Analytical Data
-
基因名
FNTB
- Application
-
别名
CAAX farnesyltransferase subunit beta; EC 2.5.1.58; EC=2.5.1.58; Farnesyltransferase; farnesyltransferase CAAX box beta1; farnesyltransferase; CAAX box; beta; FNTB; FNTB_HUMAN; FPTB; FTase beta; FTase-beta; MGC105303
-
种属
Human
-
表达系统
E. coli
-
标签
GST-tag at N-terminal
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P49356
-
表达区间
1-437aa
-
氨基酸序列
MASPSSFTYYCPPSSSPVWSEPLYSLRPEHARERLQDDSVETVTSIEQAKVEEKIQEVFSSYKFNHLVPRLVLQREKHFHYLKRGLRQLTDAYECLDASRPWLCYWILHSLELLDEPIPQIVATDVCQFLELCQSPEGGFGGGPGQYPHLAPTYAAVNALCIIGTEEAYDIINREKLLQYLYSLKQPDGSFLMHVGGEVDVRSAYCAASVASLTNIITPDLFEGTAEWIARCQNWEGGIGGVPGMEAHGGYTFCGLAALVILKRERSLNLKSLLQWVTSRQMRFEGGFQGRCNKLVDGCYSFWQAGLLPLLHRALHAQGDPALSMSHWMFHQQALQEYILMCCQCPAGGLLDKPGKSRDFYHTCYCLSGLSIAQHFGSGAMLHDVVLGVPENALQPTHPVYNIGPDKVIQATTYFLQKPVPGFEELKDETSAEPATD
-
分子量
73.81 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
FNTB (Farnesyltransferase) is an important enzyme involved in the post-translational modification of proteins, specifically in the addition of farnesyl groups to C-terminal cysteine residues of target proteins, a process crucial for their membrane localization and function. Research on FNTB and its associated recombinant proteins has gained significant attention due to its implications in various diseases, particularly cancer. Abnormal farnesylation of proteins can lead to cellular transformation and tumorigenesis, as seen in the case of oncogenic Ras proteins. As such, the study of FNTB-encoded proteins and their interactions has become vital in understanding signaling pathways that are disrupted in malignancies. Recombinant FNTB proteins can be produced in a laboratory setting, allowing researchers to dissect the enzyme's functionality, its substrate specificity, and the molecular mechanisms underlying farnesylation. Understanding the structure-function relationship of FNTB can pave the way for the development of specific inhibitors that could serve as potential therapeutic agents in treating cancers driven by aberrant farnesylation. Furthermore, insights gathered from FNTB studies can also contribute to a broader understanding of lipid modifications in cell biology, underscoring the importance of farnesylation in regulating protein interactions and cellular processes. Overall, the investigation of FNTB recombinant proteins continues to hold promise for novel therapeutic strategies and enhances our comprehension of the role of post-translational modifications in human health and disease.
