Analytical Data
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基因名
A143V
- Application
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别名
A143V；Virion membrane Protein OPG143
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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
P16710
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表达区间
1-377aa
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氨基酸序列
MGAAVTLNRIKIAPGIADIRDKYMELGFNYPEYNRAVKFAEESYTYYYETSPGEIKPKFCLIDGMSIDHCSSFIVPEFAKQYVLIHGEPCSSFKFRPGSLIYYQNEVTPEYIKDLKHATDYIASGQRCHFIKKDYLLGDSDSVAKCCSKTNTKHCPKIFNNNYKTEHCDDFMTGFCRNDPGNPNCLEWLRAKRKPAMSTYSDICSKHMDARYCSEFIRIIRPDYFTFGDTALYVFCNDHKGNRNCWCANYPKSNSGDKYLGPRVCWLHECTDESRDRKWLYYNQDVQRTRCKYVGCTINVNSLALKNSQAELTSNCTRTTSAVGDVHPGEPVVKDKIKLPTWLGAAITLVVISVIFYFISIYSRPKIKTNDINVRRR
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分子量
43.4 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 A143V recombinant protein is derived from the study of the avian influenza virus (AIV), particularly focusing on its hemagglutinin (HA) gene. As mutations in AIV are known to influence viral infectivity and host range, the A143V substitution in the HA protein has garnered significant interest. Research has indicated that this mutation may enhance the virus's ability to bind to sialic acid receptors found in different hosts, including humans and other mammals. Understanding the molecular mechanisms behind this mutation is crucial for assessing the potential zoonotic risk of AIV strains and their capacity to cause pandemics. The A143V variant has been studied using various techniques, including recombinant DNA technology and bioinformatics, to analyze structural and functional changes in the HA protein. Such insights are vital for public health surveillance, vaccine development, and antiviral strategies, as they can inform the risks posed by emerging AIV variants and guide health responses to potential outbreaks. By elucidating the characteristics of the A143V recombinant protein, researchers aim to provide a framework for better understanding AIV evolution and its implications for animal and human health.
