Analytical Data
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Gene name
AAT1
- Application
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Alternative Names
MAATS1; AAT1alpha; MYCBP-binding protein; MYCBP/AMY-1-associated testis-expressed protein 1
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q7Z4T9
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Expression Region
Ser29~Leu181
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Molecular Weight
22kDa
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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
AAT1, or Alpha-1 Antitrypsin 1, is a critical protein that plays a fundamental role in protecting the lungs and liver from damage caused by excessive protease activity, particularly from neutrophil elastase. Deficiencies in AAT can lead to serious health issues, including chronic obstructive pulmonary disease (COPD) and liver disease. Research into AAT1 recombinant proteins has gained significant attention as scientists explore ways to supplement deficient levels in affected individuals and develop potential therapeutic strategies. Recent advancements in recombinant DNA technology and protein engineering have enabled the production of modified AAT1 proteins with enhanced stability and functional activity. Studies have focused on characterizing these recombinant proteins for their ability to inhibit proteolytic enzymes, reduce inflammation, and promote tissue repair. Furthermore, preclinical and clinical trials are underway to assess the efficacy and safety of recombinant AAT1 treatments, paving the way for innovative approaches to treat AAT deficiency and related disorders. Understanding the structure-function relationship of AAT1 and its interaction with various biological systems remains a crucial area of investigation, as it may provide insights into optimizing therapeutic applications and improving patient outcomes.
