Analytical Data
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Gene name
ail
- Application
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Alternative Names
ailAttachment invasion locus protein
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Species
Yersinia enterocolitica
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P16454
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Expression Region
24-178aa
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Molecular Weight
33.2 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
AIL (Arabidopsis Inflorescence Locus) recombinant proteins have garnered significant attention in plant biology due to their crucial roles in the regulation of floral development and inflorescence architecture. Understanding the molecular mechanisms governing flower formation is essential not only for basic plant science but also for agricultural applications, as it directly impacts crop yield and quality. The AIL family of transcription factors, characterized by the presence of a basic helix-loop-helix (bHLH) domain, plays a key role in modulating gene expression involved in meristem identity and flower development. Recent advances in molecular biology techniques, such as CRISPR-Cas9 and advanced recombinant protein expression systems, have enabled researchers to investigate the function of AIL proteins in more detail. By producing AIL recombinant proteins in heterologous systems, scientists can conduct binding assays, functional analyses, and protein interaction studies to elucidate their specific roles in developmental processes. This research not only provides insight into the genetic and biochemical pathways that govern floral development but also holds promise for biotechnological innovations aimed at improving flowering traits in economically important crops. As the global population continues to grow, enhancing agricultural productivity by manipulating flowering behaviors through the insights gained from AIL research could be pivotal for food security in the future.
