Analytical Data
-
基因名
POFUT2
- Application
-
别名
GDP-fucose protein O-fucosyltransferase 2. EC:2.4.1.221. Peptide-O-fucosyltransferase 2. O-FucT-2
-
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
Q9Y2G5
-
表达区间
1-429 aa
-
氨基酸序列
MATLSFVFLLLGAVSWPPASASGQEFWPGQSAADILSGAASRRRYLLYDVNPPEGFNLRRDVYIRIASLLKTLLKTEEWVLVLPPWGRLYHWQSPDIHQVRIPWSEFFDLPSLNKNIPVIEYEQFIAESGGPFIDQVYVLQSYAEGWKEGTWEEKVDERPCIDQLLYSQDKHEYYRGWFWGYEETRGLNVSCLSVQGSASIVAPLLLRNTSARSVMLDRAENLLHDHYGGKEYWDTRRSMVFARHLREVGDEFRSRHLNSTDDADRIPFQEDWMKMKVKLGSALGGPYLGVHLRRKDFIWGHRQDVPSLEGAVRKIRSLMKTHRLDKVFVATDAVRKEYEELKKLLPEMVRFEPTWEELELYKDGGVAIIDQWICAHARFFIGTSVSTFSFRIHEEREILGLDPKTTYNRFCGDQEKACEQPTHWKITY
-
分子量
76.4 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.
Quality inspection process
Related Products
Protein Description
POFUT2, or protein O-fucosyltransferase 2, is an enzyme that catalyzes the transfer of fucose, a sugar molecule, to specific serine and threonine residues on target proteins, primarily within the context of Notch signaling pathways. This O-fucosylation process is crucial for the proper functioning of various cellular processes, including cell differentiation, proliferation, and communication. Aberrant POFUT2 activity has been implicated in numerous diseases, including cancer, where altered glycosylation patterns can influence tumor growth and metastasis. Studies have shown that POFUT2 plays a pivotal role in regulating Notch receptor activation and modulating downstream signaling, which is essential for maintaining tissue homeostasis. Given the significance of glycosylation in protein function and the pathological consequences of its dysregulation, researchers have focused on characterizing POFUT2's structure and enzymatic mechanism, as well as exploring its potential as a therapeutic target. Understanding the nuances of POFUT2's activity could pave the way for novel interventions in diseases characterized by Notch signaling dysregulation, making it a key focus in the field of glycoscience and cancer research. Recent advances in recombinant protein technology have enabled the detailed study of POFUT2, providing insights into its substrate specificity and regulatory mechanisms, thereby enhancing our understanding of its biological roles and therapeutic potential.
