Recombinant E.Coli Atp-Dependent Dna Helicase Recg (RECG) Protein (His-SUMO)

Name: Recombinant E.Coli Atp-Dependent Dna Helicase Recg (RECG) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03884P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant E.Coli Atp-Dependent Dna Helicase Recg (RECG) 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	P24230
Target Symbol	RECG
Synonyms	recG; radC; b3652; JW3627; ATP-dependent DNA helicase RecG; EC 3.6.4.12
Species	Escherichia coli (strain K12)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MKGRLLDAVPLSSLTGVGAALSNKLAKINLHTVQDLLLHLPLRYEDRTHLYPIGELLPGVYATVEGEVLNCNISFGGRRMMTCQISDGSGILTMRFFNFSAAMKNSLAAGRRVLAYGEAKRGKYGAEMIHPEYRVQGDLSTPELQETLTPVYPTTEGVKQATLRKLTDQALDLLDTCAIEELLPPELSQGMMTLPEALRTLHRPPPTLQLSDLETGQHPAQRRLILEELLAHNLSMLALRAGAQRFHAQPLSANDTLKNKLLAALPFKPTGAQARVVAEIERDMALDVPMMRLVQGDVGSGKTLVAALAALRAIAHGKQVALMAPTELLAEQHANNFRNWFAPLGIEVGWLAGKQKGKARLAQQEAIASGQVQMIVGTHAIFQEQVQFNGLALVIIDEQHRFGVHQRLALWEKGQQQGFHPHQLIMTATPIPRTLAMTAYADLDTSVIDELPPGRTPVTTVAIPDTRRTDIIDRVHHACITEGRQAYWVCTLIEESELLEAQAAEATWEELKLALPELNVGLVHGRMKPAEKQAVMASFKQGELHLLVATTVIEVGVDVPNASLMIIENPERLGLAQLHQLRGRVGRGAVASHCVLLYKTPLSKTAQIRLQVLRDSNDGFVIAQKDLEIRGPGELLGTRQTGNAEFKVADLLRDQAMIPEVQRLARHIHERYPQQAKALIERWMPETERYSNA
Expression Range	1-693aa
Protein Length	Full Length
Mol. Weight	92.4kDa
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	Plays a critical role in recombination and DNA repair. Helps process Holliday junction intermediates to mature products by catalyzing branch migration. Has a DNA unwinding activity characteristic of a DNA helicase with 3'- to 5'- polarity. Unwinds branched duplex DNA (Y-DNA). Has a role in constitutive stable DNA replication (cSDR) and R-loop formation. Is genetically synergistic to RadA and RuvABC.
Protein Families	Helicase family, RecG subfamily
Database References	KEGG: ecj:JW3627 STRING: 316385.ECDH10B_3834

Gene Functions References

results provide mechanistic insights into the modes of interaction of RecG with the replication fork, suggesting a novel role of RecG in the repair of stalled DNA replication forks. PMID: 29432678
Data suggest that RecG and RuvABC catalyze alternative steps in DNA repair/recombination and collaborate to stabilize DNA during repair of double-strand DNA breaks; RecG may prevent DNA amplification at D-loops formed by recombination and at arrested replication forks. (RecG = RecG DNA helicase; Ruv = Holliday junction DNA helicase subunit) [REVIEW] PMID: 28155219
interaction occurs via the wedge domain of RecG and the intrinsically disordered linker (IDL) of SSB, in a manner similar to that of SH3 domains binding to PXXP motif-containing ligands in eukaryotic cells. PMID: 28078722
Once RecG has regressed the fork, it will dissociate leaving the now relaxed, Holliday junction-like DNA, available for further processing by enzymes such as RuvAB. [review] PMID: 25613916
RecG co-localises with sites of DNA replication in Escherichia coli. PMID: 24692661
Abolishing PriB leads to suppression of the recG null phenotype. PMID: 22957744
data are consistent with RecG and ssDNA exonucleases acting to limit PriA-mediated re-replication of the chromosome and the consequent generation of linear DNA branches that provoke recombination and delay chromosome segregation PMID: 20647503
The authors show that the extensive DnaA-independent stable DNA replication observed without RecG can lead to replication of any area of the chromosome. PMID: 19818016
allows repair of damaged replication forks to proceed without recourse to potentially mutagenic recombination PMID: 15516585
Data suggest that the processivity of RecG on branched DNA substrates is dependent on the ability of its wedge domain to establish strong binding at the branch point. PMID: 15695524
Inactivation of recG stimulates recombinant formation about five-fold PMID: 16257588
manner and timing of the interaction of RecG with DNA at stalled replication forks PMID: 17292398
RecG decreases the number of replication forks in UV-irradiated cells by limiting UV-induced, DnaA-independent initiation of replication. PMID: 19538444

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.