Analytical Data
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基因名
MPO
- Application
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别名
MPO；Myeloperoxidase
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种属
Human
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表达系统
E. coli
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标签
N-terminal His-tag
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纯度
Greater than 90% as determined by SDS-PAGE.
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蛋白编号
P05164
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表达区间
49~745aa
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氨基酸序列
AAPAVLGEVDTSLVLSSMEEAKQLVDKAYKERRESIKQRLRSGSASPIELLSYFKQPVAATRTAVRAADYLHVALDLLERKLRSLWRRPFNVTDVLTPAQLNVL SKSSGCAYQDVGVTCPEQDKYRTITGMCNNRRSPTLGASNRAF VRWLPAEYEDGF SLPYGWTPGVKRNGFPVALARAVSNEIVRFPTDQLTPDQERSLMF MQWGQLLDHDLDFTPEPAARASFVTGVNCETSCVQQPPCFPLKIPPNDPRIKNQADCIPFFRSCPACPGSNITIRNQINALTSFVDASMVYGSEEPLARNLRNMISNQLGLLAVNQRFQDNGRALLPFDNLHDDPCLLTNRSARIPCFLAGDTRSSEMPELTSMHTLLLREHNRLATELKSLNPRWDGERLYQEARKIVGAMVQIITYRDYLPLVLGPTAMRKYLPTYRSYNDSVDPRIANVFTNAFRYGHTLIQPFIFRLDNRYQPMEPNPRVPLSRVFFASWRVVLEGGIDPILRGLMATPAKLNRONOIAVDEIRERLFEQVIRIGLDLPALNMIQRSRDHGLPGYNAWRRFCGLPQPETVGQLGTVLRNLKLARKLMEQYGTPNNIDIWMGGVSEPLKRKGRVGPLLACIIGTQFRKLRDGDRFWWENEGVF SMQQRQALAQI SLPRIICDNTGITTVSKNNIFISNSYPRDF VNCSTLPALNLASWREAS
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分子量
82.7kDa
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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
Identification
Protein Description
MPO (myeloperoxidase) is a heme enzyme primarily found in neutrophils, playing a crucial role in the immune response by producing hypochlorous acid from hydrogen peroxide and chloride ions. This antimicrobial agent aids in the destruction of pathogens during inflammation. Research into MPO has expanded beyond its traditional roles, uncovering its involvement in various diseases, including cardiovascular diseases, cancer, and autoimmune disorders. The enzyme's pro-inflammatory effects have triggered interest in its potential as a biomarker for these conditions. However, the study of MPO also presents challenges, such as its complex structure and the difficulty of obtaining large quantities of functional protein for experimental purposes. Therefore, the development of recombinant MPO through techniques like genetic engineering is gaining momentum. Recombinant MPO can be produced in various systems, enabling researchers to investigate its functionality, interactions, and potential therapeutic applications more thoroughly. This approach not only allows for the detailed study of MPO's enzymatic properties but also offers insights into how it can be modulated for therapeutic benefit, highlighting its significance in both basic research and clinical applications.
