Analytical Data
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基因名
F8A1
- Application
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别名
F8A1;FAM51A1;Gem-associated Protein 8
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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
P23610
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表达区间
2-371aa
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氨基酸序列
AAAAAGLGG GGAGPGPEAG DFLARYRLVS NKLKKRFLRK PNVAEAGEQF GQLGRELRAQ ECLPYAAWCQ LAVARCQQAL FHGPGEALAL TEAARLFLRQ ERDARQRLVC PAAYGEPLQA AASALGAAVR LHLELGQPAA AAALCLELAA ALRDLGQPAA AAGHFQRAAQ LQLPQLPLAA LQALGEAASC QLLARDYTGA LAVFTRMQRL AREHGSHPVQ SLPPPPPPAP QPGPGATPAL PAALLPPNSG SAAPSPAALG AFSDVLVRCE VSRVLLLLLL QPPPAKLLPE HAQTLEKYSW EAFDSHGQES SGQLPEELFL LLQSLVMATH EKDTEAIKSL QVEMWPLLTA EQNHLLHLVL QETISPSGQG V
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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
F8A1 recombinant protein is a pivotal subject of study in the field of biotechnology and protein engineering, primarily due to its relevance in understanding and treating hemophilia A, a genetic disorder characterized by the deficiency of clotting factor VIII. The recombinant form of factor VIII derived from genetically modified cells has revolutionized hemophilia treatment, enabling more effective and safer therapeutic options for patients. Research into F8A1 involves elucidating its structure-function relationship, optimizing expression systems, and enhancing protein stability to improve therapeutic efficacy. Furthermore, the modulation of F8A1 through various techniques, such as glycosylation adjustments and fusion protein engineering, aims to overcome issues related to immunogenicity and therapeutic half-life. Recent advancements have led to the development of extended half-life therapies, significantly reducing the frequency of infusions needed by patients. Additionally, understanding the molecular mechanisms of F8A1 interactions in the coagulation cascade is crucial for the development of novel treatments and gene therapies targeting the underlying genetic defects. Ongoing studies also explore innovative delivery methods and personalized medicine approaches to tailor treatments to individual patient profiles. Overall, the research surrounding F8A1 recombinant protein not only provides insights into hemophilia management but also contributes to the broader field of therapeutic protein development, with the potential to extend applications to other genetic disorders and diseases involving similar coagulation pathways.












