Analytical Data
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Gene name
UA
- Application
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Alternative Names
UA；U2AF65；Splicing factor U2AF 65 kDa subunit
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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
Q13838
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Expression Region
2-251aa
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AA Sequence
AENDVDNELLDYEDDEVETAAGGDGAEAPAKKDVKGSYVSIHSSGFRDFLLKPELLRAIVDCGFEHPSEVQHECIPQAILGMDVLCQAKSGMGKTAVFVLATLQQLEPVTGQVSVLVMCHTRELAFQISKEYERFSKYMPNVKVAVFFGGLSIKKDEEVLKKNCPHIVVGTPGRILALARNKSLNLKHIKHFILDECDKMLEQLDMRRDVQEIFRMTPHEKQVMMFSATLSKEIRPVCRKFMQDPMEIFV
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Molecular Weight
55.2kDa
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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
UA (Urokinase-type plasminogen activator) recombinant proteins have gained significant attention in biomedical research due to their pivotal role in various physiological and pathological processes, particularly in fibrinolysis, wound healing, and tissue remodeling. Urokinase is an enzyme that catalyzes the conversion of plasminogen to plasmin, the latter being essential for the breakdown of fibrin in blood clots. Dysregulation of this pathway is associated with numerous conditions, including cardiovascular diseases, cancer metastasis, and inflammatory disorders. As a result, the development of UA recombinant proteins offers promising therapeutic applications, such as in the treatment of thromboembolic disorders and enhancing tissue regeneration. Researchers have been exploring the optimization of expression systems for the production of these proteins, including bacterial, yeast, and mammalian cell systems, to enhance yield, functionality, and safety for clinical use. Furthermore, advancements in genetic engineering and protein purification techniques have facilitated the creation of more effective UA variants with tailored properties for specific medical applications. The growing understanding of UA's biological mechanisms and its interactions with other molecules has also opened avenues for novel drug design and targeted therapies, making UA recombinant proteins a focal point of ongoing research aimed at improving patient outcomes in various diseases. Overall, the study of UA recombinant proteins is a dynamic field that bridges molecular biology and clinical medicine, highlighting the potential for innovative treatments derived from recombinant biotechnology.
