Analytical Data
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Gene name
F7
- Application
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Alternative Names
F7；SIAT7F；Alpha-N-acetylgalactosaminide alpha-2.6-sialyltransferase 6
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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
Q969X2
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Expression Region
1-333aa
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AA Sequence
MACSRPPSQCEPTSLPPGPPAGRRHLPLSRRRREMSSNKEQRSAVFVILFALITILILYSSNSANEVFHYGSLRGRSRRPVNLKKWSITDGYVPILGNKTLPSRCHQCVIVSSSSHLLGTKLGPEIERAECTIRMNDAPTTGYSADVGNKTTYRVVAHSSVFRVLRRPQEFVNRTPETVFIFWGPPSKMQKPQGSLVRVIQRAGLVFPNMEAYAVSPGRMRQFDDLFRGETGKDREKSHSWLSTGWFTMVIAVELCDHVHVYGMVPPNYCSQRPRLQRMPYHYYEPKGPDECVTYIQNEHSRKGNHHRFITEKRVFSSWAQLYGITFSHPSWT
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Molecular Weight
38 kDa
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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
The F7 recombinant protein, derived from the human coagulation factor VII gene, plays a crucial role in the hemostatic process, facilitating blood coagulation by activating factor X in the presence of tissue factor. Research into F7 has gained significant attention due to its therapeutic potential in treating various bleeding disorders, including hemophilia and other coagulation deficiencies. The production of F7 as a recombinant protein has revolutionized the treatment landscape, offering a safer alternative to plasma-derived products, which pose risks of transmission of infectious diseases and immunogenic reactions. Advances in biotechnology have enabled the development of stable cell lines and optimized production methodologies, allowing for consistent and high-yield synthesis of F7. Additionally, studies have focused on characterizing the protein’s biochemical properties, such as its stability and activity in clot formation, while exploring the development of novel delivery systems to enhance its pharmacokinetics and therapeutic efficacy. Furthermore, the exploration of F7 variants and their functional implications has opened avenues for personalized medicine approaches. Overall, the research surrounding F7 recombinant protein not only aims to improve patient outcomes in coagulation disorders but also contributes to a deeper understanding of the complex mechanisms underlying hemostasis and thrombosis.
