Analytical Data
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基因名
STE13
- Application
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别名
YSCIV
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种属
Saccharomyces cerevisiae
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表达系统
E. coli
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标签
N- His
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P33894
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表达区间
1-119aa
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分子量
18 kDa
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内毒素
< 1.0 EU per μg protein as determined by the LAL method.
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性状
Freeze-dried powder
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缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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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
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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.
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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.
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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
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Protein Description
STE13 is a key enzyme in yeast that plays a crucial role in the mating process, specifically by acting as an aminopeptidase involved in the regulation of pheromone signaling pathways. This enzyme is responsible for the cleavage of specific peptide bonds in the a- and α-factor pheromones, which are essential for yeast mating response and sexual differentiation. The study of STE13 and its recombinant protein form has garnered attention due to its potential applications in understanding the molecular mechanisms of cell signaling and mating behaviors in eukaryotic organisms. Furthermore, investigating STE13 could provide insights into the evolutionary biology of sexual reproduction and its regulation. The recombinant expression of STE13 allows researchers to produce large quantities of the protein for biochemical characterization, structural studies, and functional assays. Such research can also contribute to the development of biotechnological applications, including the design of novel therapeutics targeting similar pathways in other organisms. The exploration of STE13's structure-function relationships can reveal critical information about substrate specificity and catalytic mechanisms, making it a significant focus in enzymology and reproductive biology studies. Overall, the research on STE13 recombinant protein not only enhances our understanding of yeast biology but also opens avenues for interdisciplinary applications in microbial physiology and medicinal chemistry.












