Analytical Data
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Gene name
Serpina3n
- Application
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Alternative Names
Serpina3n；Spi2；Serine protease inhibitor A3N
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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
P29508
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Expression Region
1-390aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMNSLSEANTKFMFDLFQQFRKSKENNI FYSPISITSALGMVLLGAKDNTAQQIKKVLHFDQVTENTTGKAATYHVDR SGNVHHQFQKLLTEFNKSTDAYELKIANKLFGEKTYLFLQEYLDAIKKFY QTSESVDFANAPEESRKKINSWVESQTNEKIKNLIPEGNIGSNTTLVLNA IYFKGQWEKKFNKEDTKEEKFWPNKNTYKSIQMMRQYTSFHFASLEDVQA KVLEIPYKGKDLSMIVLLPNEIDGLQKLEEKLTAEKLMEWTSLQNMRETR VDLHLPRFKVEESYDLKDTLRTMGMVDIFNGDADLSGMTGSRGLVLSGVL HKAFVEVTEEGAEAAAATAVVGFGSSPTSTNEEFHCNHPFLFFIRQNKTN SILFYGRFSSP
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Molecular Weight
47 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
Serpina3n, a member of the serine proteinase inhibitors (serpins) family, has garnered significant attention in biomedical research due to its potential roles in various physiological and pathological processes. Originally identified for its involvement in the regulation of inflammation and immune responses, Serpina3n has been linked to multiple diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. Its ability to inhibit serine proteases implies a crucial function in maintaining homeostasis within the extracellular environment. Researchers are particularly interested in understanding the structural and functional properties of recombinant Serpina3n, as these insights could lead to the development of novel therapeutic strategies. Recombinant protein expression systems allow for the production of Serpina3n in a controlled manner, enabling detailed studies on its activity, interaction with target proteases, and potential applications in drug design. By elucidating the mechanisms through which Serpina3n exerts its effects, scientists hope to uncover new biomarkers for disease progression and develop targeted interventions that leverage its inhibitory functions. This research is further supported by advances in proteomics and structural biology, which facilitate the exploration of Serpina3n's complex interactions and regulatory networks within the body. Overall, the study of Serpina3n as a recombinant protein offers promising avenues for enhancing our understanding of its biological significance and therapeutic potential.
