Analytical Data
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基因名
UL32
- Application
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别名
UL32；CCN1；CCNA；Cyclin-A2
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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
P08318
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表达区间
1-285aa
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氨基酸序列
MSLQFIGLQRRDVVALVNFLRHLTQKPDVDLEAHPKILKKCGEKRLHRRTVLFNELMLWLGYYRELRFHNPDLSSVLEEFEVRCVAVARRGYTYPFGDRGKARDHLAVLDRTEFDTDVRHDAEIVERALVSAVILAKMSVRETLVTAIGQTEPIAFVHLKDTEVQRIEENLEGVRRNMFCVKPLDLNLDRHANTALVNAVNKLVYTGRLIMNVRRSWEELERKCLARIQERCKLLVKELRMCLSFDSNYCRNILKHAVENGDSADTLLELLIEDFDIYVDSFPQS
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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
UL32 is a protein associated with the herpes simplex virus (HSV), specifically encoding a viral gene essential for viral replication and pathogenesis. Research on UL32 has gained significance due to the protein's role in the viral lifecycle, including its involvement in the formation of viral capsids and the incorporation of viral DNA. Understanding UL32 is critical for elucidating the mechanisms by which HSV evades the host immune response and establishes latency. Furthermore, UL32 has been identified as a potential target for antiviral drug development, as inhibiting its function could hinder viral replication and reduce the severity of infections. The protein is also linked to other herpesviruses, making it a valuable candidate for broader studies in herpesvirus biology. Recent advances in molecular biology techniques, including cryo-electron tomography and protein crystallization, have facilitated a deeper investigation of UL32's structure and function, paving the way for innovative therapeutic approaches. Overall, research on UL32 not only contributes to our fundamental understanding of herpesvirus biology but also holds promise for enhancing current therapeutic strategies against HSV and potentially other related viral infections.
