目录号 | 产品详情 | 靶点 | |
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T50098 | PARP | ||
TIQ-A 是一种 PARP1 抑制剂,通过碱基切除修复途径参与 DNA 单链断裂修复。 PARP1 由 DNA 损伤触发,其过度激活已被认为是许多病理状况的致病因素,包括缺血和再灌注损伤、哮喘相关炎症和动脉粥样硬化形成。 | |||
T1807 | PARP Wnt/beta-catenin | ||
JW 55 (JW55) 是一种有效且选择性的 β-catenin 信号通路抑制剂,通过抑制 tankyrase 1 和 tankyrase 2 (TNKS1/2) 的 PARP 结构域起作用。 | |||
T4471 | Others PARP | ||
E7449 (UNII-9X5A2QIA7C) 是一种有效的 PARP1 和 PARP2 抑制剂,也抑制 TNKS1 和 TNKS2,使用 32P-NAD+ 作为底物,对 PARP1、PARP2、TNKS1 和 TNKS2 的 IC50 分别为 2.0、1.0、约 50 和约 50 nM。 | |||
T22264 | PARP | ||
AZ9482 是一种选择性 PARP1/2/6的三重抑制剂,IC50值分别为 1 、1 和640 nM。 | |||
T7042 | PARP | ||
1,5-Isoquinolinediol 是一种多聚(ADP-核糖)合成酶抑制剂,对PARP1的IC50值为 0.39 µM。它用于研究 PARP1 在 DNA 修复和氧化应激诱导的细胞死亡中的作用。 | |||
T3062 | PARP Wnt/beta-catenin | ||
WIKI4 是tankyrase 有效抑制剂,其对TNKS2的IC50值为 26 nM。它有效抑制Wnt/β-catenin 信号传导,其EC50值为 75 nM。它通过抑制TNKS2的酶活性来介导其对Wnt/β-catenin 信号传导的影响。它对 SCLC 细胞具有细胞毒性,其IC50值为 0.02 μM。 | |||
T5058 | PARP | ||
Pamiparib (BGB-290) 是一种具有口服活性、强效、高选择性的 PARP 抑制剂,对PARP1和PARP2的IC50值分别为 0.9 nM 和 0.5 nM。它具有强大的 PARP 捕获能力,具有穿透大脑的能力,可用于研究癌症。 | |||
T6339 | PARP | ||
AG14361 是一种 PARP-1抑制剂,Ki 值小于 5 nM,在通透的 SW620 细胞和完整的 SW620 细胞中,抑制 PARP-1的活性,IC50值分别为 29 和 14 nM。 | |||
T4472 | PARP | ||
NMS-P118是可口服的高选择性PARP-1抑制剂,用于癌症治疗,在HeLa 细胞中的IC50值为0.04 μM。 | |||
T5399 | PARP | ||
GeA-69 是一种选择性变构 PARP14 大结构域 2 (MD2) 抑制剂,Kd 值为 2.1 µM。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPY-01188 | PARP Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Poly (ADP-ribose) polymerase 1(PRAP1), also known as NAD(+) ADP-ribosyltransferase 1(ADPRT), is a chromatin-associated enzyme that modifies various nuclear proteins by poly(ADP-ribosyl)ation. The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxyl group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 2-3 units. The poly(ADP-ribosyl)ation modification is critical for a wide range of processes, including DNA repair, regulation of chromosome structure, transcriptional regulation, mitosis and apoptosis. PARP1 is demonstrated to mediate the poly(ADP-ribose) ation of APLF (aprataxin PNK-like factor) and CHFR (checkpoint protein with FHA and RING domains), two representative proteins involved in the DNA damage response and checkpoint regulation. Further, It has been suggested that DNA-dependent protein kinase (DNA-PK), another component of DNA repair, suppresses PARP activity, probably through direct binding and/or sequestration of DNA-ends which serve as an important stimulator for both enzymes. PARP1 inhibitors are thus proposed as a targeted cancer therapy for recombination deficient cancers, such as BRCA2 tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPY-02465 | PARP Protein, Mouse, Recombinant (His) | Mouse | Baculovirus-Insect Cells | ||
Poly (ADP-ribose) polymerase 1(PRAP1), also known as NAD(+) ADP-ribosyltransferase 1(ADPRT), is a chromatin-associated enzyme that modifies various nuclear proteins by poly(ADP-ribosyl)ation. The ADP-D-ribosyl group of NAD+ is transferred to an acceptor carboxyl group on a histone or the enzyme itself, and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 2-3 units. The poly(ADP-ribosyl)ation modification is critical for a wide range of processes, including DNA repair, regulation of chromosome structure, transcriptional regulation, mitosis and apoptosis. PARP1 is demonstrated to mediate the poly(ADP-ribose) ation of APLF (aprataxin PNK-like factor) and CHFR (checkpoint protein with FHA and RING domains), two representative proteins involved in the DNA damage response and checkpoint regulation. Further, It has been suggested that DNA-dependent protein kinase (DNA-PK), another component of DNA repair, suppresses PARP activity, probably through direct binding and/or sequestration of DNA-ends which serve as an important stimulator for both enzymes. PARP1 inhibitors are thus proposed as a targeted cancer therapy for recombination deficient cancers, such as BRCA2 tumors.Cancer ImmunotherapyImmune CheckpointImmunotherapyTargeted Therapy
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TMPH-01943 | PARP4 Protein, Human, Recombinant (His) | Human | E. coli | ||
PARP4 Protein, Human, Recombinant (His) is expressed in E. coli.
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TMPH-01879 | PARP11 Protein, Human, Recombinant (His) | Human | E. coli | ||
Mono-ADP-ribosyltransferase that mediates mono-ADP-ribosylation of target proteins. Plays a role in nuclear envelope stability and nuclear remodeling during spermiogenesis.
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TMPH-01882 | PARP9 Protein, Human, Recombinant (His) | Human | E. coli | ||
ADP-ribosyltransferase which, in association with E3 ligase DTX3L, plays a role in DNA damage repair and in immune responses including interferon-mediated antiviral defenses. Within the complex, enhances DTX3L E3 ligase activity which is further enhanced by PARP9 binding to poly(ADP-ribose). In association with DTX3L and in presence of E1 and E2 enzymes, mediates NAD(+)-dependent mono-ADP-ribosylation of ubiquitin which prevents ubiquitin conjugation to substrates such as histones. During DNA repair, PARP1 recruits PARP9/BAL1-DTX3L complex to DNA damage sites via PARP9 binding to ribosylated PARP1. Subsequent PARP1-dependent PARP9/BAL1-DTX3L-mediated ubiquitination promotes the rapid and specific recruitment of 53BP1/TP53BP1, UIMC1/RAP80, and BRCA1 to DNA damage sites. In response to DNA damage, PARP9-DTX3L complex is required for efficient non-homologous end joining (NHEJ); the complex function is negatively modulated by PARP9 activity. Dispensable for B-cell receptor (BCR) assembly through V(D)J recombination and class switch recombination (CSR). In macrophages, positively regulates pro-inflammatory cytokines production in response to IFNG stimulation by suppressing PARP14-mediated STAT1 ADP-ribosylation and thus promoting STAT1 phosphorylation. Also suppresses PARP14-mediated STAT6 ADP-ribosylation.
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TMPH-01880 | PARP2 Protein, Human, Recombinant (His) | Human | E. coli | ||
Poly-ADP-ribosyltransferase that mediates poly-ADP-ribosylation of proteins and plays a key role in DNA repair. Mediates glutamate, aspartate or serine ADP-ribosylation of proteins: the ADP-D-ribosyl group of NAD(+) is transferred to the acceptor carboxyl group of target residues and further ADP-ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units. Serine ADP-ribosylation of proteins constitutes the primary form of ADP-ribosylation of proteins in response to DNA damage. Mediates glutamate and aspartate ADP-ribosylation of target proteins in absence of HPF1. Following interaction with HPF1, catalyzes serine ADP-ribosylation of target proteins; HPF1 conferring serine specificity by completing the PARP2 active site. PARP2 initiates the repair of double-strand DNA breaks: recognizes and binds DNA breaks within chromatin and recruits HPF1, licensing serine ADP-ribosylation of target proteins, such as histones, thereby promoting decompaction of chromatin and the recruitment of repair factors leading to the reparation of DNA strand breaks. In addition to proteins, also able to ADP-ribosylate DNA: preferentially acts on 5'-terminal phosphates at DNA strand breaks termini in nicked duplex.
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TMPY-02421 | PARP3 Protein, Human, Recombinant (His & GST) | Human | Baculovirus-Insect Cells | ||
Poly(ADP-ribose) polymerase 3 (PARP3) is an important member of the PARP family and shares high structural similarities with both PARP1 and PARP2. Poly(ADP-ribose) polymerase 3 (PARP3), a critical player in cellular response to DNA double-strand breaks (DSBs), plays an essential role in the maintenance of genome integrity. The ADP ribosyl transferase [poly(ADP-ribose) polymerase] ARTD3(PARP3) is a newly characterized member of the ARTD(PARP) family that catalyzes the reaction of ADP ribosylation, a key posttranslational modification of proteins involved in different signaling pathways from DNA damage to energy metabolism and organismal memory.
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TMPH-01941 | PARP12 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
PARP12 Protein, Human, Recombinant (His & Myc) is expressed in E. coli.
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TMPH-01942 | PARP14 Protein, Human, Recombinant (His & Myc) | Human | HEK293 | ||
PARP14 Protein, Human, Recombinant (His & Myc) is expressed in HEK293.
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TMPH-01944 | PARP9 Protein, Human, Recombinant (His & Myc) | Human | HEK293 | ||
PARP9 Protein, Human, Recombinant (His & Myc) is expressed in HEK293.
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TMPH-01881 | PARP2 Protein, Human, Recombinant (GST & His) | Human | Baculovirus | ||
PARP2 Protein, Human, Recombinant (GST & His) is expressed in Baculovirus with N-terminal GST tag and C-terminal 6xHis tag. The predicted molecular weight is 92.8 kDa. Accession number: Q9UGN5
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TMPH-01056 | Caspase-3 Protein, Human, Recombinant (His) | Human | E. coli | ||
Involved in the activation cascade of caspases responsible for apoptosis execution. At the onset of apoptosis it proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Cleaves and activates sterol regulatory element binding proteins (SREBPs) between the basic helix-loop-helix leucine zipper domain and the membrane attachment domain. Cleaves and activates caspase-6, -7 and -9. Involved in the cleavage of huntingtin. Triggers cell adhesion in sympathetic neurons through RET cleavage. Cleaves and inhibits serine/threonine-protein kinase AKT1 in response to oxidative stress. Cleaves XRCC4 and phospholipid scramblase proteins XKR4, XKR8 and XKR9, leading to promote phosphatidylserine exposure on apoptotic cell surface.
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TMPY-02831 | Caspase-7 Protein, Human, Recombinant (His) | Human | E. coli | ||
Caspase 7, also known as caspase-7 and MCH3, belongs to the cysteine-aspartic acid protease (caspase) family. Caspases play a role in the signal transduction pathways of apoptosis, necrosis and inflammation. There are two major classes of caspases: initiators and effectors. The initiator isoforms (caspases-1,-4,-5,-8,-9,-10,-11,-12) are activated by, and interact with, upstream adaptor molecules through protein-protein interaction domains known as CARD and DED. Effector caspases (-3,-6,-7) are responsible for cleaving downstream substrates and are sometimes referred to as the executioner caspases. Caspase 7 exists in lung, skeletal muscle, liver, kidney, spleen, heart, and moderately in testis. Caspase 7 cannot be detected in the brain. Caspase 7 functions in the activation cascade of caspases responsible for apoptosis execution. It cleaves and activates sterol regulatory element binding proteins (SREBPs). It proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp- -Gly-217' bond. Overexpression promotes programmed cell death.
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