Analytical Data
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Gene name
Serpine2
- Application
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Alternative Names
SERPINE2;PI7;PN1;Glia-derived nexin
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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
P07093
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Expression Region
20-398aa
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AA Sequence
SHFNPLSLEELGSNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVGKILKKINKAIVSKKNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGVLTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNDLWYNFIELPYHGESISMLIALPTESSTPLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSSKANFAKITTGSENLHVSHILQKAKIEVSEDGTKASAATTAILIARSSPPWFIVDRPFLFFIRHNPTGAVLFMGQINKP
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Molecular Weight
48.8 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
Serpine2, also known as Serpin E2, is a member of the serpin (serine protease inhibitor) superfamily, which plays critical roles in various physiological processes, including regulation of immune responses, cell migration, and tissue remodeling. Research into Serpine2 has gained traction due to its involvement in pathological conditions such as cancer, neurodegenerative diseases, and cardiovascular disorders. It has been implicated in modulating protease activities, which are essential for maintaining homeostasis in extracellular matrices and inflammatory responses. The interest in recombinant Serpine2 proteins stems from the need to elucidate its biological functions and therapeutic potential. Recombinant protein production allows for detailed structural and functional studies, as well as the generation of specific antibodies for use in diagnostics and research. Recent studies have shown that Serpine2 may influence tumor progression and metastasis, making it a potential target for novel therapeutic strategies. Additionally, understanding its mechanisms could provide insights into the development of biomolecular tools for treating diseases associated with dysregulated protease activity. Overall, the characterization of recombinant Serpine2 protein is a pivotal area of research that could unveil new pathways for intervention in various diseases, highlighting its significance in both basic and applied biomedical sciences.
