Analytical Data
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Gene name
ugd
- Application
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Alternative Names
ugd; pmrE; udg; yefA; b2028; JW2010; UDP-glucose 6-dehydrogenase; UDP-Glc dehydrogenase; UDP-GlcDH; UDPGDH; EC 1.1.1.22
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Species
Escherichia coli
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P76373
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Expression Region
2-388aa
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Molecular Weight
47.5 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
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Protein Description
Urokinase-type plasminogen activator (uPA) plays a crucial role in various physiological and pathological processes, including tissue remodeling, wound healing, and tumor metastasis. The uPA system is integral to the plasminogen activation cascade, mediating the conversion of plasminogen to plasmin, thus promoting extracellular matrix degradation and facilitating cellular migration. Research has increasingly focused on the development and application of recombinant uPA proteins, particularly their potential as therapeutic agents in treating diseases characterized by excessive fibrinolysis or as targeted delivery systems for drugs in cancer therapy. Additionally, recombinant uPA can serve as a valuable tool for studying proteolytic processes and their implications in health and disease. Advances in molecular biology techniques have enabled the production of modified uPA variants with altered activity or specificity, enhancing their utility. Moreover, the investigation of uPA's role in tumor biology has led to the exploration of its potential as a biomarker for cancer prognosis and treatment response. Understanding uPA’s functions and mechanisms is not only vital for improving therapeutic strategies but also for developing diagnostic tools that can better predict disease outcomes. This growing body of research aims to elucidate the intricate balance of uPA in both promoting and inhibiting pathological processes, thus providing insights into novel approaches for disease intervention and management.
