Analytical Data
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Gene name
AA
- Application
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Alternative Names
AA；Serine/threonine-Protein phosphatase 2A catalytic subunit alpha isoform
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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
P67775
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Expression Region
1-309aa
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AA Sequence
MDEKVFTKELDQWIEQLNECKQLSESQVKSLCEKAKEILTKESNVQEVRCPVTVCGDVHGQFHDLMELFRIGGKSPDTNYLFMGDYVDRGYYSVETVTLLVALKVRYRERITILRGNHESRQITQVYGFYDECLRKYGNANVWKYFTDLFDYLPLTALVDGQIFCLHGGLSPSIDTLDHIRALDRLQEVPHEGPMCDLLWSDPDDRGGWGISPRGAGYTFGQDISETFNHANGLTLVSRAHQLVMEGYNWCHDRNVVTIFSAPNYCYRCGNQAAIMELDDTLKYSFLQFDPAPRRGEPHVTRRTPDYFL
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Molecular Weight
35.5 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
AA recombinant proteins have garnered significant attention in the fields of biotechnology and medicine due to their diverse applications, including therapeutic development, vaccine formulation, and diagnostic tools. The study of these proteins is rooted in the understanding of their structural and functional properties, as they often serve as models for studying protein interactions and modifications. Advances in genetic engineering techniques, such as CRISPR and recombinant DNA technology, have facilitated the production of high-yield, biologically active AA proteins in various host systems, including bacteria, yeast, and mammalian cells. Researchers focus on optimizing expression systems and purification methods to achieve proteins with desired folding and activity. Additionally, AA recombinant proteins play a crucial role in elucidating mechanisms of disease, providing insights into cellular processes, and identifying potential drug targets. As the demand for novel therapeutics continues to rise, efforts to harness the unique characteristics of AA proteins—such as their stability, specificity, and immunogenicity—have led to innovative approaches in drug design and personalized medicine. Furthermore, ongoing research aims to enhance our understanding of AA protein post-translational modifications and their implications for biological functions, ultimately driving advancements in both academic research and clinical applications. This collective research background underscores the critical importance of AA recombinant proteins in addressing contemporary challenges in health and medicine.
