Analytical Data
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Gene name
ARX
- Application
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Alternative Names
ARX; ISSX; MRX29; MRX32; MRX33; MRX36; MRX38; MRX43; MRX54; MRXS1; PRTS; Mental Retardation,X-linked 54
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q96QS3
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Expression Region
Ser25~Asp246
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Molecular Weight
26kDa
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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
ARX (Aristaless Related Homeobox) is a transcription factor that plays a crucial role in embryonic development and is particularly important for the specification of neuronal and endocrine cells in the brain and pancreas. Mutations in the ARX gene have been associated with various genetic disorders, including intellectual disabilities, epilepsy, and developmental delays. The study of ARX and its associated protein functions has garnered significant interest in the fields of neuroscience and developmental biology, as understanding ARX's molecular mechanisms can provide insights into the pathogenesis of these conditions. Recent research has focused on the structure-function relationship of ARX, utilizing techniques such as protein purification and crystallography to investigate its conformational properties and interactions with DNA and other regulatory proteins. The re-engineering or "recombination" of ARX proteins, including the creation of ARX fusion proteins, has been employed to dissect specific domains responsible for its regulatory activities. These studies not only aim to elucidate the fundamental biological roles of ARX but also provide potential therapeutic avenues for targeting ARX-related disorders. As our understanding of ARX continues to evolve, it remains a pivotal subject of research for unraveling the complexities of neural development and its implications for human health.
