Recombinant Human Psoriasin protein (His tag N-Terminus)

Supplementary information

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

Psoriasin also known as S100A7 is a member of the S100 protein family. It has a molecular mass of approximately 11.4 kDa. This protein exhibits calcium binding properties that influence its function. Psoriasin primarily expresses in keratinocytes which are predominant in the epidermis of the skin. Additionally it appears in various epithelia like mucous membranes. The expression levels rise in certain skin conditions suggesting it has a role in skin physiology.

Biological function summary

Psoriasin acts as an antimicrobial peptide contributing to the skin’s defense system against microbial invasion. It helps in controlling the growth of bacteria like E. coli and fungi. The protein does not function as part of a larger complex. Instead it operates independently to maintain the integrity of the skin barrier. Psoriasin also shows involvement in the inflammatory response of the skin where it interact with other immune system players.

Pathways

Several biological systems involve psoriasin including inflammation and skin homeostasis pathways. It interacts closely with other S100 proteins such as S100A8 and S100A9 which are part of the inflammatory process. These interactions can regulate immune cell migration and cytokine production highlighting its active role in modulating skin immune responses. Psoriasin serves as an important component in maintaining the balance between immune protection and inflammation within these pathways.

Psoriasin associates with psoriasis and breast cancer. In psoriasis it significantly increases aligning with its role in inflammation and skin barrier maintenance. The upregulation of psoriasin in psoriasis has been linked to overexpression of related proteins like S100A8 contributing to the chronic inflammatory state. In breast cancer particularly in certain carcinoma contexts its presence suggests a role in cancer cell survival. Researchers study its interaction with proteins in the cancer microenvironment to better understand its influence on tumor progression.