Analytical Data
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Gene name
SERPINA3-5
- Application
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Alternative Names
SERPINA3-5; Serpin A3-5
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Species
Bovine
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Source
Yeast
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A2I7N1
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Expression Region
25-411aa
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Molecular Weight
47.8 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
Related Products
Protein Description
SERPINA3-5, a member of the serine protease inhibitor (SERPIN) family, plays a crucial role in various biological processes, including inflammation, immune response, and cellular regulation. It is primarily known for its capacity to inhibit a range of serine proteases, thereby modulating proteolytic activity and maintaining homeostasis within the extracellular environment. Research has increasingly focused on SERPINA3-5 due to its potential implications in various diseases, including cancer and neurodegenerative disorders, where dysregulation of protease activity is often observed. The recombinant protein version of SERPINA3-5 offers a valuable tool for detailed functional studies, enabling researchers to explore its structural properties and interactions with target proteases. Understanding the mechanism of action of SERPINA3-5 could offer insights into therapeutic avenues for conditions influenced by proteolytic imbalance. Additionally, the development of recombinant technologies has facilitated the large-scale production of SERPINA3-5, enhancing its availability for experimental applications and potential clinical use. As we delve deeper into the characterization of SERPINA3-5, it becomes increasingly clear that its role extends beyond mere inhibition of proteases, potentially influencing broader biological pathways. This highlights the need for comprehensive studies investigating the multifaceted functions of SERPINA3-5 and its implications in health and disease.
