Analytical Data
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基因名
RRAD
- Application
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别名
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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种属
Human
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P55042
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表达区间
1-308 aa
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氨基酸序列
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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分子量
33.2 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
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稳定性测试
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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保存条件 & 期限
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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运输条件
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
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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.
