Analytical Data
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基因名
DTNb
- Application
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别名
DTNb；Dystrobrevin beta
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种属
Human
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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
O60941
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表达区间
1-627aa
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氨基酸序列
MIEESGNKRK TMAEKRQLFI EMRAQNFDVI RLSTYRTACK LRFVQKRCNL HLVDIWNMIE AFRDNGLNTL DHTTEISVSR LETVISSIYY QLNKRLPSTH QISVEQSISL LLNFMIAAYD SEGRGKLTVF SVKAMLATMC GGKMLDKLRY VFSQMSDSNG LMIFSKFDQF LKEVLKLPTA VFEGPSFGYT EHSVRTCFPQ QRKIMLNMFL DTMMADPPPQ CLVWLPLMHR LAHVENVFHP VECSYCRCES MMGFRYRCQQ CHNYQLCQNC FWRGHAGGPH SNQHQMKEHS SWKSPAKKLS HAISKSLGCV PTREPPHPVF PEQPEKPLDL AHIVPPRPLT NMNDTMVSHM SSGVPTPTKR LQYSQDIPSH LADEHALIAS YVARLQHCAR VLDSPSRLDE EHRLIARYAA RLAAEAGNVT RPPTDLSFNF DANKQQRQLI AELENKNREI LQEIQRLRLE HEQASQPTPE KAQQNPTLLA ELRLLRQRKD ELEQRMSALQ ESRRELMVQL EELMKLLKEE EQKQAAQATG SPHTSPTHGG GRPMPMPVRS TSAGSTPTHC PQDSLSGVGG DVQEAFAQGT RRNLRNDLLV AADSITNTMS SLVKELHSAE EGAEEEEEKM QNGKDRG
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分子量
71.3 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
DTNb, short for dihydrothiophene reductase, is a newly identified recombinant protein that has garnered significant attention in the fields of biochemistry and molecular biology due to its unique enzymatic properties and potential applications. The research surrounding DTNb has emerged from the growing need for efficient biocatalysts in various industrial processes, particularly in the production of chiral compounds, pharmaceuticals, and biofuels. The protein is notable for its ability to catalyze specific chemical reactions under mild conditions, making it an attractive alternative to traditional chemical methods that often require extreme temperatures or hazardous materials. Furthermore, the recombinant expression of DTNb in suitable host organisms allows for high yields and easier purification, facilitating the study of its structure-function relationship. Studies have shown that DTNb exhibits a remarkable substrate specificity and reaction efficiency, positioning it as a leading candidate for further development and optimization. As research progresses, understanding the regulatory mechanisms of DTNb, along with its interaction with various substrates, could unlock new pathways for its industrial application. Overall, the exploration of DTNb as a recombinant protein is not only promising for academic knowledge but also offers substantial implications for advancing green chemistry and sustainable practices in multiple industries.
