S100P, human, recombinant, full length
- Known as:
- S100P, H. sapiens, Rec., length
- Catalog number:
- G02S1P01
- Product Quantity:
- 5 mg
- Category:
- -
- Supplier:
- Giotto Biotech
- Gene target:
- S100P human recombinant full length
Related genes to: S100P, human, recombinant, full length
- Gene:
- S100P NIH gene
- Name:
- S100 calcium binding protein P
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 4p16.1
- Locus Type:
- gene with protein product
- Date approved:
- 1993-10-04
- Date modifiied:
- 2016-10-05
- Gene:
- S100PBP NIH gene
- Name:
- S100P binding protein
- Previous symbol:
- -
- Synonyms:
- FLJ12903, S100PBPR
- Chromosome:
- 1p35.1
- Locus Type:
- gene with protein product
- Date approved:
- 2005-12-01
- Date modifiied:
- 2019-03-19
Related products to: S100P, human, recombinant, full length
Related articles to: S100P, human, recombinant, full length
- The S100 family contains more than 20 Ca2+-binding proteins that participate in numerous cellular biological processes. However, the prognostic value of individual S100s in hepatocellular carcinoma (HCC) remains unclear. Therefore, we comprehensively assessed the prognostic value of S100s in HCC. - Source: PubMed
Wan RenruiTan ZhenhuaQian HaiLi PengZhang JianZhu XiaofengXie PingRen Lingyan - We have previously shown that expression of S100PBP, an S100P binding partner, gradually decreases during progression of pancreatic ductal adenocarcinomas (PDAC). Here, we show that loss of S100PBP leads to oncogenic transformation of pancreatic cells; after deregulation of S100PBP expression, both in silico and in vitro analyses highlighted alterations of genes known to modulate cytoskeleton, cell motility and survival. Overexpression of S100P reduced S100PBP expression, while co-immunoprecipitation indicated the interaction of S100P with S100PBP-p53-ubiquitin protein complex, likely causing S100PBP degradation. The doxycycline-induced Kras activation resulted in decreased S100PBP levels, while low-dose treatment with HDAC inhibitor MS-275 rescued its expression in both human and mouse PDAC cell lines. This indicates Kras as an upstream epigenetic regulator of S100PBP. Finally, analysis of TCGA PanCancer Atlas PDAC datasets demonstrated poor prognosis in patients with high S100P and low S100PBP expression, suggesting that S100PBP is a novel tumour suppressor gene with potential clinical utility. - Source: PubMed
Publication date: 2023/10/04
Srivastava KLines K EJach DCrnogorac-Jurcevic T - S100 proteins are intracellular calcium ion sensors that participate in cellular processes, some of which are involved in normal breast functioning and breast cancer development. Despite several S100 genes being overexpressed in breast cancer, their roles during disease development remain elusive. Human mammary epithelial cells (HMECs) can be exposed to fluid shear stresses and implications of such interactions have not been previously studied. The goal of this study was to analyze expression profiles of S100 genes upon exposing HMECs to fluid flow. - Source: PubMed
Publication date: 2021/10/27
Fuh Kenneth FWithell JessicaShepherd Robert DRinker Kristina D - Interleukin-11 (IL-11) and S100P are oncoproteins co-expressed in numerous cancers, which might favor their interaction during oncogenesis. We have explored the possibility of this interaction by surface plasmon resonance spectroscopy, intrinsic fluorescence, and chemical crosslinking. Recombinant forms of IL-11 and S100P interact with each other under physiological level of calcium ions. IL-11 molecule has at least two S100P-binding sites with dissociation constants of 32 nM and 288 nM, which is 5-13-fold lower than its affinity to extracellular domain of IL-11 receptor subunit α. S100P does not alter IL-11-induced STAT3 activation in HEK293 cells co-expressing IL-11 receptors, but could affect other tumorigenic signaling pathways. The highly specific IL-11 - S100P interaction occurring under physiologically relevant conditions should be taken into consideration upon development of the antineoplastics inhibiting IL-11 signaling. - Source: PubMed
Publication date: 2015/11/06
Kazakov Alexei SSokolov Andrei SRastrygina Victoria ASolovyev Valery VIsmailov Ramis GMikhailov Roman VUlitin Andrei BYakovenko Andrey RMirzabekov Tajib APermyakov Eugene APermyakov Sergei E - Altered expression of specific microRNAs (miRNAs) has been observed in human cervical cancer. However, the biological functions of many of these miRNAs are yet to be discovered. We previously showed that miR-944 is significantly more abundant in cervical cancer tissues than their normal counterparts. In this study, we investigated the functions and targets of miR-944 in human cervical cancer cells. MiR-944 is located in the intron of the tumor protein p63 (TP63) gene, which is frequently overexpressed in cervical carcinomas. Using gain- and loss-of-function experiments in vitro, we demonstrate that miR-944 promotes cell proliferation, migration and invasion, but has no effect on apoptosis, in human cervical cancer cells. To identify the targets of miR-944, we performed photoactivatable-ribonucleoside-enhanced crosslinking and immunoprecipitation followed by deep sequencing. Among the candidate targets, we validated HECW2 (HECT domain ligase W2) and S100PBP (S100P binding protein) as direct targets of miR-944 using luciferase reporter assays and western blot analysis. Our findings reveal novel functions and targets of miR-944 in human cervical cancer cells, which may provide new insights of its role in cervical carcinogenesis. - Source: PubMed
Publication date: 2014/09/04
Xie HongLee LinkiatScicluna PatrickKavak ErsenLarsson CatharinaSandberg RickardLui Weng-Onn