Analytical Data
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Gene name
SERPINF2
- Application
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Alternative Names
SERPINF2；AAP；PLI；Alpha-2-antiplasmin
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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
P08697
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Expression Region
全长
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AA Sequence
MVLLWGLLVLSWSCLQGPCSVFSPVSAMEPLGRQLTSGPNQEQVSPLTLL KLGNQEPGGQTALKSPPGVCSRDPTPEQTHRLARAMMAFTADLFSLVAQT STCPNLILSPLSVALALSHLALGAQNHTLQRLQQVLHAGSGPCLPHLLSR LCQDLGPGAFRLAARMYLQKGFPIKEDFLEQSEQLFGAKPVSLTGKQEDD LANINQWVKEATEGKIQEFLSGLPEDTVLLLLNAIHFQGFWRNKFDPSLT QRDSFHLDEQFTVPVEMMQARTYPLRWFLLEQPEIQVAHFPFKNNMSFVV LVPTHFEWNVSQVLANLSWDTLHPPLVWERPTKVRLPKLYLKHQMDLVAT LSQLGLQELFQAPDLRGISEQSLVVSGVQHQSTLELSEVGVEAAAATSIA MSRMSLSSFSVNRPFLFFIFEDTTGLPLFVGSVRNPNPSAPRELKEQQDS PGNKDFLQSLKGFPRGDKLFGPDLKLVPPMEEDYPQFGSPK
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Molecular Weight
81 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
SERPINF2, also known as alpha-2-antiplasmin, is a serine protease inhibitor that plays a crucial role in regulating fibrinolysis, the process responsible for dissolving blood clots. Its main function is to inhibit the activity of plasmin, the enzyme that breaks down fibrin in blood clots, ensuring proper hemostasis. Dysregulation of SERPINF2 has been implicated in various pathological conditions, including thrombosis, cardiovascular diseases, and certain types of cancer. Research into SERPINF2 recombinant proteins has gained attention for their potential therapeutic applications, such as developing anticoagulant therapies, improving wound healing, and enhancing tissue repair. Recombinant SERPINF2 can be produced in sufficient quantities for functional studies and preclinical trials, enabling scientists to investigate its structure-function relationships, understand its role in disease mechanisms, and explore its applications in targeted therapies. Furthermore, the generation of SERPINF2 recombinant proteins allows for the assessment of genetic variations and their effects on protein function, which is essential for personalized medicine approaches. Overall, the study of SERPINF2 and its recombinant forms holds promise for advancing our understanding of hemostatic balance and developing new strategies for managing conditions related to fibrinolytic dysfunction.
