目录号 | 产品详情 | 靶点 | |
---|---|---|---|
T80644 | Antiviral DNA/RNA Synthesis | ||
DNA polymerase-IN-1 作为DNA聚合酶抑制剂,展现出对肿瘤细胞的抗增殖活性,其半抑制浓度(IC50)为20.7 μM。DNA polymerase-IN-1 抑制 Taq DNA 聚合酶,IC 值低于 250μM。DNA polymerase-IN-1 通过RT-PCR检测在体外显示出抗逆转录病毒活性,可用于研究氧化损伤和结直肠癌。 | |||
T79922 | DNA/RNA Synthesis | ||
Taq DNA 聚合酶是一种在PCR过程中广泛使用的耐热性酶,由Thermus aquaticus细菌产生,其功能是在高温下合成DNA链。 | |||
T79926 | DNA/RNA Synthesis | ||
Poly(A) polymerase 通过使用 ATP 作为单元,催化在 RNA 的 3'末端顺序掺入 AMP,形成多聚腺苷尾,从而增强 RNA 稳定性并提升真核细胞 mRNA 的翻译效能。该酶具备高效的聚腺苷酸化活性,能在 RNA 3'端添加 20-200 个腺苷酸(A)单元。 | |||
T82536 | |||
DNA polymerase-IN-4 (Compd 5c),香豆素衍生物,显示出抗逆转录病毒活性,IC50为134.22 μM。 | |||
T79308 | DNA/RNA Synthesis | ||
DNA polymerase-IN-3 (Compd 5b) 为香豆素衍生物,对 Taq DNA聚合酶具有抑制活性,适用于增值性疾病研究。 | |||
T79307 | DNA/RNA Synthesis | ||
DNA polymerase-IN-2 (Compd 3c)为香豆素衍生物,对Taq DNA聚合酶具有抑制作用,IC50为48.25 μM,适用于增殖性疾病研究。 | |||
T74630 | DNA/RNA Synthesis | ||
RNA polymerase II-IN-1(compound 19iv)是一款鹅膏毒素类化合物,能够抑制RNA聚合酶II(Pol II),其半抑制浓度IC50为36.66 nM。该化合物相较于α-Amanitin,对癌细胞展现出更高的细胞毒性,而对正常细胞的毒性较低。 | |||
T74765 | |||
Viral polymerase-IN-1 hydrochloride 是一种 Gemcitabine 衍生物,有效抑制甲型和乙型流感病毒 (influenza) 感染,IC90值为 11.4-15.9 μM。Viral polymerase-IN-1 hydrochloride 对 SARS-CoV-2感染具有活性。Viral polymerase-IN-1 hydrochloride 通过影响细胞中的病毒 RNA 复制/转录来抑制流感病毒感染。 | |||
T79923 | DNA/RNA Synthesis | ||
T7 RNA polymerase是一种由大肠杆菌表达的聚合酶,由T7噬菌体的RNA聚合酶基因编码。它在合成mRNA体外转录(IVT)过程中显示出高度专一性。T7 RNA polymerase能在Mg2+的作用下,针对含有T7启动子序列的单链或双链DNA模板,使用NTP作为底物进行RNA合成,产生的RNA与DNA模板的启动子下游区域互补。 | |||
T74631 | |||
RNA polymerase II-IN-2 (compound 20iii)是高效的RNA polymerase II (Pol II)抑制剂,其Ki值为74.1 nM。该化合物对癌细胞展现出细胞毒性,其对CHO和HEK293细胞的毒性分别为α-amanitin的2倍和5倍。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
---|---|---|---|---|---|
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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
|
|||||
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
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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).
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
TMPK-01348 | 3CLpro/3C-like Protease Protein, SARS-COV-2, Recombinant (aa 1-306) | 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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|
|||||
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.
|