|
ORF cDNA clones
|
CRISPR / TALEN
|
Lentivirus
|
AAV
|
TALE-TF
|
ORF knockin clones
|
|
Antibody
|
Proteins
|
miRNA target clones
|
qPCR primers
|
shRNA clones
|
miRNA products
|
Promoter clones
|
Validated All-in-One™ qPCR Primer for TOP1(NM_003286.2) Search again
Product ID:
HQP018171
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
TOPI
Gene Description:
DNA topoisomerase I
Target Gene Accession:
NM_003286.2(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
|
|
| A | B |
|
Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
|
Summary
This gene encodes a DNA topoisomerase, an enzyme that controls and alters the topologic states of DNA during transcription. This enzyme catalyzes the transient breaking and rejoining of a single strand of DNA which allows the strands to pass through one another, thus altering the topology of DNA. This gene is localized to chromosome 20 and has pseudogenes which reside on chromosomes 1 and 22. [provided by RefSeq].
Gene References into function
- CPT-11 may provide therapeutic efficacy for esophageal squamous cell cancer and the effects correlate with the level of DNA topoisomerase I protein.
- active site of a type I DNA topoisomerase from the kinetoplastid protozoan Leishmania donovani, compared to human structure
- Different effects on human topoisomerase I by minor groove and intercalated deoxyguanosine adducts derived from two polycyclic aromatic hydrocarbon diol epoxides at or near a normal cleavage site.
- Point mutations in the topoisomerase I gene in patients with non-small cell lung cancer treated with irinotecan
- The origin recognition complex (ORC) marks a replication origin in the promoter
- ATP and Topoisomerase I activity found indispensable for cDNA synthesis in the HIV-1 replication process. Mutant enzyme lacking activity inhibited HIV-1 infectivity
- role of N-terminal domain in nucleolar localization of human DNA topoisomerase I
- TOP1 delocalizes from the nucleolus to the nucleoplasm when sumoylated by camptothecin
- binds to DNA first in an inactive conformation and then rearranges its active site for catalysis
- DNA binding induces conformational transition within this enzyme in solution
- presence of dna topoisomerase I in different testicular tumor types
- Binding and dissociation of human emzyme with hairpin-loop RNAs: implications for the regulation of HIV-1 replication
- RNA splicing factor ASF/SF2 inhibits human topoisomerase I mediated DNA relaxation
- The x-ray crystal structure of human topoisomerase I covalently joined to double-stranded DNA & bound to Topotecan shows that Topotecan mimics a DNA base pair & binds at the DNA cleavage site, intercalating between the upstream & downstream base pairs.
- proteins indentified binding to the N-terminal domain of human topoisomerase I
- DNA is unwound bidirectionally by a ternary complex of T antigen, nucleolin and this enzyme.
- The exon 2 region was required for physical binding of p14(ARF) to Topo I & stimulatory activity. p14(ARF) (R71A) was more efficient than wild-type to activate Topo I. Nucleolar location is linked the biological function of the ARF-Topo I complex.
- The contributions of strong and week nonspecific electrostatic, van der Waals's, and hydrophobic interactions, and hydrogen bonding of the enzymes to the complex formation with the single- and double-stranded DNAs were determined.
- DNA relaxation by this enzyme occurs in the closed clamp conformation of the protein.
- Factors affecting the specific recognition of topologically stressed DNA were analyzed on the basis of the thermodynamic and kinetic data on the Topo-DNA interaction and the X-ray data on human Topo
- Human topoisomerase I plays an important role in HIV-1 replication and infectivity, and differences in the species specificity of HIV-1 infection can at least in part be attributed to differences in topoisomerase I activities.
- a single mutation in the linker domain confers protein flexibility and camptothecin resistance to human topoisomerase I
- Topo I activity is now shown to be involved in DNA damage/repair pathway in vivo
- Lys(532) functions as a general acid during cleavage to protonate the leaving 5'-oxygen
- topo I truncated up to position 210 is not stabilized by camptothecin in covalent DNA-complexes inside a living cell, whereas in vitro it retains full DNA-relaxation activity, and is targeted by camptothecin in the usual manner
- topoisomerase I-mediated DNA damage and cell death is induced by hydrogen peroxide
- human topoisomerase I exclusively dissociated HIV-1 reverse transcriptase, which strongly binds to structural RNAs
- DNA damage at telomeric repeats by topoisomerase I is a prominent feature of camptothecin-induced apoptosis
- Data describe the specific functions of individual N-terminal regions of topoisomerase I by characterizing mutants lacking amino acid residues 1-202 or 191-206 or having tryptophane-205 substituted by glycine.
- p53 disruption has a dramatic effect on how glioblastoma cells process topoisomerase I inhibitor-mediated DNA damage.
- topoisomerase I cleavage complexes correlate with apoptosis, however, at low UV doses the cleavage complex level was very low and the complexes were repaired
- nucleolar/nucleoplasmic partitioning of topoisomerase I is regulated by interactions with RNA polymerase I and DNA but not by sumoylation
- expression of human NUP98-TOP1 in murine bone marrow confers a potent in vitro growth advantage and a block in differentiation in hematopoietic precursors
- Data report the synthesis of a number of oligonucleotides containing methylphosphonates at single positions for the purpose of investigating the hydrogen-bonding contacts necessary for human topoisomerase I function.
- propose that arsenic trioxide induces topoisomerase I-DNA complexes that participate in chromatin fragmentation and programmed cell death during apoptosis
- function for the automodification reaction is to regulate the interaction between PARP-1 and Topo I, and consequently, the Topo I activity, in response to DNA damage.
- An essential component of this Top1/DNA active site model is the rotated +1 deoxyguanosine, and in vitro experiments and molecular modeling studies supported rotation of the +1 deoxyguanosine out of the helix
- This is the first report that conjugated PUFA such as cEPA act as inhibitors of pols and topos.
- The complexities of the relaxation reaction, the cellular roles, and the pathways that must exist to repair topoisomerase I-mediated DNA damage highlight the importance of continued study of this essential enzyme. (review)
- Identification of 36 nuclear proteins that were associated with topoisomerase I.
- The polypeptide containing tandem RRM domains inhibited DNA cleavage by topoisomerase I similarly as the complete SF2/ASF
- A single Thr718Ala mutation in human topoisomerase I slows down DNA relaxation.
- Molecular simulations reveal a dynamical picture of how topoisomerase I accommodates large-scale motion of DNA as it changes its supercoiling state, and indicate that relaxation of positive and negative supercoils are fundamentally different.
- mechanism for the recruitment of topoisomerase I to papillomavirus DNA replication forks and for stimulating topoisomerase I to allow for efficient relaxation of the torsional stress induced by replication fork progression
- SUMO1 polymeric chain assembles on human topoisomerase I in vitro
- Using both purified proteins and through co-precipitation, it was determined that HPV-11 E2 binds human topoisomerase I. E2 can stimulate topoisomerase I DNA relaxation activity 3- to 4-fold.
- DNA damage-independent induction of cell death using colcemid and tumor necrosis factor alpha is also accompanied by a strong topoisomerase I response that correlates with the onset of apoptotic hallmarks
- It was found that modifications involving replacement of the nucleophilic tyrosine OH group with NH2, SH, or I groups eliminated DNA relaxation activity, as did changing the orientation of the nucleophilic tyrosine OH group.
- human topoisomerase I double cleavage complexes are part of the normal catalytic cycle of this enzyme that occur in vitro and possibly also in vivo
- analysis of Holliday junction substrate resolution by human topoisomerase I
- analyses of the C-terminal domain indicate that this fragment protein (topo6.3)is in a molten globule state with a native-like tertiary fold that contains a large population of alpha-helix structure and extensive surface hydrophobic regions
- A molecular dynamics simulation of the conformational changes of human topoisomerase I.
- The present study showed elevated expression of topo-I, Ki-67, and mutant p53 in patients with uterine carcinosarcoma suggesting sensitivity to topo-I-targeted drug treatment.
- Topo I DNA relaxation activity is present in nuclear extracts derived from human sperm. The sperm topo I activity is inhibited by camptothecin, similarly to the somatic enzyme.
- very high levels of topoisomerase 1 (TOP1) in the nucleus, and specifically the nucleolus, of human Purkinje neurons.
- topoisomerase I functions as a component of DNA damage recognition and/or a cofactor of fast DNA-repair processes
- topoisomerase I and mutants lacking tryptophane-205 relax positive supercoils faster than negative supercoils under both processive and distributive conditions.
- Topors enhances the formation of high-molecular weight SUMO-1 conjugates of TOP1 in a reconstituted in vitro system and also in human osteosarcoma cells
- These results strongly indicate that the association of topo I with these six residues in T antigen is essential for DNA replication.
- this paper, we show that the translocation depends on the short fragment of the domain (residues from 1 to 67).
- Betulinic acid inhibits formation of apoptotic topoisomerase I-DNA complexes in prostate cancer cells and prevents cellular topoisomerase I from participating in the apoptotic process.
- tryptophan anchor stabilized the N-terminus of the functional domain and prevented the loss of Top1 structure and function
- topo I is phosphorylated during mitosis at multiple sites, one of which enhances DNA relaxation activity in vitro and interaction with DNA in cells
- poly(ADP-ribose) targeting of topoisomerase I and ASF/SF2 functions may participate in the regulation of gene expression
- analysis of the ubiquitin-proteasome pathway for the repair of topoisomerase I-DNA covalent complexes
- Six amino acids from the Cre linker loop constitute the minimal length of a functional linker in human topoisomerase I.
- Top1 induces apoptotic nuclear fusion with death receptors
- transcription-induced degradation of Top1 is Brca1 dependent, suggesting a role for Brca1 in the repair or removal of transcription-blocking Top1-DNA cleavage complexes.
- catalytic activity of TOP1 is repressed by Par-4
- Disulfide cross-links reveal conserved features of DNA topoisomerase I architecture and a role for the N terminus in clamp closure
- The simulations show the complete abolishment, in the Thr729Lys mutant, of the protein communications between the C-terminal domain (where the active Tyr723 is located) and the linker domain, that plays an essential role in the control of DNA rotation.
- Thr729 is crucial for DNA binding by human DNA topoisomerase I (hTop1p).
- Mitochondrial topoisomerase I sites in the regulatory D-loop region of mitochondrial DNA are reported.
- Copy-number analysis of TOPI genes in frozen and FFPE DNAas of colorectal cancers is reported.