Analytical Data
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基因名
SDSL
- Application
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别名
L serine deaminase; L serine dehydratase/L threonine deaminase; L threonine dehydratase; L-serine deaminase; L-serine dehydratase/L-threonine deaminase; L-threonine dehydratase; SDH 2; SDH; SDH1; SDS RS1; Sdsl; SDSL_HUMAN; Serine dehydratase 2; Serine dehydratase like; Serine dehydratase related sequence 1; Serine dehydratase-like; TDH
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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
Q96GA7
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表达区间
1-329 aa
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氨基酸序列
MDGPVAEHAK QEPFHVVTPL LESWALSQVA GMPVFLKCEN VQPSGSFKIR GIGHFCQEMA KKGCRHLVCS SGGNAGIAAA YAARKLGIPA TIVLPESTSL QVVQRLQGEG AEVQLTGKVW DEANLRAQEL AKRDGWENVP PFDHPLIWKG HASLVQELKA VLRTPPGALV LAVGGGGLLA GVVAGLLEVG WQHVPIIAME THGAHCFNAA ITAGKLVTLP DITSVAKSLG AKTVAARALE CMQVCKIHSE VVEDTEAVSA VQQLLDDERM LVEPACGAAL AAIYSGLLRR LQAEGCLPPS LTSVVVIVCG GNNINSRELQ ALKTHLGQV
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分子量
34.6 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
SDSL (Site-Directed Spin Labeling) is a powerful technique utilized in the field of structural biology to investigate the dynamics and conformational changes of proteins. This method primarily involves attaching stable free radical spin labels to specific sites on proteins, allowing researchers to study the local environment, interactions, and conformational states through electron paramagnetic resonance (EPR) spectroscopy. The unique advantage of SDSL lies in its capacity to provide insight into membrane proteins, which are often challenging to analyze due to their complex structures and environments. The quest to understand protein folding, dynamics, and interactions under physiological conditions has made SDSL an invaluable tool in modern biochemistry. Researchers have increasingly focused on integrating SDSL with complementary techniques such as X-ray crystallography and NMR spectroscopy to achieve a comprehensive understanding of protein structures. The advances in protein engineering techniques have facilitated the selective incorporation of spin labels, thereby enhancing the specificity and sensitivity of SDSL studies. Thus, SDSL continues to play a crucial role in deciphering the intricate mechanisms governing protein function, contributing to our broader understanding of biological processes and potential therapeutic interventions.
