Summary:
Recombinant human EXDL2 protein
Cat：P07408
| 【Derived From】： E.coli |
| 【Endotoxin】： Not measured |
| 【Amino Acid】： 148-497aa |
| 【Purity】： ≥85% by SDS-PAGE. |
| 【Name】： EXDL2 |
| 【Full Name】： exonuclease 3'-5' domain-like 2 |
| 【Uniprot】： Q9NVH0 |
| 【Gene ID】： 55218 |
| 【Mol Mass】： 38kDa |
| 【Application】： Immunology research |
| 【Purification】： NI-NTA affinity purification |
| 【Bioactive】： N0 |
| 【Tag】： With a 6×His tag at the N/C-terminus. |
| 【Concentration】： 1mg/ml by SDS-PAGE. |
Store:
| 【Reconstitution】： Reconstituted protein solution can be diluted with distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. (It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water.) |
| 【Storage】： Reconstituted protein solution can be stored at 4-7℃ for 1-2 weeks， stored at < -20℃ for 1 year. |
| 【Formulation】： Powder: Lyophilized from a 0.2 μm filtered solution of 2-8M Urea, 20mM Tris-HCl, 150mM NaCl, 1mM DTT, PH7.2-8.0. |
Background:
Exonuclease that has both 3'-5' exoribonuclease and exodeoxyribonuclease activities, depending on the divalent metal cation used as cofactor (PubMed:29335528, PubMed:31127291). In presence of Mg2+, only shows 3'-5' exoribonuclease activity, while it shows both exoribonuclease and exodeoxyribonuclease activities in presence of Mn2+ (PubMed:29335528, PubMed:31127291). Acts as an exoribonuclease in mitochondrion, possibly by regulating ATP production and mitochondrial translation (PubMed:29335528). Also involved in the response to DNA damage (PubMed:26807646, PubMed:31255466). Acts as 3'-5' exodeoxyribonuclease for double-strand breaks resection and efficient homologous recombination (PubMed:20603073, PubMed:26807646). Plays a key role in controlling the initial steps of chromosomal break repair, it is recruited to chromatin in a damage-dependent manner and functionally interacts with the MRN complex to accelerate resection through its 3'-5' exonuclease activity, which efficiently processes double-stranded
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