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人 THSD1 抗体对
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人 THSD1 抗体对

01AB00603

THSD1 is a protein encoded by the THSD1 gene, which contains a type 1 thrombospondin domain found in proteins involved in the complement pathway and extracellular matrix. It is a type I transmembrane protein with a 388 amino acid extracellular region, a 21 amino acid transmembrane region, and a 418 amino acid cytoplasmic region, featuring six potential N-linked glycosylation sites, a thrombospondin type-1 (TSP1) domain, and three Ig-like domains. THSD1 is highly expressed in hematopoietic stem cells (HSCs) and progenitor cells, and it is postulated to play a role in the regulation of vasculogenesis and/or angiogenesis, as well as in HSC homing to the bone marrow niche. Mutations in THSD1 have been associated with intracranial aneurysms and subarachnoid hemorrhage, indicating its critical role in endothelial cell adhesion to the extracellular matrix.

Human
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技术参数

靶点基因名
THSD1
基因别名
TMTSP
蛋白别名
thrombospondin type 1 domain containing 1; THSD1
UniProt
Q9NS62
物种
Human

产品详情

靶点名称
THSD1
蛋白名称
thrombospondin type 1 domain containing 1
蛋白别名
Thrombospondin type-1 domain-containing protein 1; Transmembrane molecule with thrombospondin module
靶点基因名
THSD1
基因别名
TMTSP
UniProt
Q9NS62
来源物种
Homo sapiens (Human)
物种反应性
Human

背景介绍

THSD1 is a protein encoded by the THSD1 gene, which contains a type 1 thrombospondin domain found in proteins involved in the complement pathway and extracellular matrix. It is a type I transmembrane protein with a 388 amino acid extracellular region, a 21 amino acid transmembrane region, and a 418 amino acid cytoplasmic region, featuring six potential N-linked glycosylation sites, a thrombospondin type-1 (TSP1) domain, and three Ig-like domains. THSD1 is highly expressed in hematopoietic stem cells (HSCs) and progenitor cells, and it is postulated to play a role in the regulation of vasculogenesis and/or angiogenesis, as well as in HSC homing to the bone marrow niche. Mutations in THSD1 have been associated with intracranial aneurysms and subarachnoid hemorrhage, indicating its critical role in endothelial cell adhesion to the extracellular matrix.