Analytical Data
-
基因名
RICTOR
- Application
-
别名
Arhgap8; AU043908; C030017C09Rik; C78947; FLJ20185; FLJ20185k; MGC109513; MGC32512; PP610; Proline rich 5 (renal); Proline-rich protein 5; Protein observed with Rictor-1; Protor-1; PROTOR1; PRR5; PRR5_HUMAN; PTOR1; Rho GTPase activating protein 8; RP1-181C9.3
-
种属
Human
-
表达系统
E. coli
-
标签
His tag N-Terminus
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P85299
-
表达区间
1-388 aa
-
氨基酸序列
MRTLRRLKFM SSPSLSDLGK REPAAAADER GTQQRRACAN ATWNSIHNGV IAVFQRKGLP DQELFSLNEG VRQLLKTELG SFFTEYLQNQ LLTKGMVILR DKIRFYEGQK LLDSLAETWD FFFSDVLPML QAIFYPVQGK EPSVRQLALL HFRNAITLSV KLEDALARAH ARVPPAIVQM LLVLQGVHES RGVTEDYLRL ETLVQKVVSP YLGTYGLHSS EGPFTHSCIL EKRLLRRSRS GDVLAKNPVV RSKSYNTPLL NPVQEHEAEG AAAGGTSIRR HSVSEMTSCP EPQGFSDPPG QGPTGTFRSS PAPHSGPCPS RLYPTTQPPE QGLDPTRSSL PRSSPENLVD QILESVDSDS EGIFIDFGRG RGSGMSDLEG SGGRQSVV
-
分子量
42.7 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
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
-
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.
-
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.
-
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
Related Products
Protein Description
RICTOR is a key component of the mTORC2 (mechanistic Target of Rapamycin Complex 2), a critical regulator of various cellular processes, including metabolism, growth, and survival. Research into RICTOR and its associated signaling pathways has gained immense interest within the scientific community due to its pivotal role in cancer biology, particularly regarding tumor growth and resistance to therapy. Dysregulation of mTORC2, where RICTOR is centrally involved, has been implicated in a variety of cancers, underscoring the importance of this protein in oncogenic signaling. Furthermore, RICTOR's involvement in several physiological processes, such as insulin signaling and cell migration, reveals its broader biological significance. As a result, the study of recombinant RICTOR protein holds promise for elucidating the mechanisms underlying its function, potentially leading to the development of novel therapeutic strategies targeting mTORC2 in cancer treatment and other diseases associated with mTOR signaling dysregulation. Understanding the structural and functional properties of RICTOR can also provide insights into its interactions with other signaling molecules in the mTOR pathway, thereby advancing the field of targeted therapy and precision medicine. Overall, RICTOR represents not only a critical molecular entity within mTORC2 but also a valuable target for research aimed at understanding and combating cancer and metabolic disorders.












