Analytical Data
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Gene name
Serpina3k
- Application
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Alternative Names
Serpina3k；Mcm2；Spi2；Serine protease inhibitor A3K
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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
P07759
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Expression Region
22-418aa
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AA Sequence
FPDGTKEMDIVFHEHQDNGTQDDSLTLASVNTDFAFSLYKKLALKNPDTNIVFSPLSISAALALVSLGAKGKTMEEILEGLKFNLTETPEADIHQGFGNLLQSLSQPEDQDQINIGNAMFIEKDLQILAEFHEKTRALYQTEAFTADFQQPTEAKNLINDYVSNQTQGMIKELISELDERTLMVLVNYIYFKGKWKISFDPQDTFESEFYLDEKRSVKVPMMKMKLLTTRHFRDEELSCSVLELKYTGNASALLILPDQGRMQQVEASLQPETLRKWRKTLFPSQIEELNLPKFSIASNYRLEEDVLPEMGIKEVFTEQADLSGITETKKLSVSQVVHKAVLDVAETGTEAAAATGVIGGIRKAILPAVHFNRPFLFVIYHTSAQSILFMAKVNNPK
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Molecular Weight
49.8 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
Serpina3k, a member of the serpin superfamily, plays a crucial role in regulating various physiological processes, including immune response, inflammation, and apoptosis. This protein acts as an inhibitor of serine proteases, contributing to the modulation of proteolytic activity in the extracellular environment. Given its involvement in numerous pathophysiological conditions, such as cancer and autoimmune diseases, understanding the structure and function of Serpina3k is vital for potential therapeutic applications. Recent studies have highlighted the importance of reconstituting Serpina3k as a recombinant protein, allowing researchers to investigate its functional properties more effectively. The ability to produce Serpina3k in microbial or mammalian expression systems facilitates the study of its interaction with specific targets and its biological effects. Moreover, recombinant Serpina3k can be utilized in drug development and diagnostic applications, making it a promising candidate for further exploration. As the understanding of Serpina3k's role in disease continues to expand, research into its recombinant form will provide valuable insights into the mechanisms underlying its function and the potential for novel treatment strategies. Overall, the study of recombinant Serpina3k is pivotal for advancing our knowledge of serpin biology and its implications in health and disease.
