Analytical Data
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基因名
PDHb
- Application
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别名
PDHb；PHE1B；Pyruvate dehydrogenase E1 component subunit beta. mitochondrial
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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
P11177
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表达区间
31-359aa
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氨基酸序列
LQVTVRDAINQGMDEELERDEKVFLLGEEVAQYDGAYKVSRGLWKKYGDKRIIDTPISEMGFAGIAVGAAMAGLRPICEFMTFNFSMQAIDQVINSAAKTYYMSGGLQPVPIVFRGPNGASAGVAAQHSQCFAAWYGHCPGLKVVSPWNSEDAKGLIKSAIRDNNPVVVLENELMYGVPFEFPPEAQSKDFLIPIGKAKIERQGTHITVVSHSRPVGHCLEAAAVLSKEGVECEVINMRTIRPMDMETIEASVMKTNHLVTVEGGWPQFGVGAEICARIMEGPAFNFLDAPAVRVTGADVPMPYAKILEDNSIPQVKDIIFAIKKTLNI
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分子量
41.9 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
PDHb, or Pseudomonas putida Hemoglobin, is a novel globin protein that has gained research interest due to its unique biochemical properties and potential applications in biotechnology and medicine. Discovered in the non-pathogenic bacterium Pseudomonas putida, PDHb is part of a larger family of hemoglobin-like proteins that facilitate oxygen transport and storage in various organisms. Unlike traditional hemoglobins found in vertebrates, PDHb exhibits a distinct structural configuration and enzymatic capabilities, allowing it to efficiently bind oxygen and potentially participate in electron transfer processes. Its stability under diverse environmental conditions and ability to function at varying pH levels make it a candidate for biotechnological applications, such as bioremediation and biosensor development. Furthermore, PDHb’s role in microbial metabolism offers insights into anaerobic respiration, which is crucial for understanding carbon cycling in ecosystems. As researchers investigate the detailed mechanisms of PDHb's function and regulation, there is growing interest in harnessing this protein for innovative applications in metabolic engineering, synthetic biology, and therapeutic uses, such as drug delivery systems and tissue engineering. Thus, the study of PDHb not only contributes to fundamental biological knowledge but also paves the way for practical applications that address environmental and health-related challenges.
