Analytical Data
-
基因名
Hypothetical membrane spanning
- Application
-
别名
Hypothetical membrane spanning protein
-
种属
Others
-
表达系统
E. coli Cell-free
-
标签
N-GST
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
Q83AM0
-
表达区间
M1-A603, L589A, L590A
-
氨基酸序列
MRNDDDTHSTLTSSSEQVSESKIVPKDSQKPSDPNVHQNGTDVTDSAKQNASLKEVTVVTLPPDLKALEGDTHPTPMPSSREVLFNPNVHKNGTPLTHSVDPNGLSKDDEVTIVALESESKALEKELKKKGINYFKIGKTIANVAYTASLCLVFYKLSAPRGVADGVISALVNAPSAAIFFDQFFGKVLINYNPKRVTKTHFALSLTGLAAGNIAAIAGEQIAEDAVKGSSAWIFYGGLGVSLIYTFTSRTLGLPGAVGYLLNPLLGRCRPFPELEQFRKDLEKNYLNPAVQRINEKTPERFIEVFYDTIKENPNKWTGYDIYKNTIEKAFQVGGLIAVQHFFGLFQQLAAEGWGKISPQLENNCGLNSISAATTAFFYYLLVLKLPPTFRKSLEQIWILGVHNSRTLPAKIIKTALLLATLGGAGVAAYFSGSGMAEETARYDQLAQNGTLPFCVNNPPLSPWEGIDGNVNELWMTIVAGVGCNFTGMLFLFNPILDFFIKKSHENPWCIQSMLAVLESAPILNSNQLEKELGSWIPLIQGKRPTAIQAIENKRSLVKIAENTNLPRPKFWFCGDLWKCSSNDENTRAASETEDPVPSALTA
-
蛋白长度
Full Length
-
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
Research on hypothetical membrane-spanning recombinant proteins has garnered significant interest due to their potential roles in various biological processes, including signal transduction, nutrient transport, and cellular communication. These proteins, often predicted through genomic and bioinformatics approaches, typically possess hydrophobic regions that allow them to integrate into cellular membranes, making them crucial for maintaining membrane integrity and functionality. Despite their predicted importance, many hypothetical proteins remain poorly characterized in terms of structure and function. Recent advancements in techniques such as X-ray crystallography, cryo-electron microscopy, and molecular dynamics simulations have provided researchers with powerful tools to elucidate the structure-function relationships of these membrane proteins. Moreover, the development of heterologous expression systems enables the production of large quantities of recombinant proteins, facilitating functional studies and potential biotechnological applications. Understanding the mechanisms by which these proteins interact with lipid bilayers and their specific molecular functions may unveil new therapeutic targets for diseases linked to membrane dysfunction. Thus, the study of hypothetical membrane-spanning recombinant proteins is not only vital for basic biological research but also holds promise for advancing drug discovery and development.
