目录号 | 产品详情 | 靶点 | |
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T9430 | PARP | ||
Venadaparib (NOV140101) 是一种选择性和具有口服活性的 PARP 抑制剂,对 PARP1和 PARP2的 IC50分别为 1.4 和 1.0 nM。它可防止 DNA 单链断裂 (SSB) 的修复,可研究实体瘤。 | |||
T7896 | PARP | ||
BYK204165 (RT-017290) 是一种选择性PARP1抑制剂,对重组人 PARP1的pIC50值为 7.35,pKi 值为7.05。它对鼠 PARP-2的pIC50值为 5.38 ,其对 PARP1 的选择性比对 PARP2 高 100 倍。 | |||
T3649 | PARP | ||
BGP-15 (BGP-15 2HCl) 是一种PARP 抑制剂,IC50和Ki 值分别为 120 和 57 μM,在缺血再灌注损伤后具有保护作用。 | |||
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。 | |||
T0220 | Virus Protease Reverse Transcriptase DNA/RNA Synthesis | ||
Foscarnet sodium (Phosphonoformate) 是一种病毒 DNA 聚合酶活性抑制剂,可逆地抑制病毒复制。它是一种用于治疗巨细胞病毒性视网膜炎的抗病毒剂。 | |||
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。 | |||
T1454 | Apoptosis DNA/RNA Synthesis Antibacterial Antibiotic HSV | ||
Acyclovir (Aciclovir) 是鸟嘌呤类似物和具有口服活性的抗病毒剂。它对HSV-1(IC50为 0.85 μM),HSV-2(IC50为 0.86 μM) 和水痘带状疱疹病毒有活性。 | |||
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。 | |||
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。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
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TMPH-00426 | DNA polymerase IV Protein, Colwellia psychrerythraea, Recombinant (His) | Colwellia psychrerythraea | E. coli | ||
DNA polymerase IV Protein, Colwellia psychrerythraea, Recombinant (His) is expressed in E. coli.
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TMPH-00427 | DNA polymerase IV Protein, Colwellia psychrerythraea, Recombinant | Colwellia psychrerythraea | E. coli | ||
DNA polymerase IV Protein, Colwellia psychrerythraea, Recombinant is expressed in E. coli.
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TMPH-00523 | DNA-directed DNA polymerase Protein, Enterobacteria phage RB69, Recombinant (His & Myc) | Escherichia phage RB69 | E. coli | ||
Replicates the viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction for proofreading purpose.
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TMPH-00613 | DNA polymerase II Protein, E. coli, Recombinant (His & Myc) | E. coli | E. coli | ||
Thought to be involved in DNA repair and/or mutagenesis. Its processivity is enhanced by the beta sliding clamp (dnaN) and clamp loader.
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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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TMPH-00360 | DNA polymerase II large subunit Protein, Cenarchaeum symbiosum, Recombinant | Cenarchaeum symbiosum | E. coli | ||
Possesses two activities: a DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction. Has a template-primer preference which is characteristic of a replicative DNA polymerase.
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TMPJ-00792 | DNA PolymeraseBeta Protein, Human, Recombinant (His) | Human | E. coli | ||
Human DNA polymerase β is constitutively expressed in cells. It fills in gaps in DNA that are formed following base excision repair. Repair polymerase that plays a key role in base-excision repair. Has 5'-deoxyribose-5-phosphate lyase (dRP lyase) activity that removes the 5' sugar phosphate and also acts as a DNA polymerase that adds one nucleotide to the 3' end of the arising single-nucleotide gap. It conducts 'gap-filling' DNA synthesis in a stepwise distributive fashion rather than in a processive fashion as for other DNA polymerases. The activity cannot be affected by Aphidicolin, which is an inhibitor of DNA polymerase β.
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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-02884 | CTDP1 Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
Processively dephosphorylates 'Ser-2' and 'Ser-5' of the heptad repeats YSPTSPS in the C-terminal domain of the largest RNA polymerase II subunit. This promotes the activity of RNA polymerase II. Plays a role in the exit from mitosis by dephosphorylating crucial mitotic substrates (USP44, CDC20 and WEE1) that are required for M-phase-promoting factor (MPF)/CDK1 inactivation.
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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-06071 | SARS-CoV-2 RNA-dependent RNA polymerase/RDRP Protein (His) | SARS-CoV-2 | Baculovirus-Insect Cells | ||
SARS-CoV-2 RNA-dependent RNA polymerase/RDRP Protein (His) is expressed in Baculovirus-Insect Cells with His tag. The predicted molecular weight is 108.3 kDa. Accession number: YP_009725307.1
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TMPH-00533 | T7 RNA polymerase Protein, Enterobacteria phage T7, Recombinant (His & Myc) | Escherichia phage T7 | E. coli | ||
Highly processive DNA-dependent RNA polymerase that catalyzes the transcription of class II and class III viral genes. Recognizes a specific promoter sequence and enters first into an 'abortive phase' where very short transcripts are synthesized and released before proceeding to the processive transcription of long RNA chains. Unwinds the double-stranded DNA to expose the coding strand for templating. Participates in the initiation of viral DNA replication presumably by making primers accessible to the DNA polymerase, thus facilitating the DNA opening. Plays also a role in viral DNA packaging, probably by pausing the transcription at the right end of concatemer junction to allow packaging complex recruitment and beginning of the packaging process.
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TMPH-02356 | Influenza A H1N1 (strain A/USA:Huston/AA/1945) Polymerase acidic Protein (His) | H1N1 | Yeast | ||
Plays an essential role in viral RNA transcription and replication by forming the heterotrimeric polymerase complex together with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using a unique mechanism called cap-snatching. It consists in the hijacking and cleavage of host capped pre-mRNAs. These short capped RNAs are then used as primers for viral mRNAs. The PB2 subunit is responsible for the binding of the 5' cap of cellular pre-mRNAs which are subsequently cleaved after 10-13 nucleotides by the PA subunit that carries the endonuclease activity.
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TMPH-02357 | Influenza A H3N2 (strain A/X-31) Polymerase acidic Protein (His) | H3N2 | E. coli | ||
Plays an essential role in viral RNA transcription and replication by forming the heterotrimeric polymerase complex together with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using a unique mechanism called cap-snatching. It consists in the hijacking and cleavage of host capped pre-mRNAs. These short capped RNAs are then used as primers for viral mRNAs. The PB2 subunit is responsible for the binding of the 5' cap of cellular pre-mRNAs which are subsequently cleaved after 10-13 nucleotides by the PA subunit that carries the endonuclease activity.
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TMPH-02580 | CHRAC1 Protein, Mouse, Recombinant (His & Myc) | Mouse | E. coli | ||
Forms a complex with DNA polymerase epsilon subunit POLE3 and binds naked DNA, which is then incorporated into chromatin, aided by the nucleosome remodeling activity of ISWI/SNF2H and ACF1. Does not enhance nucleosome sliding activity of the ACF-5 ISWI chromatin remodeling complex.
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TMPH-01450 | Human herpesvirus 6A (HHV-6 variant A) (strain Uganda-1102) DNA polymerase processivity factor (His) | HHV-6A | Yeast | ||
Human herpesvirus 6A (HHV-6 variant A) (strain Uganda-1102) DNA polymerase processivity factor (His) is expressed in Yeast.
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TMPH-03230 | PHB depolymerase Protein, Ralstonia pickettii, Recombinant (His) | Ralstonia pickettii | E. coli | ||
This protein degrades water-insoluble and water-soluble PHB to monomeric D(-)-3-hydroxybutyrate.
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TMPY-05822 | Hepatitis B Virus (HBV)(ayw/France/Tiollais/1979) Capsid protein (His) | HBV-D | E. coli | ||
Hepatitis B virus (HBV) capsid assembly is a critical step in the propagation of the virus and is mediated by the core protein. The first cytoplasmic step in the formation of an infectious HBV virion is the formation of a capsid containing pregenomic RNA (pgRNA) and the viral polymerase (Pol). HBV capsid assembly is an attractive target for new antiviral therapies.
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TMPH-01247 | POLR3K Protein, Human, Recombinant (His) | Human | Baculovirus | ||
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway.
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TMPH-01648 | MED1 Protein, Human, Recombinant (His & SUMO) | Human | E. coli | ||
Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to promoters by direct interactions with regulatory proteins and serves as a scaffold for the assembly of a functional preinitiation complex with RNA polymerase II and the general transcription factors. Acts as a coactivator for GATA1-mediated transcriptional activation during erythroid differentiation of K562 erythroleukemia cells.
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TMPH-02384 | Lake Victoria marburgvirus (MARV) (strain Popp-67) L Protein (His & Myc) | MARV | E. coli | ||
RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all viral mRNAs with a decreasing efficiency. The first gene is the most transcribed, and the last the least transcribed. The viral phosphoprotein acts as a processivity factor. Capping is concommitant with initiation of mRNA transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase) adds the cap structure when the nascent RNA chain length has reached few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and facilitates subsequent guanine-N-7 methylation, both activities being carried by the viral polymerase. Polyadenylation of mRNAs occur by a stuttering mechanism at a slipery stop site present at the end viral genes. After finishing transcription of a mRNA, the polymerase can resume transcription of the downstream gene.; RNA-directed RNA polymerase that catalyzes the replication of viral genomic RNA. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The replicase mode is dependent on intracellular N protein concentration. In this mode, the polymerase replicates the whole viral genome without recognizing transcriptional signals, and the replicated genome is not caped or polyadenylated.
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TMPH-03734 | Zaire ebolavirus (strain Mayinga-76) L Protein (His) | ZEBOV | E. coli | ||
RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all viral mRNAs with a decreasing efficiency. The first gene is the most transcribed, and the last the least transcribed. The viral phosphoprotein acts as a processivity factor. Capping is concommitant with initiation of mRNA transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase) adds the cap structure when the nascent RNA chain length has reached few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and facilitates subsequent guanine-N-7 methylation, both activities being carried by the viral polymerase. Polyadenylation of mRNAs occur by a stuttering mechanism at a slipery stop site present at the end viral genes. After finishing transcription of a mRNA, the polymerase can resume transcription of the downstream gene.; RNA-directed RNA polymerase that catalyzes the replication of viral genomic RNA. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The replicase mode is dependent on intracellular N protein concentration. In this mode, the polymerase replicates the whole viral genome without recognizing transcriptional signals, and the replicated genome is not caped or polyadenylated.
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TMPH-03735 | Zaire ebolavirus (strain Kikwit-95) L Protein (His & Myc) | ZEBOV | E. coli | ||
RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all viral mRNAs with a decreasing efficiency. The first gene is the most transcribed, and the last the least transcribed. The viral phosphoprotein acts as a processivity factor. Capping is concommitant with initiation of mRNA transcription. Indeed, a GDP polyribonucleotidyl transferase (PRNTase) adds the cap structure when the nascent RNA chain length has reached few nucleotides. Ribose 2'-O methylation of viral mRNA cap precedes and facilitates subsequent guanine-N-7 methylation, both activities being carried by the viral polymerase. Polyadenylation of mRNAs occur by a stuttering mechanism at a slipery stop site present at the end viral genes. After finishing transcription of a mRNA, the polymerase can resume transcription of the downstream gene.; RNA-directed RNA polymerase that catalyzes the replication of viral genomic RNA. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The replicase mode is dependent on intracellular N protein concentration. In this mode, the polymerase replicates the whole viral genome without recognizing transcriptional signals, and the replicated genome is not caped or polyadenylated.
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TMPJ-01067 | TFIIB Protein, Human, Recombinant (GST) | Human | E. coli | ||
Transcription Initiation Factor IIB (TFIIB) is an essential factor for transcription by RNA Polymerase II. TFIIB localizes to the nucleus where it forms a complex (the DAB complex) with transcription factor IID and IIA. TFIIB plays a role as a bridge between IID, which initially recognizes the promoter sequence, and RNA polymerase II. TFIIB is involved in the selection of transcription start site.
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TMPH-01246 | POLR3A Protein, Human, Recombinant (His) | Human | E. coli | ||
DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic core component of RNA polymerase III which synthesizes small RNAs, such as 5S rRNA and tRNAs. Forms the polymerase active center together with the second largest subunit. A single-stranded DNA template strand of the promoter is positioned within the central active site cleft of Pol III. A bridging helix emanates from RPC1 and crosses the cleft near the catalytic site and is thought to promote translocation of Pol III by acting as a ratchet that moves the RNA-DNA hybrid through the active site by switching from straight to bent conformations at each step of nucleotide addition. Plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved in innate immune response. Can sense non-self dsDNA that serves as template for transcription into dsRNA. The non-self RNA polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I pathway.
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TMPH-00811 | Hepatitis delta virus genotype I (HDV) Small delta antigen Protein (His & Myc) | HDV | Yeast | ||
Promotes both transcription and replication of genomic RNA. Following virus entry into host cell, provides nuclear import of HDV RNPs thanks to its nuclear localization signal. May interact with host RNA polymerase II thereby changing its template requirement from DNA to RNA. RNA pol II complex would then acts as an RNA-directed RNA polymerase, and transcribe and replicate HDV genome.
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TMPH-03184 | P2 Protein, Pseudomonas phage phi6, Recombinant (His & Myc) | Pseudomonas phage phi6 | E. coli | ||
Rna-dependent RNA polymerase part of the packaging complex that packages the viral RNA segments, replicate them into a double-stranded form and transcribe them.
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TMPH-01244 | POLM Protein, Human, Recombinant (His) | Human | E. coli | ||
Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ). Participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination.
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TMPH-00094 | HSP21, chloroplastic Protein, Arabidopsis thaliana, Recombinant (His & Myc) | Arabidopsis thaliana | E. coli | ||
Chaperone protein required for seedling and chloroplast development under heat stress, probably by maintaining plastid-encoded RNA polymerase (PEP)-dependent transcription.
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TMPH-01799 | Nucleolar transcription factor 1 Protein, Human, Recombinant (E. coli, His & SUMO) | Human | E. coli | ||
Recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element.
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TMPH-01798 | Nucleolar transcription factor 1 Protein, Human, Recombinant (Cell-Free, His & SUMO) | Human | in vitro E. coli expression system | ||
Recognizes the ribosomal RNA gene promoter and activates transcription mediated by RNA polymerase I through cooperative interactions with the transcription factor SL1/TIF-IB complex. It binds specifically to the upstream control element.
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TMPY-05024 | Zika virus (ZIKV) (strain Zika SPH2015) ZIKV-NS5 protein (His) | ZIKV | Baculovirus-Insect Cells | ||
Zika virus NS5 is involved in methytransferase and RNA guanylytransferase activities and capping and synthesis of RNA. And, NS5 is also an RNA-dependent RNA polymerase.
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TMPH-01245 | POLM Protein, Human, Recombinant (His & Myc) | Human | Baculovirus | ||
Gap-filling polymerase involved in repair of DNA double-strand breaks by non-homologous end joining (NHEJ). Participates in immunoglobulin (Ig) light chain gene rearrangement in V(D)J recombination.
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TMPH-00717 | Protease 7 Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
Protease that can cleave T7 RNA polymerase, ferric enterobactin receptor protein (FEP), antimicrobial peptide protamine and other proteins. This protease has a specificity for paired basic residues.
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TMPH-03229 | Rabies virus (RABV) (strain PM) Phosphoprotein (His) | RABV | E. coli | ||
Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by binding and retaining phosphorylated STAT1 in the cytoplasm or by inhibiting the DNA binding of STAT1 in the nucleus. Might be involved, through interaction with host dynein, in intracellular microtubule-dependent virus transport of incoming virus from the synapse toward the cell body.
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TMPH-00728 | FliA Protein, E. coli, Recombinant | E. coli | E. coli | ||
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes.
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TMPH-00680 | Protease 7 Protein, E. coli O157:H7, Recombinant (G236K K237G, His & SUMO) | E. coli | E. coli | ||
Protease that can cleave T7 RNA polymerase, ferric enterobactin receptor protein (FEP), antimicrobial peptide protamine and other proteins. This protease has a specificity for paired basic residues.
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TMPH-00089 | SPT16 Protein, Arabidopsis thaliana, Recombinant (His & SUMO) | Arabidopsis thaliana | E. coli | ||
Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone that both destabilizes and restores nucleosomal structure. It facilitates the passage of RNA polymerase II and transcription by promoting the dissociation of one histone H2A-H2B dimer from the nucleosome, then subsequently promotes the reestablishment of the nucleosome following the passage of RNA polymerase II (Probable).
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TMPY-02543 | PCNA Protein, Human, Recombinant (His) | Human | Baculovirus-Insect Cells | ||
Proliferating Cell Nuclear Antigen (PCNA) is a protein only expressed in normal proliferate cells and cancer cells. It is central to both DNA replication and repair. One of the well-established functions for PCNA is its role as the processivity factor for DNA polymerase delta and epsilon. PCNA tethers the polymerase catalytic unit to the DNA template for rapid and processive DNA synthesis. Two forms of PCNA exist in cells: (i) a detergent-insoluble trimeric form stably associated with the replicating forks during S phase and (ii) a soluble form in quiescent cells in G1 and G2 phases. PCNA forms a toroidal trimer in S phase with replication factor-C (RF-C) and DNA in an ATP-dependent manner and enables the loading of DNA polymerase delta and epsilon onto the complex. The close association of PCNA with kinase complexes involved in cell cycle machinery indicates that PCNA has a regulatory role in cell cycle progression. PCNA also participates in the processing of branched intermediates that arise during the lagging strand DNA synthesis.
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TMPH-00531 | SSB Protein, Enterobacteria phage T7, Recombinant (His & SUMO) | Enterobacteria phage T7 | E. coli | ||
Single-stranded DNA-binding protein that participates in viral DNA replication, formation of concatemers, recombination and repair of double-stranded breaks. Coats the lagging-strand ssDNA as the replication fork advances and stimulates the activities of viral DNA polymerase and primase/helicase. Coordinates simultaneous synthesis of leading- and lagging-strands. Together with DNA primase/helicase, promotes pairing of two homologous DNA molecules containing complementary single-stranded regions and mediates homologous DNA strand exchange. Promotes also the formation of joint molecules. Disrupts loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation.
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TMPK-01342 | 3CLpro/3C-like Protease Protein (A191V), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01347 | 3CLpro/3C-like Protease Protein (E166A), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPH-00727 | FliA Protein, E. coli, Recombinant (His) | E. coli | E. coli | ||
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor controls the expression of flagella-related genes.
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TMPH-00729 | RpoH Protein, E. coli, Recombinant (His & Myc) | E. coli | E. coli | ||
Sigma factors are initiation factors that promote the attachment of RNA polymerase to specific initiation sites and are then released. This sigma factor is involved in regulation of expression of heat shock genes. Intracellular concentration of free RpoH protein increases in response to heat shock, which causes association with RNA polymerase (RNAP) and initiation of transcription of heat shock genes, including numerous global transcriptional regulators and genes involved in maintaining membrane functionality and homeostasis. RpoH is then quickly degraded, leading to a decrease in the rate of synthesis of heat shock proteins and shut-off of the heat shock response.
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TMPK-01339 | 3CLpro/3C-like Protease Protein (S144A), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01336 | 3CLpro/3C-like Protease Protein (L50F, E166V), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPK-01346 | 3CLpro/3C-like Protease Protein (L50F), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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TMPH-00532 | SSB Protein, Enterobacteria phage T7, Recombinant | Enterobacteria phage T7 | Yeast | ||
Single-stranded DNA-binding protein that participates in viral DNA replication, formation of concatemers, recombination and repair of double-stranded breaks. Coats the lagging-strand ssDNA as the replication fork advances and stimulates the activities of viral DNA polymerase and primase/helicase. Coordinates simultaneous synthesis of leading- and lagging-strands. Together with DNA primase/helicase, promotes pairing of two homologous DNA molecules containing complementary single-stranded regions and mediates homologous DNA strand exchange. Promotes also the formation of joint molecules. Disrupts loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at specific sites during elongation.
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TMPJ-01443 | HChFc2 Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Host cell factor 2(HCFC2) is a cytoplasmic protein. It contains 2 fibronectin type-III domains.HCFC2 binds KMT2A/MLL1, as component of the MLL1/MLL complex.Hcfc2 negative regulation of transcription from RNA polymerase II promoter.
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TMPK-01344 | 3CLpro/3C-like Protease Protein (L167F), SARS-COV-2, Recombinant | SARS-CoV-2 | E. coli | ||
3CL protease, a viral cysteine proteinase, plays an important role in co-translational proteolytic processing of Coronavirus polyproteins. The 3CL protease cleaves as much as 11 sites in the replicase polyproteins and also releases the key replicative functions of polymerase and helicase.
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