Product Details

Purity

>85% (SDS-PAGE)

Target Names

XRS2

Uniprot No.

P33301

Alternative Names

XRS2; YDR369C; D9481.13; DNA repair protein XRS2

Species

Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)

Protein Length

Partial

Tag Info

Tag type will be determined during the manufacturing process.

The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.

Form

Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.

Buffer before Lyophilization

Tris/PBS-based buffer, 6% Trehalose, pH 8.0

Reconstitution

We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.

Troubleshooting and FAQs

Protein FAQs

Storage Condition

Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.

Shelf Life

The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.

Lead Time

Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.

Notes

Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Datasheet

Please contact us to get it.

Target Background

Function

During meiosis is involved in homologous recombination and during vegetative growth it is necessary for DNA repair. It probably regulates the 5'-3' exonuclease degradation of double strand breaks either at the initiation stage or a later stage.

Gene References into Functions

Xrs2 dependent and independent functions of the Mre11-Rad50 complex orchestrating the cellular response to double-strand DNA breaks have been described. PMID: 27746018
The Saccharomyces cerevisiae Mre11-Rad50-Xrs2 complex promotes trinucleotide repeat expansions independently of homologous recombination. PMID: 27173583
Phosphorylation sites on Xrs2 that are required for MMS resistance were identified. PMID: 27017623
Mre11 recruits conjugated SUMO moieties to facilitate the assembly and function of the Mre11-Rad50-Xrs2 complex. PMID: 26743002
the Xrs2 FHA domain and Tel1 kinase work in a coordinated manner to maintain DSB repair fidelity. PMID: 26990569
the mechanisms of DNA end resection in Saccharomyces cerevisiae, which includes short-range resection by Mre11-Rad50-Xrs2 and Sae2, as well as processive long-range resection by Sgs1-Dna2 or Exo1 pathways. PMID: 26231213
Data suggest that the major function of Sae2 in response to DNA double-strand breaks (DSBs) is to actively remove Mre11-Rad50-Xrs2 from break ends and prevent Rad53 in response to DSBs. PMID: 25831494
To our surprise, genes encoding the Mre11-Rad50-Xrs2 (MRX) complex, which are also required for homologous recombination, are epistatic to TLS mutations PMID: 25343618
Sae2 promotes dsDNA-specific endonuclease activity by the Mre11 subunit within the Mre11-Rad50-Xrs2 (MRX) complex PMID: 25231868
Processing of DNA double-stranded breaks and intermediates of recombination and repair by Saccharomyces cerevisiae Mre11 and its stimulation by Rad50, Xrs2, and Sae2 proteins. PMID: 23443654
A pivotal role for the MRX (Mre11, Rad50, Xrs2) complex for fork integrity at replication forks. PMID: 23376930
interaction with Xrs2 may enable Pch2 to remodel chromosome structure adjacent to the site of a DSB and thereby promote accessibility of Hop1 to the Tel1 kinase PMID: 22072981
a direct role for the Mre11-Rad50-Xrs2 complex in the base excision repair process, which contributes to resistance against base-damaging agents and to the avoidance of mutations PMID: 20040573
total amount of Xrs2 protein is a critical determinant for the function of the Mre11/Rad50/Xrs2 complex especially with regard to telomere maintenance and meiotic DSB formation PMID: 15716496
confirmed that signal joint formation in yeast is dependent on the same Mre11p-Rad50p-Xrs2p (MRX) complex factors known to be required in mammalian cells PMID: 15757898
MRX (Mre11/Rad50/Xrs2) is not required for the intra-S-phase checkpoint in response to DNA alkylation damage, but is required in the presence of double-stranded DNA breaks PMID: 15970664
The Mre11/Rad50/Xrs2 (MRX) complex is essential for joining of incompatible ends by non-homologous end-joining during DNA repair. PMID: 16043424
Individual and combined deletions of the Yku80 C terminus and the Xrs2 forkhead-associated (FHA) domain were shown to block nonhomologous end joining. PMID: 16314503
expression of EcoRI activated the G1 and intra-S phase checkpoints in a MRX- and Mec1-dependent, but Tel1-independent manner. PMID: 16879433
Data show that the Saccharomyces cerevisiae MRX complex, or its subunits Mre11/Rad50/Xrs2, prefer G-quadruplex DNA much more than telomeric single-stranded or double-stranded DNA, implicating the possible existence of this DNA structure in vivo. PMID: 17698079
Recombinant Sae2 binds DNA and exhibits endonuclease activity on single-stranded DNA independently of Mre11/Rad50 complexes, but hairpin DNA structures are cleaved cooperatively in the presence of Mre11/Rad50 or Mre11/Rad50/Xrs2. PMID: 18042458
Forkhead-associated domain of yeast Xrs2, a homolog of human Nbs1, promotes nonhomologous end joining through interaction with a ligase IV partner protein, Lif1. PMID: 18458108
the Xrs2-Lif1 interaction depends on Xrs2 FHA residues (R32, S47, R48, and K75) analogous to those known in other proteins to contact phosphorylated threonines PMID: 18832348

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Database Links

KEGG: sce:YDR369C

STRING: 4932.YDR369C

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Recombinant Saccharomyces cerevisiae DNA repair protein XRS2 (XRS2), partial

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