Recombinant E.Coli Holliday Junction Atp-Dependent Dna Helicase Ruva (RUVA) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-02932P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant E.Coli Holliday Junction Atp-Dependent Dna Helicase Ruva (RUVA) Protein (His-SUMO)

Beta LifeScience SKU/CAT #: BLC-02932P
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Product Overview

Description Recombinant E.Coli Holliday Junction Atp-Dependent Dna Helicase Ruva (RUVA) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb P0A809
Target Symbol RUVA
Synonyms ruvA; b1861; JW1850; Holliday junction ATP-dependent DNA helicase RuvA; EC 3.6.4.12
Species Escherichia coli (strain K12)
Expression System E.coli
Tag N-6His-SUMO
Target Protein Sequence MIGRLRGIIIEKQPPLVLIEVGGVGYEVHMPMTCFYELPEAGQEAIVFTHFVVREDAQLLYGFNNKQERTLFKELIKTNGVGPKLALAILSGMSAQQFVNAVEREEVGALVKLPGIGKKTAERLIVEMKDRFKGLHGDLFTPAADLVLTSPASPATDDAEQEAVAALVALGYKPQEASRMVSKIARPDASSETLIREALRAAL
Expression Range 1-203aa
Protein Length Full Length
Mol. Weight 38.1kDa
Research Area Others
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 The RuvA-RuvB complex in the presence of ATP renatures cruciform structure in supercoiled DNA with palindromic sequence, indicating that it may promote strand exchange reactions in homologous recombination. RuvAB is a helicase that mediates the Holliday junction migration by localized denaturation and reannealing. RuvA stimulates, in the presence of DNA, the weak ATPase activity of RuvB. Binds both single- and double-stranded DNA (dsDNA). Binds preferentially to supercoiled rather than to relaxed dsDNA.
Subcellular Location Cytoplasm. Note=In 15% of cell localizes to discrete nucleoid foci (probable DNA damage sites) upon treatment with mitomycin C (MMC) for 2 hours.
Protein Families RuvA family
Database References

Gene Functions References

  1. Regression of replication forks stalled by leading-strand template damage: both RecG and RuvAB catalyze regression, but RuvC cleaves the holliday junctions formed by RecG preferentially. PMID: 25138216
  2. These results suggest that RecQ acts upstream of RuvABC, RecG and XerC proteins, a finding that is compatible with its primary role in initiation of the RecF recombination pathway. PMID: 24036154
  3. RNA polymerase mutations reduce the synergism between priB and ruvABC. PMID: 22957744
  4. DNA fragmentation absolutely depends on both RecA-catalyzed homologous strand exchange and RuvABC-catalyzed Holliday junction resolution PMID: 22194615
  5. Role in converting the initial single-strand DNA-protein cleavage complex into a double-strand break prior to repair by homologous recombination. PMID: 20601468
  6. Study hypothesized that RuvAB catalyzes replication fork reversal in order to produce SOS(Con) expression. PMID: 20304994
  7. RuvA octamerization is essential for the full biological activity of RuvABC. PMID: 15556943
  8. RuvA is less mobile at a heterologous junction compared to a homologous junction, as two opposing DnaB pumps are required to mobilize RuvA over heterologous DNA. PMID: 16324713
  9. RuvABC is required to resolve junctions that arise during the repair of a subset of nonarresting lesions after replication has passed through the template PMID: 16895921
  10. The authors present here the isolation and characterization of ruvA and ruvB single mutants that are impaired for replication fork reversal at forks arrested by the inactivation of polymerase III, while they remain capable of homologous recombination. PMID: 18942176

FAQs

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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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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