Analytical Data
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Gene name
ARID1A
- Application
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Alternative Names
ARID1A；BAF250；BAF250A；C1orf4；AT-rich interactive domain-containing Protein 1A
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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
O14497
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Expression Region
1216-1325aa
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AA Sequence
NTSDMMGRMSYEPNKDPYGSMRKAPGSDPFMSSGQGPNGGMGDPYSRAAG PGLGNVAMGPRQHYPYGGPYDRVRTEPGIGPEGNMSTGAPQPNLMPSNPD SGMYSPSRYP
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Molecular Weight
38 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
ARID1A (AT-rich interactive domain-containing protein 1A) is a crucial component of the SWI/SNF chromatin remodeling complex, playing a significant role in regulating gene expression and maintaining genomic integrity. Its dysfunction has been implicated in various human cancers, particularly ovarian clear cell carcinoma and endometrial carcinoma, where ARID1A mutations or loss of expression are frequently observed. The protein facilitates the remodeling of chromatin, influencing DNA accessibility and transcriptional activity. Research has highlighted that ARID1A mutations not only disrupt its role in chromatin dynamics but also lead to impaired cellular responses to DNA damage and stress. Consequently, understanding the molecular mechanisms underlying ARID1A functionality and its dysregulation in cancer is critical for the development of targeted therapies. Current studies have focused on elucidating the interaction networks involving ARID1A, its post-translational modifications, and the downstream effects on cell cycle regulation and apoptosis. As a result, ARID1A has garnered attention as a potential biomarker for cancer diagnosis and prognosis, as well as a promising target for innovative therapeutic strategies aimed at restoring its normal functions or compensating for its loss in tumor contexts.
