人 FHIT 抗体对
01AB03449
Fragile histidine triad diadenosine triphosphatase (FHIT) is a 17-kDa cytoplasmic enzyme and a member of the histidine triad protein family. It functions as a dinucleoside polyphosphate hydrolase, specifically catalyzing the magnesium-dependent hydrolysis of diadenosine triphosphate into AMP and ADP. Structurally, FHIT exists as a homodimer with conserved residues essential for nucleoside and phosphate binding. It is widely recognized as a tumor suppressor, with frequent loss of heterozygosity or homozygous deletions observed across various human malignancies. Unlike classical tumor suppressors, FHIT does not directly inhibit cell proliferation but instead influences tumorigenesis through distinct pathways, such as the regulation of apoptosis. Recent studies have demonstrated that FHIT binds to annexin A4, leading to its delocalization from the plasma membrane. This interaction is critical for restoring chemosensitivity in paclitaxel-resistant lung cancer cells, highlighting its clinical relevance in oncology and therapeutic resistance.
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技术参数
- 靶点基因名
- FHIT
- 蛋白别名
- fragile histidine triad diadenosine triphosphatase; FHIT
- UniProt
- P49789
- 物种
- Human
产品详情
- 靶点名称
- FHIT
- 蛋白名称
- fragile histidine triad diadenosine triphosphatase
- 蛋白别名
- Bis(5'-adenosyl)-triphosphatase; AP3A hydrolase; AP3Aase; Adenosine 5'-monophosphoramidase FHIT; Adenylylsulfatase; Adenylylsulfate-ammonia adenylyltransferase; Diadenosine 5'; 5'''-P1; P3-triphosphate hydrolase; Dinucleosidetriphosphatase; Fragile histidine triad protein
- 靶点基因名
- FHIT
- UniProt
- P49789
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Fragile histidine triad diadenosine triphosphatase (FHIT) is a 17-kDa cytoplasmic enzyme and a member of the histidine triad protein family. It functions as a dinucleoside polyphosphate hydrolase, specifically catalyzing the magnesium-dependent hydrolysis of diadenosine triphosphate into AMP and ADP. Structurally, FHIT exists as a homodimer with conserved residues essential for nucleoside and phosphate binding. It is widely recognized as a tumor suppressor, with frequent loss of heterozygosity or homozygous deletions observed across various human malignancies. Unlike classical tumor suppressors, FHIT does not directly inhibit cell proliferation but instead influences tumorigenesis through distinct pathways, such as the regulation of apoptosis. Recent studies have demonstrated that FHIT binds to annexin A4, leading to its delocalization from the plasma membrane. This interaction is critical for restoring chemosensitivity in paclitaxel-resistant lung cancer cells, highlighting its clinical relevance in oncology and therapeutic resistance.