Analytical Data
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Gene name
RSG1
- Application
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Alternative Names
CPLANE2;C1orf89;RSG1;Ciliogenesis and planar polarity effector 2
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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
Q9BU20
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Expression Region
1-258aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMARPPVPGSVVVPNWHESAEGKEYLAC ILRKNRRRVFGLLERPVLLPPVSIDTASYKIFVSGKSGVGKTALVAKLAG LEVPVVHHETTGIQTTVVFWPAKLQASSRVVMFRFEFWDCGESALKKFDH MLLACMENTDAFLFLFSFTDRASFEDLPGQLARIAGEAPGVVRMVIGSKF DQYMHTDVPERDLTAFRQAWELPLLRVKSVPGRRLADGRTLDGRAGLADV AHILNGLAEQLWHQDQVAAGLLPNPPESAPE
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Molecular Weight
31 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
RSG1, a member of the Ras superfamily of GTPases, has garnered significant attention in recent years due to its pivotal role in various cellular processes, including signal transduction, cytoskeletal dynamics, and cell migration. Its involvement in cellular functions has implications for understanding various diseases, particularly cancer and neurodegenerative disorders. RSG1 acts as a molecular switch that toggles between an active GTP-bound state and an inactive GDP-bound state, orchestrating a variety of downstream signaling pathways. Research into RSG1 has focused on its structural characteristics, including the identification of key residues necessary for its GTPase activity and binding affinities. Furthermore, studies examining the potential post-translational modifications that may modulate RSG1 activity help elucidate its functional mechanisms in cellular contexts. The availability of recombinant RSG1 proteins has facilitated the exploration of its biochemical properties, interactions with other cellular partners, and its overall contribution to oncogenic processes. Understanding RSG1's functionality and regulatory mechanisms is crucial for developing targeted therapies that could mitigate its dysregulation in pathological conditions. As such, the study of RSG1 not only deepens our knowledge of cellular signaling networks but also holds promise for therapeutic interventions in diseases linked to GTPase dysfunction.
