S100A15 Proteins, Antibodies, cDNA Clones Research Reagents

S100A7A (S100 Calcium Binding Protein A7A) is a protein coding gene located on human chromosome 1q21.3. S100A7A is also known as NICE2, NICE-2, S100A15, S100A7f, and S100A7L1. The human S100A7A gene encodes a 11305 Da protein containing 101 amino acids. Among its related pathways are Innate Immune System and Defensins. S100A7A is related to calcium ion binding and protein self-association. S100A7 is an important paralog of S100A7A gene. S100A7A is associated with some diseases, including Psoriasis and Macular Degeneration, Age-Related, 13.

S100A15 Protein (1)

    S100A15 Antibody (1)

      S100A15 cDNA Clone (16)


      In expression vector

      S100A15 qPCR Primer (1)

      S100A15 Background

      Koebnerisin is also known as protein S100-A7A (S100A7A), S100 calcium-binding protein A7-like 1 (S100A7L1) or S100 calcium-binding protein A15 (S100A15). Human S100A7A / S100A15 is a novel member of the S100 family of EF-hand calcium-binding proteins and was recently identified in psoriasis, where it is significantly upregulated in lesional skin. S100A7 is expressed by both normal cultured and malignant keratinocytes and malignant breast epithelial cells within ductal carcinoma in situ, suggesting an association with abnormal pathways of differentiation. S100A7 plays a role in the pathogenesis of inflammatory skin disease, as a chemotactic factor for hematopoietic cells. It also plays a role in early stages of breast tumor progression in association with the development of the invasive phenotype. The association of the 11.2 kDa S100A7A / S100A15 with psoriasis suggests that it contributes to the pathogenesis of the disease and could provide a molecular target for therapy.

      S100A15 References

      • Wolf R, et al. (2009) Highly homologous hS100A15 and hS100A7 proteins are distinctly expressed in normal breast tissue and breast cancer. Cancer Lett. 277 (1): 101-7.
      • Buchau AS, et al. (2007) S100A15, an antimicrobial protein of the skin: regulation by E. coli through Toll-like receptor 4. J Invest Dermatol. 127 (11): 2596-604.
      • Boeshans KM, et al. (2006) Purification, crystallization and preliminary X-ray diffraction of human S100A15. Acta Crystallogr Sect F Struct Biol Cryst Commun. 62 (5): 467-70.

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