S100 Calcium Binding Protein P, Recombinant, Human (S100P)

S100P was originally described as a placental protein of 95 amino acid residues shares about 50% sequence identity with the brain S100 proteins alpha and beta. S100 proteins are small dimeric members of the EF-hand superfamily of Ca(2+) binding proteins thought to participate in mediating intracellular Ca(2+) signals by binding to and thereby regulating target proteins in a Ca(2+)-dependent manner. S100P is dysregulated in the androgen-independent prostate cancer cell lines LNCaP-R, DU145, and PC3 and may play a role in the etiology of prostate cancer. In ductal hyperplasias, in situ and invasive ductal carcinoma, but not in the normal tissues, S100P overexpression is an early event that might play an important role in the imortalization of human breast epithelial cells in vitro and tumor progression in vivo. In NIH3T3 cells, the expression of S100P led to the presence of S100P in the culture medium, increased cellular proliferation, and enhanced survival following detachment from the culture substrate or after exposure to the chemotherapeutic agent 5-flurouracil. The proliferation and survival effects of S100P expression were duplicated in a time- and concentration-dependent manner by extracellular addition of purified S100P to wild-type NIH3T3 cells and correlated with the activation of Erks and NFB. To determine the mechanisms involved in these effects, we tested the hypothesis that S100P activated RAGE (Receptor for Activated Glycation End-Products). It was found that S100P coimmunoprecipitated with RAGE. Furthermore, the effects of S100P on cell signaling, proliferation and survival were blocked by agents that interfere with RAGE including administration of an amphoterin derived peptide known to antagonize RAGE activation, anti-RAGE antibodies and by expression of a dominant negative RAGE. These data suggest that S100P can act in an autocrine manner via RAGE to stimulate cell proliferation and survival.\n \nThe Recombinant Human S100P has a molecular mass of 10.4kD containing 95 amino acid residues of the human S100P.\n\nAA Sequence: \nMTELEAAMGM IIDVFSRYSG SEGSTQTLTK GELKVLMEKE LPGFLQSGKD KDAVDKLLKD LDANGDAQVD FSEFIVFVAA ITSACHKYFE KAGLK\n\nSpecificity: \nThe recombinant human S100P is 100% homologous with the human S100P.\n\nApplications: \nSuitable for use in Western Blot. Other applications not tested.\n\nRecommended Dilutions:\nOptimal dilutions to be determined by the researcher.\n\nStorage and Stability:\nLyophilized powder may be stored at -20 degrees C. Stable for 12 months at -20 degrees C. Reconstitute with sterile ddH2O. Aliquot and store at -20 degrees C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

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SPECIFICATIONS

Catalog Number

S0052-04P

Size

2ug

Form

Supplied as a lyophilized powder from a solution containing 0.05M phosphate buffer, pH 7.2, 0.1M sodium chloride. Add 200ul of ddH2O and let the lyophilized pellet dissolve completely.

Purity

~ 95% (SDS-PAGE); Two-step procedure using anion-exchange and size exclusion chromatography.

References

1. Jin G, Wang S, Hu X, Jing Z, Chen J, Ying K, Xie Y, Mao Y. Characterization of the tissue-specific expression of the s100P gene whichencodes an EF-hand Ca2+binding protein. Mol Biol Rep. 2003 Dec; 30(4): 243-8. 2. Arumugam T, Simeone DM, Schmidt AM, Logsdon CD. S100P stimulates cell proliferation and survival via RAGE. J Biol Chem. 2003 Nov 14 3. Shyu RY, Huang SL, Jiang SY. Retinoic acid increases expression of the calcium-binding protein S100P in human gastric cancer cells. J Biomed Sci. 2003 May-Jun; 10(3): 313-9. 4. Sato N, Hitomi J. S100P expression in human esophageal epithelial cells: Human esophageal epithelial cells sequentially produce different S100 proteins in the process of differentiation. Anat Rec. 2002 May 1; 267(1): 60-9. 5. Gribenko A, Lopez MM, Richardson JM 3rd, Makhatadze GI. Cloning, overexpression, purification, and spectroscopic characterization of human S100P. Protein Sci. 1998 Jan; 7(1): 211-5.