Analytical Data
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基因名
NEU1
- Application
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别名
OXT;OT;Oxytocin-neurophysin 1
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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
Q99519
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表达区间
48-415aa
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氨基酸序列
MGSSHHHHHH SSGLVPRGSH MGSHMEND FGLVQPLVTM EQLLWVSGRQ IGSVDTFRIP LITATPRGTL LAFAEARKMS SSDEGAKFIA LRRSMDQGST WSPTAFIVND GDVPDGLNLG AVVSDVETGV VFLFYSLCAH KAGCQVASTM LVWSKDDGVS WSTPRNLSLD IGTEVFAPGP GSGIQKQREP RKGRLIVCGH GTLERDGVFC LLSDDHGASW RYGSGVSGIP YGQPKQENDF NPDECQPYEL PDGSVVINAR NQNNYHCHCR IVLRSYDACD TLRPRDVTFD PELVDPVVAA GAVVTSSGIV FFSNPAHPEF RVNLTLRWSF SNGTSWRKET VQLWPGPSGY SSLATLEGSM DGEEQAPQLY VLYEKGRNHY TESISVAKIS VYGTL
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分子量
43 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
NEU1, or sialidase-1, is a lysosomal enzyme that plays a crucial role in the metabolism of sialoglycoconjugates, which are essential for various biological processes, including cell-cell interactions and signaling. Abnormal activity of NEU1 has been implicated in several diseases, such as sialidosis and other lysosomal storage disorders. Understanding the function and regulation of NEU1 is vital for elucidating its role in health and disease. Researchers have been focusing on the recombinant expression of NEU1 to produce sufficient quantities of the enzyme for biochemical studies, which can provide insights into its catalytic mechanism, substrate specificity, and interaction with inhibitors. This knowledge can pave the way for developing targeted therapies for conditions associated with NEU1 dysfunction. Furthermore, recombinant NEU1 can be used in drug development and delivery systems, enhancing its clinical applications. The study of NEU1 as a recombinant protein thus represents an important frontier in biochemistry and molecular medicine, highlighting the enzyme's significance in cellular physiology and its potential as a therapeutic target.
