Analytical Data
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Gene name
a2PI
- Application
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Alternative Names
a2PI；PIP2A；Aquaporin PIP2-1
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Species
E.coli
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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
P43286
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Expression Region
1-287aa
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AA Sequence
MAKDVEAVPGEGFQTRDYQDPPPAPFIDGAELKKWSFYRAVIAEFVATLLFLYITVLTVIGYKIQSDTDAGGVDCGGVGILGIAWAFGGMIFILVYCTAGISGGHINPAVTFGLFLARKVSLPRALLYIIAQCLGAICGVGFVKAFQSSYYTRYGGGANSLADGYSTGTGLAAEIIGTFVLVYTVFSATDPKRSARDSHVPVLAPLPIGFAVFMVHLATIPITGTGINPARSFGAAVIYNKSKPWDDHWIFWVGPFIGAAIAAFYHQFVLRASGSKSLGSFRSAANV
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Molecular Weight
30.4 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
A2PI, or Alpha-2-plasmin inhibitor, is a crucial serine protease inhibitor that plays a significant role in the regulation of fibrinolysis, the process that prevents blood clots from growing and becoming problematic. The interest in A2PI research has grown due to its potential implications in various medical conditions, particularly cardiovascular diseases, where abnormal clot formation can lead to serious complications. Researchers have been investigating the structure and function of the A2PI protein to better understand its mechanism of action in inhibiting plasmin, the enzyme responsible for breaking down fibrin in blood clots. Studies on recombinant A2PI have highlighted its importance in therapeutic applications, including the development of new anticoagulant therapies and diagnostic tools for monitoring clotting disorders. The production of recombinant A2PI in various systems, such as bacteria or mammalian cells, provides a valuable platform for examining its biochemical properties and therapeutic potential. Furthermore, advancements in biotechnology and protein engineering techniques hold promise for enhancing the efficacy and specificity of A2PI-based treatments. Overall, the ongoing research into A2PI represents a significant intersection of biochemistry, medicine, and therapeutics, with the potential to contribute to better management of thromboembolic diseases and improve patient outcomes.
