Analytical Data
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Gene name
F5
- Application
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Alternative Names
F5；HTR1EL；5-hydroxytryptamine receptor 1F
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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
P30939
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Expression Region
1-366aa
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AA Sequence
MDFLNSSDQNLTSEELLNRMPSKILVSLTLSGLALMTTTINSLVIAAIIVTRKLHHPANYLICSLAVTDFLVAVLVMPFSIVYIVRESWIMGQVVCDIWLSVDITCCTCSILHLSAIALDRYRAITDAVEYARKRTPKHAGIMITIVWIISVFISMPPLFWRHQGTSRDDECIIKHDHIVSTIYSTFGAFYIPLALILILYYKIYRAAKTLYHKRQASRIAKEEVNGQVLLESGEKSTKSVSTSYVLEKSLSDPSTDFDKIHSTVRSLRSEFKHEKSWRRQKISGTRERKAATTLGLILGAFVICWLPFFVKELVVNVCDKCKISEEMSNFLAWLGYLNSLINPLIYTIFNEDFKKAFQKLVRCRC
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Molecular Weight
41.7 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 study of F5 recombinant proteins is rooted in the critical importance of coagulation factors in maintaining hemostasis and their roles in various pathological conditions. F5, also known as factor V, is a crucial cofactor in the prothrombinase complex that catalyzes the conversion of prothrombin to thrombin, which is essential for blood clot formation. Dysregulation or mutations in the F5 gene can lead to clotting disorders such as thrombophilia or hemophilia, leading to serious health risks. The advent of recombinant DNA technology has enabled the production of F5 and its variants in controlled laboratory settings, facilitating detailed studies on their structure and function. This research aims to elucidate the molecular mechanisms governing coagulation, explore therapeutic applications, and provide insights into the development of inhibitors for anticoagulant therapy. Additionally, recombinant F5 proteins serve as valuable tools in diagnostic assays and as research reagents. The ongoing investigation into the biophysical properties, biological activity, and potential medical applications underscores the significance of F5 recombinant proteins in advancing our understanding of coagulation pathways and improving patient outcomes in clotting disorders.
