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Recombinant Escherichia coli DNA topoisomerase 1 (topA), partial

Recombinant Escherichia coli DNA topoisomerase 1 (topA), partial

Code	CSB-YP024056ENV
MSDS	MSDS
Size	Pls inquire
Source	Yeast
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Code	CSB-EP024056ENV
MSDS	MSDS
Size	Pls inquire
Source	E.coli
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Code	CSB-EP024056ENV-B
MSDS	MSDS
Size	Pls inquire
Source	E.coli
Conjugate	Avi-tag Biotinylated E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.
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Code	CSB-BP024056ENV
MSDS	MSDS
Size	Pls inquire
Source	Baculovirus
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Code	CSB-MP024056ENV
MSDS	MSDS
Size	Pls inquire
Source	Mammalian cell
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Product Details
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Customer Reviews and Q&A
Target Background

Product Details

Purity

>85% (SDS-PAGE)

Target Names

topA

Uniprot No.

P06612

Alternative Names

topA; supX; b1274; JW1266; DNA topoisomerase 1; EC 5.6.2.1; DNA topoisomerase I; Omega-protein; Relaxing enzyme; Swivelase; Untwisting enzyme

Species

Escherichia coli (strain K12)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Customer Reviews and Q&A

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Target Background

Function

Releases the supercoiling and torsional tension of DNA, which is introduced during the DNA replication and transcription, by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by the catalytic tyrosine of the enzyme, resulting in the formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 3'-OH DNA strand. The free DNA strand then undergoes passage around the unbroken strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 3'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone.

Gene References into Functions

the CyaA(N600Y) mutant has a transcriptome indicative of increased CRP activity, pointing to an unknown role for CyaA and / or cAMP in gene expression..We show that the large scale transcriptomic changes in the topoisomerase I (FusA(A608E)-TopA(S180L)) mutant likely result from increased negative supercoiling in the cell. PMID: 29046437
Escherichia coli RecA physically interacts with topoisomerase I to modulate the chromosomal DNA supercoiling. PMID: 27001450
Structural study shows how the C-terminal domains of E. coli topoisomerase I bind single-stranded DNA to recognize the accumulation of negative supercoils in duplex DNA. PMID: 26490962
Antimicrobial susceptibility and SOS-dependent increase in mutation frequency are impacted by Escherichia coli topoisomerase I C-terminal point mutation. PMID: 26248366
Data indicate that transcription-coupled DNA supercoiling (TCDS) in topoisomerase I deficient (topA) is dependent on promoter strength. PMID: 23201416
Topoisomerase I relaxes DNA in slow processive runs but with short pauses before runs. PMID: 22923519
These data show unambiguously that Escherichia coli cells are not viable in the absence of DNA topoisomerase I without the presence of compensatory mutations. PMID: 22373098
essential function is related to transcription elongation, to inhibition of R-loop formation and to allowing the synthesis of full-length mRNAs PMID: 15458416
E. coli strains bearing topA mutations, introduced into the strains by DNA-mediated gene replacement, are viable at 37 or 42 degrees C without any compensatory mutations PMID: 15522872
analysis of topoisomerase I DNA cleavage activity PMID: 16159875
Catalytic roles of the conserved lysine and serine found at the active site of DNA topoisomerase I. PMID: 16582104
in response to oxidative stress, Fis binds the promoter region of topA PMID: 17233826
DNA of topA null mutants became relaxed rather than hypernegatively supercoiled following depletion of RNase HI activity. PMID: 18554330
The Asp-to-Asn substitutions at the TOPRIM domain residues can selectively decrease Mg(2+) binding affinity with minimal disruption of the active-site geometry, leading to trapping of the covalent complex with cleaved DNA and causing bacterial cell death. PMID: 19013470