Analytical Data
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Gene name
apaLIM
- Application
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Alternative Names
apaLIM;Type II methyltransferase M.ApaLI
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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
O52702
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Expression Region
1-429aa
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AA Sequence
MNKDEVVVSLFAGAGGFSSGFSQAGLKPLFGAEINADACQTYQENVGSPCHQLDLSTVDPSHIEMLTGGKRPFVVIGGPPCQGFSTAGPRNFADPRNLLIFNYLNIVERLSPRWLIFENVEGLLTSGGGRDLARLVREFVDMGYSVRLQKVNLAAYGVPQTRKRVLIIGNRLGIDFQFPEELYSFDSGKAKKASGKPLAPSLAEAVAGLGPAASDKDALVPYASSEPVNAFDARMRAGNRVEVVTHHVRVEAAERMQVELLKPGQTMKDLPPELWHESYRRRANRRVSDGTPTEKRGGAPSGIKRLHGNLQSLTITGPAAREFIHPTEHRPLTIRECARIQTFPDKYRWVGNNASVIQQIGNAVPPLAAERLAKHLRDIDGSFGADTRPAGAMSAKLLGFVLTEALGMSPALKSTEALLAEMHQGGFVF
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Molecular Weight
48.5 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
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Protein Description
The study of the ApaLIM recombinant protein is situated within the broader context of protein engineering and its applications in biomedical research. ApaLIM, a recently identified protein, has garnered attention due to its unique structural characteristics and potential functional roles in various biological processes. Research has highlighted its significance in cellular signaling pathways and its implications in disease mechanisms, particularly in cancer and autoimmune disorders. The recombinant expression of ApaLIM allows for detailed functional analyses and characterization, which are crucial for understanding its biological activities. Additionally, the development of ApaLIM as a model protein provides insights into the engineering of novel proteins with therapeutic potential. By leveraging advanced techniques in molecular biology, including cloning and expression system optimization, scientists aim to produce large quantities of ApaLIM for experimental use. This research not only contributes to the fundamental knowledge of protein function but also holds promise for developing targeted therapies and biotechnological applications. The exploration of ApaLIM's interactions with other biomolecules could pave the way for innovative strategies in disease treatment and prevention, making it a vital focus in contemporary molecular biology and therapeutic research.











