Analytical Data
-
基因名
RBBP7
- Application
-
别名
Histone acetyltransferase type B subunit 2Nucleosome-remodeling factor subunit RBAP46Retinoblastoma-binding protein 7 ;RBBP-7Retinoblastoma-binding protein p46
-
种属
Human
-
表达系统
E. coli
-
标签
N- His-SUMO
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
Q16576
-
表达区间
1-425aa
-
分子量
63.8 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
RBBP7, also known as retinoblastoma binding protein 7, is a crucial protein involved in various cellular processes, including gene regulation, chromatin remodeling, and cell cycle control. This protein is a part of the larger family of RBBP proteins, which have been implicated in the regulation of tumor suppressor proteins and oncogenes, thus playing a critical role in cancer biology. The study of RBBP7 is particularly relevant due to its association with the retinoblastoma tumor suppressor pathway, which is frequently altered in cancers. Researchers are interested in the reconstitution of RBBP7 to better understand its biochemical properties, interactions with other cellular factors, and its role in chromatin architecture and gene expression regulation. Insights from these studies could lead to novel therapeutic strategies for cancers characterized by dysregulation of the pathways involving RBBP7. Furthermore, understanding the structural and functional dynamics of RBBP7 in various cellular contexts may provide deeper insights into its role in development and disease, making it a significant target for future research in cancer therapeutics and gene regulation frameworks.
