人 SBSPON 抗体对
01AB02445
Somatomedin B and thrombospondin type 1 domain containing (SBSPON) is a secreted extracellular matrix (ECM) protein characterized by an N-terminal somatomedin B-like domain and multiple thrombospondin type 1 repeats. Functioning as a structural constituent of the ECM, SBSPON exhibits scavenger receptor and polysaccharide binding activities, localizing primarily to collagen-containing matrices. It is broadly expressed across various tissues, including the brain, kidney, and diverse epithelial and stromal environments, suggesting a fundamental role in cell adhesion and matrix organization. By interacting with various ECM components, SBSPON helps maintain the integrity and functional architecture of the extracellular environment. Its domain structure is consistent with other proteins involved in cell-matrix interactions and signaling, supporting its role in tissue homeostasis and structural support.
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技术参数
- 靶点基因名
- SBSPON
- 基因别名
- C8orf84; RPESP
- 蛋白别名
- somatomedin B and thrombospondin type 1 domain containing; SBSPON
- UniProt
- Q8IVN8
- 物种
- Human
产品详情
- 靶点名称
- SBSPON
- 蛋白名称
- somatomedin B and thrombospondin type 1 domain containing
- 蛋白别名
- Somatomedin-B and thrombospondin type-1 domain-containing protein; RPE-spondin
- 靶点基因名
- SBSPON
- 基因别名
- C8orf84; RPESP
- UniProt
- Q8IVN8
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Somatomedin B and thrombospondin type 1 domain containing (SBSPON) is a secreted extracellular matrix (ECM) protein characterized by an N-terminal somatomedin B-like domain and multiple thrombospondin type 1 repeats. Functioning as a structural constituent of the ECM, SBSPON exhibits scavenger receptor and polysaccharide binding activities, localizing primarily to collagen-containing matrices. It is broadly expressed across various tissues, including the brain, kidney, and diverse epithelial and stromal environments, suggesting a fundamental role in cell adhesion and matrix organization. By interacting with various ECM components, SBSPON helps maintain the integrity and functional architecture of the extracellular environment. Its domain structure is consistent with other proteins involved in cell-matrix interactions and signaling, supporting its role in tissue homeostasis and structural support.