Analytical Data
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Gene name
H2AFX
- Application
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Alternative Names
H2AFX；H2AFX；Histone H2AX
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P16104
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Expression Region
1-143aa
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AA Sequence
MSGRGKTGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGHYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTSATVGPKAPSGGKKATQASQEY
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Molecular Weight
46.7 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
H2AFX, a variant of histone H2A, plays a critical role in the cellular response to DNA damage and chromatin remodeling. Its phosphorylation at serine 139 is a key event in the formation of gamma-H2AX, which serves as a marker for double-strand breaks in DNA. This modification facilitates the recruitment of DNA repair proteins to the sites of damage, thereby playing a vital role in maintaining genomic stability. Research on H2AFX recombination proteins has gained momentum due to their implications in various fields, including cancer biology, aging, and neurodegenerative disorders. Understanding the mechanisms by which H2AFX and its phosphorylated forms coordinate DNA repair processes could yield insights into tumorigenesis and treatment resistance in cancers. Moreover, the utilization of recombinant H2AFX proteins in in vitro assays provides a valuable tool for dissecting the complex interactions involved in DNA damage response pathways. Consequently, studies focusing on the structure, regulation, and functional characterization of H2AFX recombinant proteins are essential for advancing our knowledge of chromatin biology and its impact on cellular physiology. This research not only contributes to basic science but also has potential therapeutic implications, as targeting the pathways involving H2AFX may enhance the efficacy of cancer treatment strategies that exploit DNA damage.
