Analytical Data
-
基因名
RBP1
- Application
-
别名
RALBP1;RLIP;RLIP1;RLIP76;RalA-binding Protein 1
-
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
P09455
-
表达区间
1-197aa
-
氨基酸序列
MGSSHHHHHHSSGLVPRGSHMGSMDPPAGFVRAGNPAVAAPQSPLSPEGA HFRAAHHPRSTGSRCPGSLQPSRPLVANWLQSLPEMPVDFTGYWKMLVNE NFEEYLRALDVNVALRKIANLLKPDKEIVQDGDHMIIRTLSTFRNYIMDF QVGKEFEEDLTGIDDRKCMTTVSWDGDKLQCVQKGEKEGRGWTQWIEGDE LHLEMRVEGVVCKQVFKKVQ
-
分子量
25 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
RBP1, or retinol-binding protein 1, plays a crucial role in the transport of retinol (vitamin A) in the bloodstream and is vital for various physiological processes, including vision, immune function, and cellular growth. Understanding the structure and function of RBP1 is essential due to its implications in several diseases, such as diabetes, obesity, and certain cancers, where vitamin A metabolism may be disrupted. Research into recombinant RBP1 has gained momentum in recent years, focusing on its production, purification, and functional characterization. By employing recombinant DNA technology, scientists are able to produce RBP1 in a controlled manner, facilitating detailed studies on its binding properties and biological activities. This research not only helps elucidate the mechanistic role of RBP1 in vitamin A transport but also paves the way for potential therapeutic applications, such as using RBP1 as a biomarker for disease states or developing vitamin A-based treatments. As the field advances, the recombinant RBP1 serves as a valuable tool for both basic and applied research, highlighting its importance in the intersection of nutrition and health.
