Human ATPase SWSAP1 Recombinant Protein N-6 His Tag Lyophilized from Innovative Research has been recombinantly produced in E. coli. This is a Lyophilized protein buffered in Lyophilized from a 0.2 um filtered solution of PBS, pH7.4. It is not recommended to reconstitute to a concentration less than 100UG/ml. Dissolve the lyophilized protein in ddH2O. with a purity of Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test..More Details: Species: Human Target: SWSAP1 Purity: Greater than 95% as determined by reducing SDS-PAGE.Endotoxin level less than 0.1 ng/ug (1 IEU/ug) as determined by LAL test. Source: E. coli Storage Conditions: Lyophilized protein should be stored at -20░C, though stable at room temperature for 3 weeks.Reconstituted protein solution can be stored at 4-7░C for 2-7 days.Aliquots of reconstituted samples are stable at -20░C for 3 months.

Additional Information:

SWSAP1 is a nucleus ATPase protein, interacts with ZSWIM7 and forms a functional complex. The complexs involved in homologous recombination repair and stabilizes each other. SWS1AP1 also interacts with RAD51, RAD51B, RAD51C, RAD51D and XRCC3. It involves in homologous recombination repair. ATPase is preferentially stimulated by single-stranded DNA and is involved in homologous recombination repair (HRR). SWSAP1 has a DNA-binding activity which is independent of its ATPase activity.This recombinant protein can be used for biological assays. For research use only. . At Innovative Research we provide reliable, consistent products that deliver reliable, consistent results.

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This material is sold for in-vitro use only for manufacturing and research. This material is not suitable for human or animal use. While we make every effort to ensure the safety of our products, we recommend handling any biological materials with standard precautions as if capable of spreading infectious disease. The statements herin are offered for informational purposes only to be used solely for your consideration, investigation, and verification.

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