Analytical Data
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Gene name
H4
- Application
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Alternative Names
H4；H4/A；H4FA；HIST1H4A；Histone H4
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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
P62805
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Expression Region
2-103aa
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AA Sequence
SGRGKGGKGLGKGGAKRHRKVLRDNIQGITKPAIRRLARRGGVKRISGLI YEETRGVLKVFLENVIRDAVTYTEHAKRKTVTAMDVVYALKRQGRTLYGF GG
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Molecular Weight
12 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
The H4 histone protein, a crucial component of the nucleosome, plays a vital role in the regulation of chromatin structure and gene expression. Histone H4, along with other histones, forms octamers around which DNA winds, creating the fundamental unit of chromatin. Research into H4 recombinant proteins has gained significance as scientists seek to understand the intricate mechanisms of epigenetic regulation and chromatin dynamics. The post-translational modifications of histones, including H4, such as acetylation, methylation, and phosphorylation, have been linked to various cellular processes, including transcriptional activation and repression, DNA repair, and replication. Recombinant H4 proteins allow for detailed studies of these modifications, enabling researchers to dissect their functional implications in cellular health and disease. Moreover, such studies are integral in fields like cancer research, where aberrant histone modification patterns are often observed. Advances in recombinant DNA technology have facilitated the production of H4 in various forms, providing tools for in vitro assays and structural studies, which are instrumental in the development of potential therapeutic strategies targeting epigenetic alterations. Overall, the investigation of H4 recombinant proteins not only enhances our understanding of fundamental biological processes but also paves the way for novel approaches in treating diseases associated with epigenetic dysregulation.
