目录号 | 产品详情 | 靶点 | |
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T72862 | |||
PARP-2/1-IN-2 是 Veliparib 的对映异构体,是一种有效的PARP 抑制剂,对PARP-2和PARP-1的Ki 分别为 2 和 5 nM。在以PARP 活性为基础的细胞测定中,PARP-2/1-IN-2 的 EC50为 3 nM。 | |||
T39139 | |||
PARP1-IN-6 is a dual tubulin/PARP-1 inhibitor with IC 50 values of 0.94 and 0.48 μM, respectively. | |||
T6181 | PARP | ||
UPF 1069 是一种特异性PARP 抑制剂,对 PARP-1 和 PARP-2 的IC50值分别为 8 和 0.3 μM。 | |||
T67932 | PARP | ||
PARP10-IN-3 是一种有效且具有选择性的单-ADP-核糖基转移酶 PARP10 抑制剂,对人 PARP10 具有抑制作用( IC50 :480 nM)。PARP10-IN-3 对人 PARP2 和 人 PARP15也具有抑制作用, IC50 值都是 1.7 μM。 | |||
T16761 | Others PARP | ||
RK-287107 是一种有效且特异性的 tankyrase 抑制剂,可阻断结直肠癌细胞生长,对 tankyrase-1和 tankyrase-2的 IC50分别为 14.3 和 10.6 nM。 | |||
T73007 | PARP | ||
PARP10-IN-2 是一种有效的单-ADP-核糖基转移酶 PARP10 抑制剂,对人 PARP10 的 IC50 值为 3.64 μM。PARP10-IN-2 对 PARP2 和 PARP15也具有抑制作用, IC50 分别为 27 μM 和 11 μM。 | |||
T8184 | PARP Endogenous Metabolite PPAR | ||
Fucosterol 是从藻类、海藻或硅藻中分离的一种甾醇,具有抗氧化、抗脂肪、降低血液胆固醇、抗糖尿病和抗癌活性。它通过抑制 PPARα和C/EBPα的表达调控脂肪生成,可用于抗肥胖试剂开发研究。 | |||
T2484 | PARP | ||
AZD-2461 是一种 PARP 抑制剂,可抑制 PARP1、PARP2 和 PARP3 的活性,IC50值分别为 5、2 和 200 nM。 | |||
T21524 | PARP | ||
4-amino-1,8-Naphthalimide 是PARP 抑制剂,可增强癌细胞对 γ 辐射诱导的细胞毒性的敏感度。 | |||
T72553 | PARP | ||
ARTD10/PARP10-IN-1 是一种强效性的 PARP 抑制剂,抑制单 ADP 核糖转移酶 ARTD7/PARP15,ARTD8/PARP14,ARTD10/PARP10 和聚 ADP-核糖聚合酶-1 (ARTD1/PARP1),具有潜在的抗癌抗肿瘤活性,可用于研究前列腺癌和乳腺癌。 |
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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