Analytical Data
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Gene name
ARHGDIG
- Application
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Alternative Names
Arhgdig; GDIR3_HUMAN; OTTHUMP00000067353; OTTHUMP00000194914; Rho GDI 3
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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
Q99819
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Expression Region
1-225aa
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AA Sequence
MLGLDACELGAQLLELLRLALCARVLLADKEGGPPAVDEVLDEAVPEYRAPGRKSLLEIRQLDPDDRSLAKYKRVLLGPLPPAVDPSLPNVQVTRLTLLSEQAPGPVVMDLTGDLAVLKDQVFVLKEGVDYRVKISFKVHREIVSGLKCLHHTYRRGLRVDKTVYMVGSYGPSAQEYEFVTPVEEAPRGALVRGPYLVVSLFTDDDRTHHLSWEWGLCICQDWKD
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Molecular Weight
50.49 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
ARHGDIG (Rho GDP dissociation inhibitor gamma) is a member of the Rhogap family and plays a pivotal role in the regulation of Rho GTPases, which are critical for various cellular processes including cytoskeletal dynamics, cell migration, and signal transduction. Research has shown that ARHGDIG is involved in several physiological and pathological conditions, including cancer metastasis, neuronal functioning, and cardiovascular diseases. These roles make it a significant target for therapeutic interventions. Recent studies have focused on the structural characterization of ARHGDIG and its interaction with Rho proteins to elucidate the molecular mechanisms underlying its function. Understanding the conformational states of ARHGDIG in relation to its activity could provide insights into its regulatory mechanisms and offer potential therapeutic avenues for diseases where Rho GTPase dysregulation occurs. Furthermore, the development of recombinant ARHGDIG proteins allows for the exploration of inhibitor design and the investigation of its biological pathways. Continued research in this area contributes to a deeper understanding of cell signaling dynamics and the development of novel strategies to modulate Rho GTPase activity for improved disease management.
