression in pterygium versus normal conjunctiva.

Main Methods:

Immunofluorescent staining for S100A4, S100A6, S100A8, S100A9, and S100A11.
Western blot and quantitative real-time polymerase chain reaction (RT-PCR) to confirm protein expression and secretion.

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Expression, Purification, and Antimicrobial Activity of S100A12

Expression, Purification, and Antimicrobial Activity of S100A12

Published on: May 13, 2017

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Last Updated: Jun 25, 2026

Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation

Purification of Human S100A12 and Its Ion-induced Oligomers for Immune Cell Stimulation

Published on: September 29, 2019

Expression, Purification, and Antimicrobial Activity of S100A12

Expression, Purification, and Antimicrobial Activity of S100A12

Published on: May 13, 2017

Main Results:

S100A4, S100A6, S100A8, S100A9, and S100A11 were detected in both pterygium and conjunctiva epithelium.
S100A6, S100A8, and S100A9 showed higher expression in pterygium epithelium.
S100A11 exhibited altered localization in pterygium epithelium compared to conjunctiva.

Conclusions:

Elevated S100A6, S100A8, and S100A9 levels in pterygium suggest their involvement in the disease.
Changes in S100A11 localization further support a role in pterygium pathogenesis.
S100 proteins are potential biomarkers and therapeutic targets for pterygium.