Analytical Data
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Gene name
PLAU
- Application
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Alternative Names
SERPINA5;PCI;PLANH3;PROCI;Plasma serine protease inhibitor
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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
P00749
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Expression Region
21-431aa
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AA Sequence
SNELHQVPSNCDCLNGGTCVSNKYFSNIHWCNCPKKFGGQHCEIDKSKTC YEGNGHFYRGKASTDTMGRPCLPWNSATVLQQTYHAHRSDALQLGLGKHN YCRNPDNRRRPWCYVQVGLKPLVQECMVHDCADGKKPSSPPEELKFQCGQ KTLRPRFKIIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVI SATHCFIDYPKKEDYIVYLGRSRLNSNTQGEMKFEVENLILHKDYSADTL AHHNDIALLKIRSKEGRCAQPSRTIQTICLPSMYNDPQFGTSCEITGFGK ENSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTKMLCAADPQWKTD SCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPWIR SHTKEENGLAL
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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
Plasminogen activator, urokinase (PLAU), is a serine protease that plays a crucial role in the fibrinolytic system, which is responsible for the breakdown of fibrin in blood clots. Its primary function is to convert plasminogen to plasmin, an enzyme that dissolves fibrin and aids in tissue remodeling and wound healing. The study of PLAU recombinant proteins has gained significant attention due to its implications in various physiological and pathological conditions, including cancer metastasis, cardiovascular diseases, and inflammatory disorders. Researchers have been particularly interested in understanding the molecular mechanisms of PLAU and its interactions with other proteins in the extracellular matrix. Additionally, the manipulation of PLAU activity through recombinant technologies has potential therapeutic applications, such as developing novel anticoagulants or enhancing wound healing strategies. By exploring the structural and functional properties of PLAU, scientists aim to improve our understanding of its role in disease processes and to harness its potential for clinical applications. This ongoing research is vital for identifying new biomarkers for disease progression and for formulating targeted therapies that can effectively modulate PLAU activity in various medical contexts.
