Analytical Data
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Gene name
Histone H2A
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简介
Histone H2A, an integral nucleosome component, forms the histone octamer with H2B, H3, and H4. This molecular spool, consisting of two H2A-H2B heterodimers and one H3-H4 heterotetramer, wraps around approximately 147 base pairs of DNA, organizing chromatin structure. The intricate histone-DNA association, especially with H2A, plays a vital role in regulating cellular processes like gene expression and DNA packaging. Histone H2A Protein, Xenopus laevis is the recombinant Xenopus laevis-derived Histone H2A protein, expressed by E. coli , with tag free.
- Application
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Alternative Names
h2ac14.L
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Species
Xenopus laevis
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q6AZJ8
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Expression Region
T17-L197
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Protein Length
Partial
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Molecular Weight
12.3 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
Histone H2A is a crucial component of the nucleosome, which forms the fundamental unit of chromatin and plays a vital role in packaging DNA within the cell nucleus. The study of H2A, particularly its variant forms, has gained considerable attention due to their significance in regulating gene expression and maintaining genomic stability. Research has shown that modifications, such as acetylation, methylation, and phosphorylation of H2A, can influence chromatin structure and function, thereby impacting cellular processes including DNA replication, repair, and transcription. Furthermore, the discovery of H2A variants, like H2A.Z and macroH2A, has revealed their unique roles in various biological contexts, such as stem cell differentiation, development, and responses to environmental stress. Investigating recombinant H2A proteins allows for a deeper understanding of their structural and functional properties, facilitating insights into the molecular mechanisms by which histones influence chromatin dynamics. This research is crucial for elucidating the complex interplay between histone modifications and cellular regulation, with implications for understanding diseases such as cancer, where dysregulation of histone dynamics is often observed. As such, recombinant Histone H2A proteins have become important tools in epigenetics and molecular biology, enabling researchers to dissect the intricate relationships between histone structure, modification, and cellular function.
