
人 S100P 抗体对
01AB01827
S100 calcium binding protein P (S100P) is a calcium-sensing protein characterized by two EF-hand motifs that facilitate interactions with various signaling partners, including ezrin, IQGAP1, and the receptor for advanced glycation end products (RAGE). Through these interactions, S100P regulates cytoskeletal dynamics, cell adhesion, migration, and proliferation via the ERK/MAPK pathway. While normally expressed in specific epithelial tissues, S100P is significantly overexpressed in numerous malignancies. Clinically, it serves as a functional driver and biomarker in pancreatic, breast, and lung carcinomas, as well as endometrial adenosquamous carcinoma. By modulating p53 and HDM2, S100P promotes tumor survival, invasion, and resistance to therapy, making it a critical factor in cancer progression and metastasis.
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技术参数
- 靶点基因名
- S100P
- 基因别名
- S100E
- 蛋白别名
- S100 calcium binding protein P; S100P
- UniProt
- P25815
- 物种
- Human
产品详情
- 靶点名称
- S100P
- 蛋白名称
- S100 calcium binding protein P
- 蛋白别名
- Protein S100-P; Migration-inducing gene 9 protein; MIG9; Protein S100-E; S100 calcium-binding protein P
- 靶点基因名
- S100P
- 基因别名
- S100E
- UniProt
- P25815
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
S100 calcium binding protein P (S100P) is a calcium-sensing protein characterized by two EF-hand motifs that facilitate interactions with various signaling partners, including ezrin, IQGAP1, and the receptor for advanced glycation end products (RAGE). Through these interactions, S100P regulates cytoskeletal dynamics, cell adhesion, migration, and proliferation via the ERK/MAPK pathway. While normally expressed in specific epithelial tissues, S100P is significantly overexpressed in numerous malignancies. Clinically, it serves as a functional driver and biomarker in pancreatic, breast, and lung carcinomas, as well as endometrial adenosquamous carcinoma. By modulating p53 and HDM2, S100P promotes tumor survival, invasion, and resistance to therapy, making it a critical factor in cancer progression and metastasis.