Human X-Ray Repair Cross Complementing 5 (XRCC5) Protein

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Description
X-Ray Repair Cross Complementing 5 Protein is a recombinant Human protein expressed in E. coli.
Documents del producto
Product specifications
Category | Proteins and Peptides |
Immunogen Target | X-Ray Repair Cross Complementing 5 (XRCC5) |
Host | E. coli |
Origin | Human |
Conjugation | Unconjugated |
Observed MW | Molecular Weight: Calculated MW: 55.7 kDa Observed MW (SDS-PAGE): 56 kDa Concentration: Prior to lyophilization: 200 µg/ml Sequence Fragment: Val2-Ser460 Tag: N-terminal His tag |
Expression | Recombinant |
Purity | > 80% |
Size 1 | 10 µg |
Size 2 | 50 µg |
Size 3 | 100 µg |
Size 4 | 200 µg |
Size 5 | 500 µg |
Form | Lyophilized Reconstitute in ddH2O to a concentration of 0.1-1.0 mg/ml. Do not vortex. |
Tested Applications | WB, SDS-PAGE |
Buffer | Prior to lyophilization: 100 mM NaHCO<sub>3</sub>, 500 mM NaCl, pH 8.3, containing 1 mM EDTA, 1 mM DTT, 0.01% Sarcosyl, 5% Trehalose and Proclin-300. |
Availability | Shipped within 5-7 working days. |
Storage | Store at 2-8 °C for up to one month. Store at -80 °C for up to one year. Avoid repeated freeze/thaw cycles. |
Dry Ice | No |
Background | Protein XRCC5 |
Status | RUO |
Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
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The protein encoded by this gene is the 80-kilodalton subunit of the Ku heterodimer protein which is also known as ATP-dependant DNA helicase II or DNA repair protein XRCC5. Ku is the DNA-binding component of the DNA-dependent protein kinase, and it functions together with the DNA ligase IV-XRCC4 complex in the repair of DNA double-strand break by non-homologous end joining and the completion of V(D)J recombination events. This gene functionally complements Chinese hamster xrs-6, a mutant defective in DNA double-strand break repair and in ability to undergo V(D)J recombination. A rare microsatellite polymorphism in this gene is associated with cancer in patients of varying radiosensitivity.
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