S100P Human

S100P, initially identified as a 95-amino acid placental protein, exhibits approximately 50% sequence homology with S100 proteins alpha and beta found in the brain. S100 proteins are small, dimeric members of the EF-hand superfamily of Ca(2+)-binding proteins. These proteins are believed to be involved in intracellular Ca(2+) signaling by binding to and regulating target proteins in a Ca(2+)-dependent manner. Besides Ca2+, S100P also binds to Zn2+ and Mg2+. The gene encoding S100P is located on chromosome 4p16. Studies have shown S100P to be dysregulated in androgen-independent prostate cancer cell lines, including LNCaP-R, DU145, and PC3, suggesting a potential role in prostate cancer development. Overexpression of S100P is observed in ductal hyperplasias, in situ and invasive ductal carcinoma, but not in normal tissues. This overexpression is an early event that may contribute to the immortalization of human breast epithelial cells in vitro and tumor progression in vivo. In NIH3T3 cells, S100P expression resulted in the protein's presence in the culture medium, increased cellular proliferation, and enhanced survival after detachment from the culture substrate or exposure to the chemotherapeutic agent 5-fluorouracil. These effects of S100P expression were replicated by adding purified S100P to wild-type NIH3T3 cells in a time- and concentration-dependent manner, leading to the activation of Erks and NFκB. To investigate the mechanisms underlying these effects, researchers explored the hypothesis that S100P activates RAGE (Receptor for Activated Glycation End-Products). Results showed that S100P co-immunoprecipitated with RAGE. Moreover, agents that interfere with RAGE, such as an amphoterin-derived peptide known to antagonize RAGE activation, anti-RAGE antibodies, and the expression of a dominant-negative RAGE, blocked S100P's effects on cell signaling, proliferation, and survival. These findings indicate that S100P may act in an autocrine fashion via RAGE to stimulate cell proliferation and survival.

Recombinant Human S100P is a protein with a molecular weight of 10.4 kDa, composed of 95 amino acid residues of the human S100P protein.

White powder, lyophilized and filtered.

The protein solution is filtered through a 0.4 μm filter and then lyophilized from a 0.5 mg/ml solution in 0.05M Phosphate buffer with a pH of 7.2 and 0.1M NaCl.

To reconstitute the lyophilized protein, add deionized water and allow the pellet to dissolve completely.

The lyophilized protein should be stored at -20°C. After reconstitution, aliquot the protein to prevent repeated freeze-thaw cycles. The reconstituted protein is stable at 4°C for a limited period and shows no significant change after two weeks at this temperature.

The purity of the protein is greater than 95% as determined by SDS-PAGE analysis.

Protein S100-P, S100 calcium-binding protein P, S100P, S100E, MIG9.

Escherichia Coli.

MTELEAAMGM IIDVFSRYSG SEGSTQTLTK GELKVLMEKE LPGFLQSGKD KDAVDKLLKD LDANGDAQVD FSEFIVFVAA ITSACHKYFE KAGLK.