关键信息
-
基因名
RINL
- 应用
-
别名
FLJ44131; FLJ45909; Ras and Rab interactor like; Ras and Rab interactor-like protein; RINL; RINL_HUMAN
-
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
Q6ZS11
-
表达区间
1-566 aa
-
氨基酸序列
MAQPEDKAPE VPTEGVRLVP PQVNKADRTP LGVLSTLEPL TRLQRTWGVW HVPELDTQDA EALVGLWPLG SFLVTGRDPS QALVLRSGPL PGEVNTYQIQ KIPRGVSLES SNLCMPDLPH LLAFLSASRD VLPRTLLLPP PTLGPRDEHT DPVQIGRVQQ DTPGKVLSIV NQLYLETHRG WGREQTPQET EPEAAQRHDP APRNPAPHGV SWVKGPLSPE VDHPGPALAS LLEEEEEDLE GKEEGREDDP EEEGPEDVLT IHVQSLVRAR SSYVARQYRS LRVRIASDSG GPHGSGDPAT ELLQDVRHLL TDLQDHLAKD SYIRAVFGSR GPGLPKKDED PGPALETAVC QAVLAPLKPA LWTRLRTLRA PELRRLRRRQ TALRAGAGPP GAQGPGPEGQ SPAPALRSRI HERLAHLHAA CAPRRKVALL LEVCRDVYAG LARGENQDPL GADAFLPALT EELIWSPDIG DTQLDVEFLM ELLDPDELRG EAGYYLTTWF GALHHIAHYQ PETDRAPRGL SSEARASLHQ WHRRRTLHRK DHPRAQANLP FKEPWAEETV TGTSDN
-
分子量
62.4 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.
质检流程
相关产品
背景信息
RINL (Reconstituted Integral Membrane Protein of the Lipid Bilayer) has emerged as a subject of significant research interest due to its crucial role in various biological processes and potential applications in biomedicine. Integral membrane proteins are essential for numerous cellular functions, including signaling, transport, and communication. However, studying these proteins has been challenging due to their complex structures and interactions with lipid environments. Recent advancements in recombinant DNA technology have enabled the expression and purification of RINL, allowing researchers to gain insights into its function and structure. Understanding RINL’s mechanisms could provide valuable information on membrane dynamics and facilitate the development of targeted therapies for diseases involving membrane proteins, such as cancer and neurodegenerative disorders. Moreover, RINL serves as a model to explore the biophysical properties of membrane proteins, contributing to the advancement of techniques in structural biology, pharmacology, and bioengineering. As research continues, the implications of RINL extend beyond fundamental biology, promising novel strategies for drug design and the development of biomimetic materials.
