关键信息
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基因名
aLA
- 应用
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别名
aLA；ACY1L2；Xaa-Arg dipeptidase
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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
Q8IYS1
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表达区间
1-436aa
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氨基酸序列
MRPGGERPVE GGACNGRSEL ELLKLRSAEC IDEAAERLGA LSRAIWSQPE LAYEEHHAHR VLTHFFEREP PAASWAVQPH YQLPTAFRAE WEPPEARAPS ATPRPLHLGF LCEYDALPGI GHACGHNLIA EVGAAAALGV RGALEGLPRP PPPVKVVVLG TPAEEDGGGK IDLIEAGAFT NLDVVFMAHP SQENAAYLPD MAEHDVTVKY YGKASHSASY PWEGLNALDA AVLAYNNLSV FRQQMKPTWR VHGIIKNGGV KPNIIPSYSE LIYYFRAPSM KELQVLTKKA EDCFRAAALA SGCTVEIKGG AHDYYNVLPN KSLWKAYMEN GRKLGIEFIS EDTMLNGPSG STDFGNVSFV VPGIHPYFHI GSNALNHTEQ YTEAAGSQEA QFYTLRTAKA LAMTALDVIF KPELLEGIRE DFKLKLQEEQ FVNAVE
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分子量
47.7 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.
质检流程
相关产品
背景信息
The study of aLA (alpha-lactalbumin) recombinant proteins has gained significant attention due to their multifunctional roles in various biological processes. aLA, a major whey protein found in milk, is crucial for lactose synthesis and has been implicated in numerous health benefits, including antioxidant properties and potential anti-cancer effects. Its unique structure, characterized by a high content of alpha-helices and a specific calcium-binding site, allows it to participate in various physiological functions and interact with other biomolecules effectively. The production of recombinant aLA proteins through genetic engineering techniques enables researchers to produce high-purity proteins for extensive studies and applications, including functional foods, pharmaceuticals, and nutritional supplements. The recombinant approach not only provides a more sustainable and cost-effective method of obtaining aLA, free from the variability of natural sources but also facilitates the study of its structure-function relationship and its modifications for enhanced bioactivity. Furthermore, as the understanding of aLA's biological activities expands, its potential applications in food technology, medicine, and biotechnology are becoming increasingly evident, making it a focal point of current research in protein engineering and functional genomics.
