Recombinant Human Dna Topoisomerase 1 (TOP1) Protein (His&Myc)

Name: Recombinant Human Dna Topoisomerase 1 (TOP1) Protein (His&Myc)
Brand: Beta LifeScience
SKU: BLC-00501P
Price: 299.0 USD
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Human Dna Topoisomerase 1 (TOP1) Protein (His&Myc) is produced by our Baculovirus expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P11387
Target Symbol	TOP1
Synonyms	(DNA topoisomerase I)
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	N-10His&C-Myc
Target Protein Sequence	NKKKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPENVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNEEKNIITNLSKCDFTQMSQYFKAQTEARKQMSKEEKLKIKEENEKLLKEYGFCIMDNHKERIANFKIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDGQEYVVEFDFLGKDSIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYNASITLQQQLKELTAPDENIPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKLNYLDPRITVAWCKKWGVPIEKIYNKTQREKFAWAIDMADEDYEF
Expression Range	191-765aa
Protein Length	Partial
Mol. Weight	72.2 kDa
Research Area	Cancer
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	Releases the supercoiling and torsional tension of DNA 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-(3'-phosphotyrosyl)-enzyme intermediate and the expulsion of a 5'-OH DNA strand. The free DNA strand then rotates around the intact phosphodiester bond on the opposing strand, thus removing DNA supercoils. Finally, in the religation step, the DNA 5'-OH attacks the covalent intermediate to expel the active-site tyrosine and restore the DNA phosphodiester backbone. Regulates the alternative splicing of tissue factor (F3) pre-mRNA in endothelial cells. Involved in the circadian transcription of the core circadian clock component ARNTL/BMAL1 by altering the chromatin structure around the ROR response elements (ROREs) on the ARNTL/BMAL1 promoter.
Subcellular Location	Nucleus, nucleolus. Nucleus, nucleoplasm. Note=Diffuse nuclear localization with some enrichment in nucleoli. On CPT treatment, cleared from nucleoli into nucleoplasm. Sumoylated forms found in both nucleoplasm and nucleoli.
Protein Families	Type IB topoisomerase family
Database References	HGNC: 11986 OMIM: 126420 KEGG: hsa:7150 STRING: 9606.ENSP00000354522 UniGene: PMID: 30060749 Results from a study on gene expression variability markers in early-stage human embryos shows that TOP1 is a putative expression variability marker for the 3-day, 8-cell embryo stage. PMID: 26288249 High TOP1 expression is associated with aggressive tumor phenotype in breast cancer. PMID: 26959889 Ru/Fe bimetallic complexes: Synthesis, characterization, cytotoxicity and study of their interactions with DNA/HSA and human topoisomerase IB. PMID: 29107586 two regions of topoisomerase I, the N-terminal and the linker domains, were critical for subnuclear localization of the enzyme. The linker domain and the distal region of the N-terminal domain directed topoisomerase I to the nucleolus, whereas the remaining region of the N-terminal domain was responsible for the nucleoplasmic localization. PMID: 27428351 High TOP1 expression is associated with Colorectal Cancers. PMID: 28870917 HMGA2 potentiates the clinically important topoisomerase I inhibitor irinotecan/SN-38 in trapping the enzyme in covalent DNA-complexes, thereby attenuating transcription. PMID: 27587582 IMMP2L transcription requires Topoisomerase I in human primary astrocytes PMID: 27932244 This work identifies ADP-ribose polymers as key determinant for regulating Top1 subnuclear dynamics. PMID: 27466387 copper(II) thiosemicarbazone complex may hit human topoisomerase IB and that metal coordination can be useful to improve cytotoxicity of this versatile class of compounds PMID: 27431056 High prevalence of anti-topoisomerase I antibody positivity was found among Thai systemic sclerosis patients and this was associated with a high frequency of hand deformity, ACA negativity, a short duration of pulmonary fibrosis in diffuse cutaneous and a lower frequency of Raynaud's phenomenon in limited cutaneous subsets. PMID: 25293362 These findings reveal BAZ1B as a key facilitator of topoisomerase I function during DNA replication that affects the response of cancer cells to topoisomerase I inhibitors. PMID: 27050524 Results identified TOP1 gene copy gain, a loss of chromosome 20, and new yet unreported TOP1 mutations (R364K and G717R) in close proximity to the SN-38 binding site conferring colon cancer cells resistance to the drug. PMID: 27029323 the highest expression of GGH and EGFR was noted in the left-sided colon; the highest expression of DHFR, FPGS, TOP1 and ERCC1 was noted in the rectosigmoid, whereas TYMP expression was approximately equivalent in the right-sided colon and rectum PMID: 26676887 We found that the resistant cell lines showed 7-100 fold increased resistance to SN-38 but remained sensitive to docetaxel and the non-camptothecin Top1 inhibitor LMP400 PMID: 26801902 Data show that the single-molecule supercoil relaxation assay is a sensitive method to elucidate the detailed mechanisms of type IB topoisomerase (Top1) inhibitors and is relevant for the cellular efficacy of Top1 inhibitors. PMID: 26351326 TOP1 bound at promoters was discovered to become fully active only after pause-release. This transition coupled the phosphorylation of the carboxyl-terminal-domain (CTD) of RNA polymerase II (RNAPII) with stimulation of TOP1 above its basal rate, enhancing its processivity. PMID: 27058666 Data show that inhibition of DNA-dependent protein kinase catalytic subunit (DNA-PK) prevents type I DNA topoisomerase (Top1) degradation and proteasome activity in camptothecin (CPT)-treated quiescent WI38 cells. PMID: 26578593 NO-induced down-regulation of topoisomerase I protein. PMID: 26540186 b-ELE could inhibit the proliferation of HepG-2 cells and interfere with the expression and activity of TOPO I and TOPO IIa PMID: 26221582 Acridine derivatives inhibited DNA topoisomerases I and II and prevented proliferation of HL-60 cells. PMID: 25960253 Topoisomerase-1 and -2A gene copy numbers are elevated in mismatch repair-proficient colorectal cancers. PMID: 25777966 Cinobufacini inhibited the proliferation of the HepG-2 cells induced apoptosis in a dose- and time-dependent manner and downregulated the mRNA and protein expression levels of TOPO I and TOPO II PMID: 25815590 YB-1 serves as an intracellular promoter of TOPO1 catalytic activity that enhances camptothecin sensitivity through its direct interaction with TOPO1. PMID: 25539742 We here report that a substantial number of patients with bile duct or pancreatic cancer have increased TOP1 copy number and increased TOP1/centromere-20 ratio. PMID: 25615400 Results show that TOP1 gene is amplified in a subset of breast cancer patients suggesting the gene as a potential biomarker for response to treatment with Top1 inhibitors. PMID: 25855483 Results show that camptothecin resistance status of colorectal cancer cells depend on the phosphorylation of TOP1 and the presence of CD44. PMID: 24960044 varying expression levels of TOP1 and TDP1 polypeptides in multiple colorectal cancer cell lines and in clinical colorectal cancer samples, are reported. PMID: 25522766 CCR6 SNPs are a risk factor for presence of anti-topoisomerase I antibodies in systemic sclerosis. PMID: 26314374 ERCC1-XPF participates in DNA repair of the Top1-DNA damage complex. PMID: 26025908 both TOP1 and TDP1 were upregulated in the tumor tissue compared to the adjacent non-tumor tissue in non-small cell lung cancer tissue PMID: 25987486 mutations at the hydrophobic or charged residues of the putative polymer binding sites do not interfere with the ability of poly(ADP-ribose) to antagonize the antitumor activity of topoisomerase I poisons. PMID: 25227992 No TOP1 copy number changes were found in patients with de novo diffuse large B-cell lymphoma or relapsed DLBCL treated with chemotherapy regimens including TOP2-targeting drugs. PMID: 25931012 Mutation of Gly717Phe in human topoisomerase 1B has an effect on enzymatic function, reactivity to the camptothecin anticancer drug and on the linker domain orientation PMID: 25910424 Top1 cleavage events generate short deletions; Top1 also promotes nick religation at rNMP sites PMID: 25887397 analysis of how human and yeast DNA topoisomerase I domain interactions impact enzyme activity and sensitivity to camptothecin PMID: 25795777 Study describes a molecular mechanism that operates at functional androgen-regulated enhancers and identify DNA topoisomerase I as a critical DNA-nicking enzyme involved in the process of cell-specific, ligand-driven enhancer activation. PMID: 25619691 The combination of Top1 inhibitors with VE-821 inhibited the phosphorylation of ATR and Chk1. PMID: 25269479 DNA topoisomerases I and II are involved in initiating APH-induced common fragile site breakage at RET PMID: 24040417 Collectively, these findings suggest that the combinatorial inhibition of MET and Top1 is a potentially efficacious treatment strategy for Small cell lung cancer . PMID: 24327519 our data show for the first time that HIF-1alpha is strongly correlated with resistance to topoisomerase I inhibitors in hepatocellular carcinoma. PMID: 24362462 Analysis of the dynamical properties of DNA topoisomerase 1B bound to the more biologically relevant supercoiled substrate reveals an increased number of protein-DNA interactions and, most strikingly, the presence of a secondary protein-DNA binding site. PMID: 25056319 homologous recombination seems relevant especially for Top1 and, to a lesser extent, for Top2 inhibitors. We also found and discuss differential pathways among Top1 inhibitors and Top2 inhibitors PMID: 24130054 key factors in a molecular pathway connecting Top1 inhibition and human HIF-1alpha protein regulation and activity, widening the biologic and molecular activity of camptothecin PMID: 24252850 [review] Telangiectasia and anti-CENP or anti-topo I antibodies in the presence of Raynaud's phenomenon and proximal skin thickening increase the sensitivity of a very early diagnosis of systemic sclerosis from 57% to 97%. PMID: 24461384 This property facilitates the deprotonation of the 5' DNA end, suggesting that this is the limiting step in the topoisomerase religation mechanism. PMID: 23368812 These results suggest that topo I is a novel target of erlotinib and a combination of TKIs with topo I inhibitors may be an effective treatment for breast cancer. PMID: 24399039 Critical endogenous pathogenic lesions are associated with neurodegenerative syndromes arising from aberrant TOP-1 DNA. PMID: 24793032 A fully functional linker is required to confer camptothecin sensitivity to topoisomerase I. PMID: 24004603 MiR-23a could directly bind to 3'untranslated region of TOP1 mRNA, and suppress the corresponding protein expression. PMID: 24103454

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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