Recombinant Mouse S100A3 protein (His tag N-Terminus)

補足情報

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S100A3 also known as protein S100-A3 is a member of the S100 protein family characterized by calcium-binding motifs specifically the EF-hand motif. This protein has a molecular mass of approximately 11 kDa. S100A3 expresses primarily in tissues such as hair follicles and is particularly abundant in the filiform region of human hair cuticles. Its presence is significant in cellular compartments where it interacts with zinc and calcium ions suggesting a role in ion homeostasis and regulation.

Biological function summary

S100A3 participates in various cellular functions including cytoskeletal dynamics cell motility and differentiation. This protein does not form part of a larger complex but interacts closely with other proteins involved in maintaining cellular architecture and intracellular signaling. Its function involves modulating enzymatic activities and facilitating structural stability. The zinc-binding properties enhance the protein's ability to participate in structural organization and signaling pathways.

Pathways

S100A3 interacts with several signaling and regulatory pathways integral to cellular structure and function. It plays a role in the calcium signaling pathway influencing processes mediated by calcium ions including muscle contraction and neurotransmitter release. Additionally S100A3 participates in pathways related to cell differentiation through interactions with cytoskeletal proteins contributing to epithelial and hair follicle cell differentiation and growth.

S100A3 has been linked to conditions such as breast cancer and melanoma. Its interaction with calcium-binding proteins may affect tumor initiation and progression. In breast cancer S100A3 expression levels could correlate with tumor invasiveness where it might work together with proteins like S100A4. In melanoma variations in S100A3 expression could contribute to cell migration and invasion indicating its potential as a biomarker for disease progression and therapeutic targeting.