Analytical Data
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Gene name
RRAD
- Application
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Alternative Names
GTP binding protein RAD; GTP-binding protein RAD; RAD; RAD_HUMAN; RAD1; RAS (RAD and GEM) like GTP binding 3; Ras associated with diabetes; Ras related associated with diabetes; REM3; RRAD
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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
P55042
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Expression Region
1-308 aa
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AA Sequence
MTLNGGGSGA GGSRGGGQER ERRRGSTPWG PAPPLHRRSM PVDERDLQAA LTPGALTAAA AGTGTQGPRL DWPEDSEDSL SSGGSDSDES VYKVLLLGAP GVGKSALARI FGGVEDGPEA EAAGHTYDRS IVVDGEEASL MVYDIWEQDG GRWLPGHCMA MGDAYVIVYS VTDKGSFEKA SELRVQLRRA RQTDDVPIIL VGNKSDLVRS REVSVDEGRA CAVVFDCKFI ETSAALHHNV QALFEGVVRQ IRLRRDSKEA NARRQAGTRR RESLGKKAKR FLGRIVARNS RKMAFRAKSK SCHDLSVL
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Molecular Weight
33.2 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
RRAD (Ras-related associated with diabetes) is a member of the Ras superfamily of small GTPases that has garnered attention for its potential role in various physiological and pathological processes, including cellular signaling, metabolism, and cancer progression. Initial studies revealed its involvement in insulin signaling pathways, suggesting a connection to diabetes and metabolic disorders. Recent research has expanded the focus on RRAD, exploring its regulatory effects on cellular proliferation and differentiation, as well as its impact on tumorigenesis. The dual functionality of RRAD in both metabolic and oncogenic contexts has prompted interest in understanding its molecular mechanisms and interaction with other cellular pathways. Given the rising prevalence of diabetes and cancer worldwide, elucidating the role of RRAD could provide valuable insights into novel therapeutic strategies. The availability of recombinant RRAD proteins has facilitated in-depth studies of its structure-function relationship and interactions with downstream effectors. Consequently, continued research on RRAD could significantly contribute to our understanding of its implications in health and disease.
