Analytical Data
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Gene name
F8A1
- Application
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Alternative Names
F8A1；FAM51A1；Gem-associated Protein 8
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P23610
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Expression Region
2-371aa
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AA Sequence
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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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
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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Storage & Shelf Life
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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Shipping
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
Related Products
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.
