人 SLURP2 抗体对
01AB03462
Secreted LY6/PLAUR domain containing 2 (SLURP2) is a secreted protein belonging to the Ly6/uPAR superfamily, characterized by a structural three-finger LU domain. It acts as an endogenous modulator of nicotinic and muscarinic acetylcholine receptors, exhibiting potent inhibitory effects on alpha-4:beta-2-containing nAChRs. SLURP2 is primarily expressed in epithelial cells, where it regulates keratinocyte proliferation, differentiation, and apoptosis. Specifically, it has been shown to accelerate keratinocyte growth while delaying differentiation and reducing pro-apoptotic signaling. Clinically, SLURP2 is significantly upregulated in psoriatic skin lesions, indicating a central role in the pathophysiology of psoriasis. Furthermore, the protein demonstrates antiproliferative activity in colorectal adenocarcinoma cells through its interaction with the alpha-7-nAChR. Its involvement in wound healing and protection against oncogenic transformation further underscores its importance in maintaining skin homeostasis and its potential as a therapeutic target in inflammatory and neoplastic skin diseases.
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技术参数
- 靶点基因名
- SLURP2
- 蛋白别名
- secreted LY6/PLAUR domain containing 2; SLURP2
- UniProt
- P0DP57
- 物种
- Human
产品详情
- 靶点名称
- SLURP2
- 蛋白名称
- secreted LY6/PLAUR domain containing 2
- 蛋白别名
- Secreted Ly-6/uPAR domain-containing protein 2; Secreted LY6/PLAUR domain-containing protein 2; Secreted Ly-6/uPAR-related protein 2; SLURP-2
- 靶点基因名
- SLURP2
- UniProt
- P0DP57
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Secreted LY6/PLAUR domain containing 2 (SLURP2) is a secreted protein belonging to the Ly6/uPAR superfamily, characterized by a structural three-finger LU domain. It acts as an endogenous modulator of nicotinic and muscarinic acetylcholine receptors, exhibiting potent inhibitory effects on alpha-4:beta-2-containing nAChRs. SLURP2 is primarily expressed in epithelial cells, where it regulates keratinocyte proliferation, differentiation, and apoptosis. Specifically, it has been shown to accelerate keratinocyte growth while delaying differentiation and reducing pro-apoptotic signaling. Clinically, SLURP2 is significantly upregulated in psoriatic skin lesions, indicating a central role in the pathophysiology of psoriasis. Furthermore, the protein demonstrates antiproliferative activity in colorectal adenocarcinoma cells through its interaction with the alpha-7-nAChR. Its involvement in wound healing and protection against oncogenic transformation further underscores its importance in maintaining skin homeostasis and its potential as a therapeutic target in inflammatory and neoplastic skin diseases.