抗人 PARP4 抗体对
01AB02995
Poly(ADP-ribose) polymerase family member 4 (PARP4), also known as vault PARP (VPARP), is a large nuclear enzyme with structural and functional similarities to PARP1, including a BRCT domain, WGR domain, helical domain (HD), and ADP-ribosyltransferase (ART) domain, which together suggest a role in recognizing DNA breaks and catalyzing poly(ADP-ribosyl)ation, although its HD maintains the catalytic region in a constitutively open and potentially active conformation, unlike the auto-inhibited state seen in PARP1. PARP4 is a component of the vault ribonucleoprotein complex, with its C-terminal region mediating vault association, while the N-terminal region is homologous to PARP1, indicating possible involvement in nucleic acid binding and regulation. Functionally, PARP4 can modulate RNA splicing and has been shown to interact with hnRNPM, contributing to tumor suppressive activity in lung adenocarcinoma, with evidence that its enzymatic and protein interaction domains both play roles in reducing tumorigenicity.
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技术参数
- 靶点基因名
- PARP4
- 基因别名
- ADPRTL1; KIAA0177; PARPL
- 蛋白别名
- poly(ADP-ribose) polymerase family member 4; PARP4
- UniProt
- Q9UKK3
- 物种
- Human
产品详情
- 靶点名称
- PARP4
- 蛋白名称
- poly(ADP-ribose) polymerase family member 4
- 蛋白别名
- Protein mono-ADP-ribosyltransferase PARP4; 193 kDa vault protein; ADP-ribosyltransferase diphtheria toxin-like 4; ARTD4; PARP-related/IalphaI-related H5/proline-rich; PH5P; Poly [ADP-ribose] polymerase 4; PARP-4; Vault poly(ADP-ribose) polymerase; VPARP
- 靶点基因名
- PARP4
- 基因别名
- ADPRTL1; KIAA0177; PARPL
- UniProt
- Q9UKK3
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Poly(ADP-ribose) polymerase family member 4 (PARP4), also known as vault PARP (VPARP), is a large nuclear enzyme with structural and functional similarities to PARP1, including a BRCT domain, WGR domain, helical domain (HD), and ADP-ribosyltransferase (ART) domain, which together suggest a role in recognizing DNA breaks and catalyzing poly(ADP-ribosyl)ation, although its HD maintains the catalytic region in a constitutively open and potentially active conformation, unlike the auto-inhibited state seen in PARP1. PARP4 is a component of the vault ribonucleoprotein complex, with its C-terminal region mediating vault association, while the N-terminal region is homologous to PARP1, indicating possible involvement in nucleic acid binding and regulation. Functionally, PARP4 can modulate RNA splicing and has been shown to interact with hnRNPM, contributing to tumor suppressive activity in lung adenocarcinoma, with evidence that its enzymatic and protein interaction domains both play roles in reducing tumorigenicity.