Analytical Data
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Gene name
PRSS12
- Application
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Alternative Names
PRSS12；Neurotrypsin
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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
P56730
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Expression Region
631-874aa
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AA Sequence
IIGGKNSLRGGWPWQVSLRLKSSHGDGRLLCGATLLSSCWVLTAAHCFKRYGNSTRSYAVRVGDYHTLVPEEFEEEIGVQQIVIHREYRPDRSDYDIALVRLQGPEEQCARFSSHVLPACLPLWRERPQKTASNCYITGWGDTGRAYSRTLQQAAIPLLPKRFCEERYKGRFTGRMLCAGNLHEHKRVDSCQGDSGGPLMCERPGESWVVYGVTSWGYGCGVKDSPGVYTKVSAFVPWIKSVTK
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Molecular Weight
43.4kDa
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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
PRSS12, also known as tumor-associated trypsinogen, is a serine protease that plays a crucial role in various physiological and pathological processes, particularly in cancer biology. Researchers have identified PRSS12 as a potential biomarker for several types of cancers due to its altered expression patterns in tumor tissues compared to normal tissues. As a serine protease, PRSS12 is involved in the activation of other proteolytic enzymes and signaling pathways, influencing cell proliferation, migration, and invasion—all critical factors in tumor development and progression. The study of PRSS12 has garnered attention for its potential to enhance our understanding of cancer mechanisms and for its utility in diagnostic and therapeutic applications. Recent advancements in recombinant protein technology have enabled the production of PRSS12 in significant quantities, facilitating detailed biochemical and structural studies. By investigating its enzymatic activity and substrate specificity, researchers aim to unravel the functional roles of PRSS12 in different cellular contexts. Furthermore, the development of PRSS12-targeted therapies could open new avenues for innovative cancer treatment strategies, focusing on disrupting its activity or mitigating its effects on tumor cell behavior. Given the critical implications of PRSS12 in tumor biology, ongoing research is essential to fully elucidate its role and therapeutic potential, paving the way for future clinical applications.
