Analytical Data
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基因名
hchA
- Application
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别名
hchA;Protein/nucleic acid deglycase HchA
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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
P31658
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表达区间
1-283aa
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氨基酸序列
MGSSHHHHHHSSGLVPRGSHMTVQTSKNPQVDIAEDNAFFPSEYSLSQYT SPVSDLDGVDYPKPYRGKHKILVIAADERYLPTDNGKLFSTGNHPIETLL PLYHLHAAGFEFEVATISGLMTKFEYWAMPHKDEKVMPFFEQHKSLFRNP KKLADVVASLNADSEYAAIFVPGGHGALIGLPESQDVAAALQWAIKNDRF VISLCHGPAAFLALRHGDNPLNGYSICAFPDAADKQTPEIGYMPGHLTWY FGEELKKMGMNIINDDITGRVHKDRKLLTGDSPFAANALGKLAAQEMLAA YAG
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分子量
33 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
The study of recombinant HchA protein has gained significant attention in the field of biochemistry and molecular biology due to its potential applications in various industrial and biomedical processes. HchA, an enzyme derived from specific microorganisms, plays a crucial role in the catabolism of complex organic compounds, particularly in the degradation of pollutants and xenobiotics in the environment. Understanding the structure and function of HchA is vital for its optimization and application in bioremediation strategies. Recombinant technology allows for the production of HchA in greater quantities and with enhanced properties, making it more effective for practical uses. Researchers have focused on the gene cloning, expression, and characterization of HchA to elucidate its enzymatic mechanisms and substrate specificity. This research not only helps in the design of more efficient biocatalysts but also opens up avenues for the development of novel therapeutic agents. The exploration of HchA's potential has broad implications, from environmental sustainability to industrial applications, highlighting the importance of such studies in addressing modern challenges in both ecology and health.
