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Storage
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Store the unopened product at 2 - 8° C. Protect from light. Do not use past
expiration date.
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Gene ID
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100101922 |
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Gene Symbol
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H2AFX |
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Synonym
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H2AFX; Histone H2AX |
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Species
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Porcine |
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Specificity
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This assay has high sensitivity and excellent specificity for detection of porcine Phospho-Histone H2AX (S139). No significant cross-reactivity or interference between porcine Phospho-Histone H2AX (S139) and analogues was observed. |
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Kit Components
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Assay plate (12 x 8 coated Microwells), Standard (Freeze dried), Biotin-antibody (60 x concentrate), HRP-avidin (20 x concentrate), Biotin-antibody Diluent, HRP-avidin Diluent, Sample Diluent, Wash Buffer (20 x concentrate), TMB Substrate, Stop Solution, Adhesive Strip (For 96 wells), Instruction manual |
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Notes
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Please contact our Technical Services with any questions regarding species reactivity |
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Standard Curve Range
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171.875 pg/ml - 11000 pg/ml |
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Sensitivity
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137.5 pg/ml |
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Inter Assay
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CV%<10% |
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Intra Assay
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CV%<8% |
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Assay Type
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Sandwich ELISA |
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Suitable Sample Type
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serum, plasma, tissue homogenates, cell lysate, cell culture medium. |
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Sample Volume
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50-100ul |
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Applications
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ELISA |
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Typical Data
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ELISA: Porcine Phospho-Histone H2AX (S139) ELISA Kit (Colorimetric) - These standard curves are provided for demonstration only. A standard curve should be generated for each set of samples assayed. |
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Background
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H2AFX (H2A histone family, member X) is one of several genes coding for histone H2A. In humans and other eukaryotes, the DNA is wrapped around histone-groups, consisting of core histones H2A, H2B, H3 and H4. Thus, the H2AX contributes to the nucleosome-formation and therefore the structure of DNA. H2AX becomes phosphorylated on serine 139, then called gamma-H2AX, as a reaction on DNA double-strand breaks (DSB). The kinases of the PI3-family (Ataxia telangiectasia mutated, ATR and DNA-PKcs) are responsible for this phosphorylation, especially ATM. The modification can happen accidentally during replication fork collapse or in the response to ionizing radiation but also during controlled physiological processes such as V(D)J recombination. Gamma-H2AX is a sensitive target for looking at DSBs in cells. The presence of gamma-H2AX by itself, however, is not the evidence of the DSBs. The role of the phosphorylated form of the histone in DNA repair is under discussion but it is known that because of the modification the DNA becomes less condensed, potentially allowing space for the recruitment of proteins necessary during repair of DSBs. Mutagenesis experiments have shown that the modification is necessary for the proper formation of ionizing radiation induced foci in response to double strand breaks, but is not required for the recruitment of proteins to the site of DSBs. |
