Recombinant E.Coli Dna Helicase Ii (UVRD)

Name: Recombinant E.Coli Dna Helicase Ii (UVRD)
Brand: Beta LifeScience
SKU: BLC-03840P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Escherichia coli (strain K12) uvrD.

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

Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant E.Coli Dna Helicase Ii (UVRD) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P03018
Target Symbol	UVRD
Synonyms	uvrD; mutU; pdeB; rad; recL; b3813; JW3786; DNA helicase II; EC 3.6.4.12
Species	Escherichia coli (strain K12)
Expression System	E.coli
Tag	Tag-Free
Target Protein Sequence	MDVSYLLDSLNDKQREAVAAPRSNLLVLAGAGSGKTRVLVHRIAWLMSVENCSPYSIMAVTFTNKAAAEMRHRIGQLMGTSQGGMWVGTFHGLAHRLLRAHHMDANLPQDFQILDSEDQLRLLKRLIKAMNLDEKQWPPRQAMWYINSQKDEGLRPHHIQSYGNPVEQTWQKVYQAYQEACDRAGLVDFAELLLRAHELWLNKPHILQHYRERFTNILVDEFQDTNNIQYAWIRLLAGDTGKVMIVGDDDQSIYGWRGAQVENIQRFLNDFPGAETIRLEQNYRSTSNILSAANALIENNNGRLGKKLWTDGADGEPISLYCAFNELDEARFVVNRIKTWQDNGGALAECAILYRSNAQSRVLEEALLQASMPYRIYGGMRFFERQEIKDALSYLRLIANRNDDAAFERVVNTPTRGIGDRTLDVVRQTSRDRQLTLWQACRELLQEKALAGRAASALQRFMELIDALAQETADMPLHVQTDRVIKDSGLRTMYEQEKGEKGQTRIENLEELVTATRQFSYNEEDEDLMPLQAFLSHAALEAGEGQADTWQDAVQLMTLHSAKGLEFPQVFIVGMEEGMFPSQMSLDEGGRLEEERRLAYVGVTRAMQKLTLTYAETRRLYGKEVYHRPSRFIGELPEECVEEVRLRATVSRPVSHQRMGTPMVENDSGYKLGQRVRHAKFGEGTIVNMEGSGEHSRLQVAFQGQGIKWLVAAYARLESV
Expression Range	1-720aa
Protein Length	Full Length
Mol. Weight	82.0 kDa
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	A helicase with DNA-dependent ATPase activity. Unwinds DNA duplexes with 3' to 5' polarity with respect to the bound strand. Initiates unwinding more efficiently from a nicked substrate than ds duplex DNA. Involved in the post-incision events of nucleotide excision repair and methyl-directed mismatch repair, and probably also in repair of alkylated DNA.
Protein Families	Helicase family, UvrD subfamily
Database References	KEGG: ecj:JW3786 STRING: 316385.ECDH10B_4005

Gene Functions References

Large domain movements upon UvrD dimerization and helicase activation has been reported. PMID: 29087333
Results show that UvrD monomer translocation rate depends on the single-stranded DNA base composition, even in the absence of any predicted basepairing within the nucleic acid. Translocation is faster on single-stranded DNA-containing pyrimidines and slower on ssDNA-containing purines PMID: 28978435
these data reveal that UvrD exhibits two distinct types of unwinding activity regulated by its stoichiometry. Furthermore, two UvrD conformational states, termed "closed" and "open," correlate with movement toward or away from the DNA fork. PMID: 25883359
The unwinding processivity is increased in the UvrD303 mutant. PMID: 24798324
UvrD binds RNA polymerase during transcription elongation, using its helicase/translocase activity, forces RNA polymerase to slide backward along DNA; UvrD exposes DNA lesions, allowing nucleotide excision repair enzymes to gain access to sites of damage PMID: 24402227
These results suggest that UvrD pauses more frequently during translocation at low ATP but with little futile ATP hydrolysis. PMID: 22342931
The anti-thymineless death role of UvrD. PMID: 21705756
crystal structure of an apo form of UvrD in which the 2B sub-domain is in an "open" state that differs by 160 degrees rotation of the 2B sub-domain PMID: 21704638
Although a 3'-ssDNA partial duplex provides a high-affinity site for a uvrD monomer, the study shows that a monomer also binds with specificity to DNA junctions possessing a 5'-ssDNA flanking region and can initiate translocation from this site. PMID: 20877334
UvrD has a critical role in the processing of DNA-protein cross-links PMID: 20444702
UvrD monomers translocate in discrete steps with an average kinetic step-size, m=3.68 nt step(-1), a translocation rate constant, kt=51.3 steps s(-1), with a processivity corresponding to an average translocation distance of 2400 nt before dissociation PMID: 15561144
mutational analysis of a thermostable UvrD helicase PMID: 15955821
acts by removing RecA or a RecA-made structure, allowing replication fork reversal PMID: 16135232
UvrD helicase is essential for Tus removal during recombination-dependent replication restart from Ter sites. PMID: 17020578
Role of UvrD on RecET-mediated illegitimate recombination. PMID: 17038801
Our results suggest that macroscopic rate of UvrD monomer translocation is not limited by each ATPase cycle but by a slow step (pause) in each translocation cycle that occurs after four to five rapid 1 nt translocation steps. PMID: 17499041
Results show that the anti-RecA action of UvrD at blocked forks reflects two different activities of this enzyme. PMID: 17641684
The multiform patterns of unwinding bursts and the distributions of the off-times favour the mechanism that UvrD unwinds DNA as a dimer. PMID: 19008855

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.