Analytical Data
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Gene name
ARHI
- Application
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Alternative Names
GTP-binding protein Di-Ras3; DIRAS3; ARHI; NOEY2; RHOI
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Species
Human
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Source
HEK293
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Tag
N-mFc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O95661
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Expression Region
M1-K225
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Protein Length
Full Length of Mature Protein
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Molecular Weight
62 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
Related Products
Protein Description
ARHI (also known as DIRAS3) is a member of the Ras superfamily of GTPases and serves as a tumor suppressor gene, primarily studied in the context of cancer biology. Its expression is frequently downregulated in various malignancies, including ovarian and breast cancers, where it is implicated in the regulation of cell growth, apoptosis, and cellular differentiation. Research indicates that ARHI functions by inhibiting the signaling pathways associated with oncogenesis, thereby contributing to the control of cell proliferation and survival. The recombinant production of ARHI protein has garnered significant interest as it allows for the exploration of its functional roles, potential therapeutic applications, and the mechanisms by which it exerts its tumor-suppressive effects. Understanding the structural and functional properties of ARHI through recombinant techniques can illuminate its interactions with other cellular pathways and help identify its potential as a biomarker for cancer diagnosis and treatment. Consequently, the study of ARHI recombinant proteins not only enhances our understanding of tumor suppressor mechanisms but also holds promise for the development of novel cancer therapies that exploit its regulatory capabilities.
