Analytical Data
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Gene name
SERPINI1
- Application
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Alternative Names
SERPINI1；PI12；Neuroserpin
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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
Q99574
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Expression Region
17-410aa
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AA Sequence
TGATFPEEAIADLSVNMYNRLRATGEDENILFSPLSIALAMGMMELGAQG STQKEIRHSMGYDSLKNGEEFSFLKEFSNMVTAKESQYVMKIANSLFVQN GFHVNEEFLQMMKKYFNAAVNHVDFSQNVAVANYINKWVENNTNNLVKDL VSPRDFDAATYLALINAVYFKGNWKSQFRPENTRTFSFTKDDESEVQIPM MYQQGEFYYGEFSDGSNEAGGIYQVLEIPYEGDEISMMLVLSRQEVPLAT LEPLVKAQLVEEWANSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIF IKDANLTGLSDNKEIFLSKAIHKSFLEVNEEGSEAAAVSGMIAISRMAVL YPQVIVDHPFFFLIRNRRTGTILFMGRVMHPETMNTSGHDFEEL
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Molecular Weight
45 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
SERPINI1, also known as Serpin Peptidase Inhibitor, clade I, member 1, is a member of the serpin superfamily, which serves as an essential regulatory component in various physiological processes, including protease inhibition, inflammation, and coagulation. Research has demonstrated that SERPINI1 plays a crucial role in several diseases, particularly neurodegenerative disorders and certain cancers, where it may influence tumor progression and metastasis. Its dysregulation has been associated with impaired protease activity, leading to altered homeostasis and exacerbated pathological conditions. Given its significance, the recombinant production of SERPINI1 protein has emerged as a valuable tool for understanding its biological functions and potential therapeutic applications. The development of recombinant SERPINI1 paves the way for in-depth studies regarding its structure-function relationships, and enables high-throughput screening of potential inhibitors or modulators. Furthermore, elucidating the mechanisms underlying SERPINI1's involvement in disease processes may inform the design of innovative therapeutic strategies aimed at restoring its normal function or targeting the pathways it regulates. As such, the study of recombinant SERPINI1 protein not only holds promise for advancing our understanding of serpin biology but also represents a step towards novel interventions in SERPINI1-related pathologies.
