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
TGATFPEEAIADLSVNMYNRLRATGEDENILFSPLSIALAMGMMELGAQGSTQKEIRHSMGYDSLKNGEEFSFLKEFSNMVTAKESQYVMKIANSLFVQNGFHVNEEFLQMMKKYFNAAVNHVDFSQNVAVANYINKWVENNTNNLVKDLVSPRDFDAATYLALINAVYFKGNWKSQFRPENTRTFSFTKDDESEVQIPMMYQQGEFYYGEFSDGSNEAGGIYQVLEIPYEGDEISMMLVLSRQEVPLATLEPLVKAQLVEEWANSVKKQKVEVYLPRFTVEQEIDLKDVLKALGITEIFIKDANLTGLSDNKEIFLSKAIHKSFLEVNEEGSEAAAVSGMIAISRMAVLYPQVIVDHPFFFLIRNRRTGTILFMGRVMHPETMNTSGHDFEEL
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Molecular Weight
44.7 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 A1 or alpha-1 antitrypsin, is a key serine protease inhibitor primarily synthesized in the liver. Its primary function is to regulate enzymes such as neutrophil elastase, thereby protecting tissues from proteolytic damage in inflammatory conditions. Deficiencies or mutations in SerpinI1 are associated with various clinical disorders, including liver disease, emphysema, and increased susceptibility to lung infections. Given its crucial role in maintaining homeostasis in the respiratory and hepatic systems, the study of SerpinI1 has garnered significant attention within the fields of biochemistry and molecular biology. Research into recombinant SerpinI1 has focused on its therapeutic potential for conditions arising from its deficiency, exploring avenues such as gene therapy, protein replacement therapy, and the development of small molecules to enhance its activity. Moreover, understanding the structural dynamics and interaction mechanisms of SerpinI1 is essential for designing effective inhibitors or enhancers. Overall, the recombinant production and study of SerpinI1 provide valuable insights into its biological functions and therapeutic implications, aiming to mitigate the effects of related diseases and improve patient outcomes.
