
人 PALM2AKAP2 抗体对
01AB02516
PALM2 and AKAP2 fusion (PALM2AKAP2) is a naturally occurring readthrough transcript producing a fusion protein combining paralemmin-2 (PALM2) and A-kinase anchoring protein 2 (AKAP2). It belongs to the paralemmin downstream gene (PDG) family and is characterized by binding to the regulatory subunit (RII) of protein kinase A (PKA). This fusion protein may play roles in establishing cell polarity and integrating PKA-RII isoforms within signaling systems, suggesting involvement in neuronal and cardiac signaling pathways. Functionally, AKAP2 anchors extracellular signal-regulated kinase 1 (ERK1), regulating cardiac myofibroblast migration, which may influence cardiac remodeling processes. Its participation in cardiac β-adrenergic signaling and regulation of cardiac cell migration implies potential relevance in cardiovascular diseases.
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技术参数
- 靶点基因名
- PALM2AKAP2
- 基因别名
- KIAA0920; PAKAP; PALM2
- 蛋白别名
- PALM2 and AKAP2 fusion; PALM2AKAP2
- UniProt
- Q9Y2D5
- 物种
- Human
产品详情
- 靶点名称
- PALM2AKAP2
- 蛋白名称
- PALM2 and AKAP2 fusion
- 蛋白别名
- PALM2-AKAP2 fusion protein; A-kinase anchor protein 2; AKAP-2; AKAP-KL; Paralemmin A kinase anchor protein; Paralemmin-2; Protein kinase A-anchoring protein 2; PRKA2
- 靶点基因名
- PALM2AKAP2
- 基因别名
- KIAA0920; PAKAP; PALM2
- UniProt
- Q9Y2D5
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
PALM2 and AKAP2 fusion (PALM2AKAP2) is a naturally occurring readthrough transcript producing a fusion protein combining paralemmin-2 (PALM2) and A-kinase anchoring protein 2 (AKAP2). It belongs to the paralemmin downstream gene (PDG) family and is characterized by binding to the regulatory subunit (RII) of protein kinase A (PKA). This fusion protein may play roles in establishing cell polarity and integrating PKA-RII isoforms within signaling systems, suggesting involvement in neuronal and cardiac signaling pathways. Functionally, AKAP2 anchors extracellular signal-regulated kinase 1 (ERK1), regulating cardiac myofibroblast migration, which may influence cardiac remodeling processes. Its participation in cardiac β-adrenergic signaling and regulation of cardiac cell migration implies potential relevance in cardiovascular diseases.