Analytical Data
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Gene name
ARHGEF11
- Application
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Alternative Names
ARHGB_HUMAN; ARHGEF 11; ARHGEF11; DKFZp667F1223
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O15085
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Expression Region
651-750aa
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AA Sequence
RSESLKGREEMKRSRKAENVPRSRSDVDMDAAAEATRLHQSASSSTSSLSTRSLENPTPPFTPKMGRRSIESPSLGFCTDTLLPHLLEDDLGQLSDLEPE
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Molecular Weight
36.63 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
ARHGEF11, also known as Rho guanine nucleotide exchange factor 11, is a member of the RhoGEF family, which plays a crucial role in regulating Rho GTPase signaling pathways. These pathways are integral for various cellular processes, including cytoskeletal dynamics, cell migration, and proliferation. Dysregulation of Rho GTPases has been implicated in numerous diseases, including cancer, cardiovascular disorders, and neurological diseases. The study of ARHGEF11 is particularly significant due to its involvement in cellular responses to external stimuli and its potential role in developmental processes. Recent research has focused on elucidating the molecular mechanisms by which ARHGEF11 modulates Rho GTPase activities and how alterations in its expression or function may contribute to disease pathogenesis. Furthermore, the recombinant expression of ARHGEF11 provides a valuable tool for studying its functional characteristics and interactions with other proteins. Investigating the properties of ARHGEF11 at a molecular level may lead to the identification of novel therapeutic targets and strategies aimed at modulating Rho GTPase signaling in various pathological conditions. Overall, the characterization of ARHGEF11 and its recombinant protein holds significant promise for advancing our understanding of RhoGEF functions and their implications in health and disease.
