Analytical Data
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Gene name
uPA
- Application
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Alternative Names
uPA；UPA；Proline-rich acidic Protein 1
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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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Molecular Weight
45 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
The study of urokinase-type plasminogen activator (uPA) recombinant proteins has gained significant attention in the fields of cancer research, thrombosis, and tissue remodeling due to the pivotal role that uPA plays in physiological and pathological processes. uPA is a serine protease that converts plasminogen to plasmin, facilitating extracellular matrix degradation and cellular invasion, which are essential mechanisms in tumor metastasis and angiogenesis. Dysregulation of uPA activity is implicated in various malignancies, making it a potential biomarker for cancer progression and a target for therapeutic intervention. The advent of recombinant DNA technology has enabled the production of uPA in heterologous systems, allowing for the generation of high-purity recombinant proteins that can be used for functional studies, drug development, and potential therapeutic applications. Research focusing on the structural and functional characterization of uPA, as well as its interactions with specific inhibitors and receptors, has provided insights into its enzymatic mechanism and regulatory pathways. Furthermore, recombinant uPA has been explored as a tool in drug delivery systems and as a component of biosensors, highlighting its versatility beyond conventional therapeutic applications. As the understanding of uPA's roles continues to evolve, the development of recombinant uPA proteins promises to enhance diagnostic and therapeutic strategies, providing a foundational aspect of translational research in oncology and related fields.
