Analytical Data
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Gene name
H2AFY
- Application
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Alternative Names
H2AFY；H2AFY；Core histone macro-H2A.1
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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
O75367
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Expression Region
2-372aa
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AA Sequence
MASMTGGQQMGRGHHHHHHGNLYFQGGEFSSRGGKKKSTKTSRSAKAGVI FPVGRMLRYIKKGHPKYRIGVGAPVYMAAVLEYLTAEILELAGNAARDNK KGRVTPRHILLAVANDEELNQLLKGVTIASGGVLPNIHPELLAKKRGSKG KLEAIITPPPAKKAKSPSQKKPVSKKAGGKKGARKSKKKQGEVSKAASAD STTEGTPADGFTVLSTKSLFLGQKLNLIHSEISNLAGFEVEAIINPTNAD IDLKDDLGNTLEKKGGKEFVEAVLELRKKNGPLEVAGAAVSAGHGLPAKF VIHCNSPVWGADKCEELLEKTVKNCLALADDKKLKSIAFPSIGSGRNGFP KQTAAQLILKAISSYFVSTMSSSIKTVYFVLFDSESIGIYVQEMAKLDAN
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Molecular Weight
43 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
H2AFY, also known as H2A.Z, is a variant of the traditional histone H2A that plays a critical role in the regulation of gene expression, chromatin structure, and DNA repair. It is particularly significant in the context of developmental biology and cellular differentiation, as its incorporation into nucleosomes can influence the accessibility of transcription factors to DNA. Research has shown that H2AFY is involved in various cellular processes, including the modulation of chromatin dynamics and the facilitation of specific transcriptional programs. Given its pivotal role, the study of recombinant H2AFY protein has gained prominence, allowing scientists to dissect its functions in greater detail. Recombinant techniques enable researchers to produce H2AFY in a controlled environment, paving the way for investigations into its structural properties and interactions with other chromatin-associated proteins. Such studies are crucial for understanding the broader implications of H2AFY in health and disease, including its potential involvement in cancer and other genetic disorders. By elucidating the mechanisms through which H2AFY influences chromatin architecture and gene regulation, researchers hope to uncover novel therapeutic targets and deepen our understanding of epigenetic regulation. In summary, the research on recombinant H2AFY not only sheds light on fundamental biological processes but also holds promise for the development of innovative strategies in disease management and gene therapy.
