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AB63827

Recombinant E. coli RuvB protein (Active)

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Recombinant E. coli RuvB protein (Active) is a Escherichia coli K-12 Full Length protein, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE, ELISA, WB, FuncS.

View Alternative Names

b1860, JW1849, ruvB, Holliday junction branch migration complex subunit RuvB

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SDS-PAGE - Recombinant E. coli RuvB protein (Active) (AB63827)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant E. coli RuvB protein (Active) (AB63827)

SDS-PAGE analysis of Recombinant E. coli RuvB protein (ab63827).

SDS-PAGE - Recombinant E. coli RuvB protein (Active) (AB63827)
  • SDS-PAGE

Unknown

SDS-PAGE - Recombinant E. coli RuvB protein (Active) (AB63827)

SDS Page analysis of ab63827

Key facts

Purity

>90% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

FuncS, WB, SDS-PAGE, ELISA

applications

Biologically active

No

Accession

P0A812

Animal free

No

Carrier free

No

Species

Escherichia coli K-12

Storage buffer

pH: 6 - 8.5 Constituents: 50% Glycerol (glycerin, glycerine), 0.58% Sodium chloride, 0.158% Tris HCl, 0.0584% EDTA, 0.039% 2-Mercaptoethanol

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "ELISA": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "WB": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" }, "FuncS": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p>Functional studies in vitro; RuvA and RuvB form a complex that promotes Holidayjunction (a recombination intermediate) branch-migration by using ATP hydrolysis energy. RuvB also has ATPase activity which is stimulated by RuvA and DNA.</p>" } } }
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Product details

This protein can be used for:- 1) Studies on homologous recombination mechanism. 2) To make use of the motor protein function that specifically migrates the Holliday junction by forming a complex with RuvA (branch-migration protein).
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Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"P0A812","tags":[]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

RuvB also known as RuvB-like 1 and 2 (RUVBL1/RUVBL2) is a highly conserved ATP-dependent helicase with a molecular mass of roughly 51 kDa. This protein can unwind DNA a function that plays an essential role in DNA repair and recombination. It is expressed in various tissues across different species with high expression in rapidly dividing cells and tissues undergoing repair. RuvB forms hexameric or dodecameric rings which allow it to interact with other protein complexes and nucleic acids.
Biological function summary

The RuvB proteins participate in the regulation of essential cellular events. They integrate into larger multi-protein complexes such as the chromatin remodeling complex INO80 and the TIP60 complex which are involved in modulating nucleosome structure. In the context of chromatin remodeling RuvB helps regulate access to the DNA by other proteins and enzymes affecting transcription DNA repair and replication. These activities underline RuvB's role in maintaining genomic stability.

Pathways

The participation of RuvB in key regulatory pathways includes DNA damage response and transcription regulation. In the DNA damage repair pathway it collaborates with proteins like RAD51 and BRCA1 to resolve DNA breaks. Additionally in the transcriptional regulation pathway RuvB interacts with RNA Polymerase complexes and is implicated in the regulation of gene expression. These interactions illustrate how RuvB is important for cellular responses to various stimuli that require rapid changes in gene transcription profiles and maintenance of DNA integrity.

Mutations or dysregulation of RuvB can contribute to the development of cancer and neurological disorders. Cancer often involves RuvB in its chromatin remodeling role where altered RuvB function can lead to unchecked cell proliferation due to improper DNA repair and transcription. Furthermore in some neurological disorders abnormal interaction between RuvB and proteins like Huntingtin has been observed suggesting a link between RuvB function and the pathogenic mechanisms in Huntington’s disease. These associations highlight RuvB as a significant target for therapeutic research in oncology and neurobiology.
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Specifications

Form

Liquid

Additional notes

purified by methods such as chromatography

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General info

Function

The RuvABC complex is involved in recombinational repair of UV or chemically damaged DNA (PubMed : 6374379). The complex also plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR); RFR and homologous recombination required for UV light survival can be separated (PubMed : 16424908, PubMed : 18942176, PubMed : 9814711). This subunit has a weak ATPase activity that is inhibited by its ADP product; binds ADP better than ATP (PubMed : 2529252). Promotes Holliday junction (HJ) branch migration in conjunction with RuvA. Binds to HJ cruciform DNA; in the presence of RuvA, ATP and Mg(2+) the junction is dissociated. Hydrolyzable (d)NTPs can replace ATP but other analogs cannot (PubMed : 1608954, PubMed : 1617728, PubMed : 6374379, PubMed : 8393934). The RuvB hexamer acts as a pump, pulling DNA into and through the RuvAB complex (PubMed : 9078376). Can bypass UV-induced lesions (PubMed : 1617728) and physically cross-linked DNA strands (PubMed : 10662672), suggesting RuvB does not unwind large sections of DNA. RuvA gives specificity by binding to cruciform junctions, while the RuvB ATPase provides the motor force for branch migration; excess RuvB can promote branch migration in the absence of RuvA (PubMed : 10662672, PubMed : 1617728). In vitro the RuvA-RuvB complex has 5'-3' helicase activity that is ATP-dependent and works best on short dsDNA hybrids; 52 and 66-nucleotide (nt) pairs are easily displaced, hybrids greater than 140-nts are not (PubMed : 8433990). RuvA stimulates the weak ATPase activity of RuvB in the presence of DNA; HJ DNA stimulates ATPase about 10-fold (PubMed : 1435721, PubMed : 1833759, PubMed : 8393934).. An in vitro resolvase system that forms and processes HJ has been reconstituted with DNA substrates, RuvA, RuvB and RuvC. RuvA-RuvB increases the rate of strand exchange (branch migration), dissociates the RecA filament and allows RuvC to cleave in both orientations at the cruciform junction (PubMed : 10421637, PubMed : 9160752). HJ-RuvA-RuvB-RuvC complexes resolve Holliday junctions and also undergo branch migration, providing evidence for a coupled branch migration/HJ resolution reaction (PubMed : 10421637).

Sequence similarities

Belongs to the RuvB family.

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Product protocols

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Target data

The RuvABC complex is involved in recombinational repair of UV or chemically damaged DNA (PubMed : 6374379). The complex also plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR); RFR and homologous recombination required for UV light survival can be separated (PubMed : 16424908, PubMed : 18942176, PubMed : 9814711). This subunit has a weak ATPase activity that is inhibited by its ADP product; binds ADP better than ATP (PubMed : 2529252). Promotes Holliday junction (HJ) branch migration in conjunction with RuvA. Binds to HJ cruciform DNA; in the presence of RuvA, ATP and Mg(2+) the junction is dissociated. Hydrolyzable (d)NTPs can replace ATP but other analogs cannot (PubMed : 1608954, PubMed : 1617728, PubMed : 6374379, PubMed : 8393934). The RuvB hexamer acts as a pump, pulling DNA into and through the RuvAB complex (PubMed : 9078376). Can bypass UV-induced lesions (PubMed : 1617728) and physically cross-linked DNA strands (PubMed : 10662672), suggesting RuvB does not unwind large sections of DNA. RuvA gives specificity by binding to cruciform junctions, while the RuvB ATPase provides the motor force for branch migration; excess RuvB can promote branch migration in the absence of RuvA (PubMed : 10662672, PubMed : 1617728). In vitro the RuvA-RuvB complex has 5'-3' helicase activity that is ATP-dependent and works best on short dsDNA hybrids; 52 and 66-nucleotide (nt) pairs are easily displaced, hybrids greater than 140-nts are not (PubMed : 8433990). RuvA stimulates the weak ATPase activity of RuvB in the presence of DNA; HJ DNA stimulates ATPase about 10-fold (PubMed : 1435721, PubMed : 1833759, PubMed : 8393934).. An in vitro resolvase system that forms and processes HJ has been reconstituted with DNA substrates, RuvA, RuvB and RuvC. RuvA-RuvB increases the rate of strand exchange (branch migration), dissociates the RecA filament and allows RuvC to cleave in both orientations at the cruciform junction (PubMed : 10421637, PubMed : 9160752). HJ-RuvA-RuvB-RuvC complexes resolve Holliday junctions and also undergo branch migration, providing evidence for a coupled branch migration/HJ resolution reaction (PubMed : 10421637).
See full target information ruvB

Additional targets

RuvB
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