Analytical Data
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Gene name
SERPINE2
- Application
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Alternative Names
Peptidase inhibitor 7 Short name: PI-7 Protease nexin 1 Short name: PN-1 Protease nexin I Serpin E2
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P07093
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Expression Region
20-398aa
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Molecular Weight
57.9 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
Related Products
Protein Description
SERPINE2, also known as Neuroserpin, is a member of the serine protease inhibitor family, primarily expressed in the central nervous system. Its main function is to regulate proteolytic enzymes, playing a critical role in neuroprotection and synaptic plasticity. Dysregulation of SERPINE2 has been implicated in various neurodegenerative diseases, including Alzheimer's disease and traumatic brain injury, where it may contribute to neuronal damage and inflammation. Researchers have been focusing on the recombinant production of SERPINE2 to explore its biological functions in greater detail and assess its potential as a therapeutic target. The ability to produce this protein in large quantities allows for structural and functional studies, which contribute to our understanding of its role in neuronal health and disease. Moreover, the development of SERPINE2 as a biomarker or therapeutic agent could provide novel interventions for neurological disorders. As such, studying recombinant SERPINE2 is pivotal for advancing our knowledge in neurobiology and developing new strategies for tackling neurodegenerative diseases.
