Analytical Data
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基因名
aprN
- Application
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别名
aprN；Subtilisin NAT
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种属
E.coli
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表达系统
E. coli
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标签
His tag N-Terminus
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P35835
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表达区间
1-381aa
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氨基酸序列
MRSKKLWISLLFALTLIFTMAFSNMSAQAAGKSSTEKKYIVGFKQTMSAMSSAKKKDVISEKGGKVQKQFKYVNAAAATLDEKAVKELKKDPSVAYVEEDHIAHEYAQSVPYGISQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLNVRGGASFVPSETNPYQDGSSHGTHVAGTIAALNNSIGVLGVAPSASLYAVKVLDSTGSGQYSWIINGIEWAISNNMDVINMSLGGPTGSTALKTVVDKAVSSGIVVAAAAGNEGSSGSTSTVGYPAKYPSTIAVGAVNSSNQRASFSSVGSELDVMAPGVSIQSTLPGGTYGAYNGTSMATPHVAGAAALILSKHPTWTNAQVRDRLESTATYLGNSFYYGKGLINVQAAAQ
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分子量
39.5 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
Related Products
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Protein Description
The study of aprN recombinant protein is rooted in the exploration of proteolytic enzymes and their applications in various industries, including food processing, pharmaceuticals, and biotechnology. AprN, or alkaline protease N, is a serine protease produced by certain microorganisms, notably in the genus Bacillus. This enzyme demonstrates remarkable stability and activity across a wide range of pH levels and temperatures, making it a prime candidate for industrial applications. Researchers have focused on the recombinant expression of aprN to enhance its yield and functional properties, overcoming limitations associated with its natural production. By utilizing recombinant DNA technology, scientists can optimize the enzyme's characteristics through genetic modifications, leading to improved enzyme efficiency and specificity. This approach not only allows for the large-scale production of aprN but also facilitates the investigation of its biochemical mechanisms and potential modifications for tailored applications. The demand for efficient and robust enzymes drives the exploration of aprN, emphasizing its significance in various biotechnological frameworks.
