目录号 | 产品详情 | 靶点 | |
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T8150 | PARP Endogenous Metabolite | ||
Nudifloramide (1-Methyl-6-oxo-1,6-dihydropyridine-3-carboxamide) 是烟酰胺-腺嘌呤二核苷酸(NAD) 降解的一种最终产物,可显著抑制PARP-1活性。 | |||
T5S2358 | BCL PARP p38 MAPK Caspase Parasite Autophagy | ||
Dehydrocorydaline (13-Methylpalmatine) 是一种生物碱。它调节Bax,Bcl-2蛋白表达,激活caspase-7,caspase-8,并使PARP 失活。它能增强p38 MAPK 活化,具有抗炎、抗癌等功效。它具有强大的抗疟疾作用,并具低细胞毒性。 | |||
T12695 | PARP | ||
RBN-2397 是一种有效的、选择性的、具有口服活性的跨物种 NAD+ 竞争性 PARP7 抑制剂,IC50 小于 3 nM。它选择性结合 PARP7 ,Kd 为0.001 μM,可恢复干扰素 I 型信号转导,有用于晚期或转移性实体肿瘤的研究潜力。 | |||
T1878 | PARP Wnt/beta-catenin | ||
XAV-939 (NVP-XAV939) 是一种 Tankyrase (TNKS) 抑制剂,抑制 TNKS1 和 TNKS2 (IC50=11/4 nM)。XAV-939 可以选择性抑制 Wnt/β-catenin 介导的转录。 | |||
T2591 | PARP Autophagy | ||
Veliparib (ABT-888) 是一种可口服的 PARP 抑制剂,抑制PARP1和PARP2的Ki 分别为 5.2 和 2.9 nM。它增强细胞凋亡和自噬。 | |||
T9497 | PARP | ||
Niraparib tosylate monohyrate 也称为 MK-4827,是一种聚 (ADP-核糖) 聚合酶 (PARP) 抑制剂,具有潜在的抗肿瘤活性。 MK4827 抑制 PARP 活性,增强 DNA 链断裂的积累,促进基因组不稳定性和细胞凋亡。 PARP 蛋白家族通过碱基切除修复 (BER) 途径检测和修复单链 DNA 断裂。 | |||
T3231 | Apoptosis Others PARP | ||
Niraparib (MK-4827) 是一种 PARP 抑制剂,可以抑制 PARP1 和 PARP2 (IC50=3.8/2.1 nM),具有选择性。Niraparib 具有抗肿瘤活性,可以抑制 DNA 损伤修复、诱导细胞凋亡。 | |||
T2124 | PARP | ||
PJ34 hydrochloride (PJ34 HCl) 是一种 PARP1/2的特异性有效抑制剂,IC50值分别为 110 nM 和 86 nM。 | |||
T7439 | PARP Antibacterial Transferase | ||
3-Methoxybenzamide (3-MBA) 是一种多聚 ADP-核糖合成酶的竞争性抑制剂,可抑制枯草芽孢杆菌的细胞分裂,诱导细胞凋亡。它可促进蓝薯植株的生长、微瘤化和转化效率。 | |||
T6912 | PARP | ||
NU1025 (NSC-696807) 是一种PARP 的有效抑制剂,IC50为 400 nM,Ki 为 48 nM。它可增强电离辐射和抗癌药物的细胞毒性,有抗癌和神经保护的作用。 |
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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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-01804 | OARD1 Protein, Human, Recombinant (His & Myc) | Human | E. coli | ||
ADP-ribose glycohydrolase that hydrolyzes ADP-ribose and acts on different substrates, such as proteins ADP-ribosylated on glutamate and O-acetyl-ADP-D-ribose. Specifically acts as a glutamate mono-ADP-ribosylhydrolase by mediating the removal of mono-ADP-ribose attached to glutamate residues on proteins. Does not act on poly-ADP-ribosylated proteins: the poly-ADP-ribose chain of poly-ADP-ribosylated glutamate residues must by hydrolyzed into mono-ADP-ribosylated glutamate by PARG to become a substrate for OARD1. Deacetylates O-acetyl-ADP ribose, a signaling molecule generated by the deacetylation of acetylated lysine residues in histones and other proteins. Catalyzes the deacylation of O-acetyl-ADP-ribose, O-propionyl-ADP-ribose and O-butyryl-ADP-ribose, yielding ADP-ribose plus acetate, propionate and butyrate, respectively.
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TMPH-01091 | CHD1L Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
DNA helicase which plays a role in chromatin-remodeling following DNA damage. Targeted to sites of DNA damage through interaction with poly(ADP-ribose) and functions to regulate chromatin during DNA repair. Able to catalyze nucleosome sliding in an ATP-dependent manner. Helicase activity is strongly stimulated upon poly(ADP-ribose)-binding.
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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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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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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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