Analytical Data
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Gene name
ASF1A
- Application
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Alternative Names
ASF1A；Histone chaperone ASF1A
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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
Q9Y294
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Expression Region
1-204aa
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AA Sequence
MAKVQVNNVVVLDNPSPFYNPFQFEITFECIEDLSEDLEWKIIYVGSAESEEYDQVLDSVLVGPVPAGRHMFVFQADAPNPGLIPDADAVGVTVVLITCTYRGQEFIRVGYYVNNEYTETELRENPPVKPDFSKLQRNILASNPRVTRFHINWEDNTEKLEDAESSNPNLQSLLSTDALPSASKGWSTSENSLNVMLESHMDCM
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Molecular Weight
50.0kDa
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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
Related Products
Protein Description
ASF1A, or Anti-Silencing Function 1A, is a crucial histone chaperone involved in various cellular processes, including DNA replication, repair, and transcription regulation. Recent studies have highlighted its importance in maintaining chromatin dynamics and epigenetic regulation. ASF1A interacts with histones to facilitate their deposition and removal during these processes, thereby influencing gene expression and genomic stability. Dysregulation of ASF1A has been associated with several diseases, including cancer, where altered histone metabolism can lead to abnormal cell proliferation and tumorigenesis. Research has shown that ASF1A plays a significant role in response to DNA damage, contributing to repair mechanisms that prevent genomic instability. Additionally, it has been implicated in various developmental processes and is essential for proper cell cycle progression. As a result, the production and characterization of recombinant ASF1A proteins have become an essential focus in understanding its structure-function relationships and biochemical properties. This involves exploring its interactions with other nuclear proteins and histones, which could elucidate its role in chromatin remodeling and the broader implications of its function in health and disease. The ongoing research in ASF1A is not only critical for basic biological understanding but also holds promise for therapeutic applications, especially in developing strategies for cancer treatment by targeting its pathways or modulating its activity. Thus, the study of recombinant ASF1A proteins represents a significant area of interest in cell biology and cancer research.
