Analytical Data
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Gene name
aac
- Application
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Alternative Names
aac；Alpha-actinin-3
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Species
E.coli
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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
P29958
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Expression Region
35-214aa
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AA Sequence
GGYAALIRRASYGVPHITADDFGSLGFGVGYVQAEDNICVIAESVVTANGERSRWFGATGPDDADVRTTSSTQAIDDRVAERLLEGPRDGVRAPCDDVRDQMRGFVAGYNHFLRRTGVHRLTDPACRGKAWVRPLSEIDLWRTSWDSMVRAGSGALLDGIVAATPPTAAGPASAPEAPDA
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Molecular Weight
35.1kDa
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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
AAC, or Amino Acid-Comparative, recombinant proteins have garnered significant attention in recent years due to their potential applications in various fields, including medicine, biotechnology, and pharmaceuticals. The primary aim of AAC research is to create proteins that can mimic or enhance the function of naturally occurring proteins, thereby offering innovative solutions for treating diseases and improving agricultural practices. By employing advanced recombinant DNA technology, researchers can manipulate genetic sequences to produce proteins with desired characteristics, such as increased stability, improved efficacy, or novel functions. This approach not only accelerates the process of protein discovery and optimization but also facilitates large-scale production, making them more accessible for industrial applications. Furthermore, the therapeutic potential of AAC recombinant proteins is being explored in the context of enzyme replacement therapy, monoclonal antibodies, and vaccine development. As a result, understanding the structure-function relationships of these proteins is crucial for designing targeted therapies. The continuous advancement in bioinformatics and structural biology tools, coupled with an increasing emphasis on personalized medicine, promises to expand the horizons of AAC recombinant protein research, paving the way for breakthroughs in disease management and treatment.
