Analytical Data
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Gene name
h1f0-a
- Application
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Alternative Names
H1-SB H1E Histone H1(0)-1 Histone H5B XlH5B
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Species
Xenopus laevis
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P22845
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Expression Region
1-194aa
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Molecular Weight
37 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
H1F0-A, a member of the histone family, plays a crucial role in various cellular processes, including gene regulation, DNA repair, and chromatin organization. Its expression is tightly regulated and is associated with distinct biological events, such as cellular differentiation and responses to environmental stress. Research has indicated that abnormalities in H1F0-A expression can lead to various diseases, including cancer and developmental disorders. The study of H1F0-A as a recombinant protein holds significant potential for elucidating its functional mechanisms and interactions within the cellular environment. By producing H1F0-A in a controlled laboratory setting, researchers aim to investigate its structural properties, post-translational modifications, and specific binding affinities to different chromatin components. This research could provide insights into how H1F0-A contributes to the regulation of gene expression and the maintenance of genomic stability. Additionally, understanding the functional roles of H1F0-A could pave the way for novel therapeutic strategies targeting diseases associated with its dysregulation. Overall, the recombinant expression and characterization of H1F0-A is vital for advancing our knowledge of histone biology and its implications in health and disease.
