Analytical Data
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Gene name
ABA
- Application
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Alternative Names
ABA；Serine/threonine-Protein phosphatase 2A 55 kDa regulatory subunit B 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
P63151
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Expression Region
1-447aa
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AA Sequence
MAGAGGGNDIQWCFSQVKGAVDDDVAEADIISTVEFNHSGELLATGDKGGRVVIFQQEQENKIQSHSRGEYNVYSTFQSHEPEFDYLKSLEIEEKINKIRWLPQKNAAQFLLSTNDKTIKLWKISERDKRPEGYNLKEEDGRYRDPTTVTTLRVPVFRPMDLMVEASPRRIFANAHTYHINSISINSDYETYLSADDLRINLWHLEITDRSFNIVDIKPANMEELTEVITAAEFHPNSCNTFVYSSSKGTIRLCDMRASALCDRHSKLFEEPEDPSNRSFFSEIISSISDVKFSHSGRYMMTRDYLSVKIWDLNMENRPVETYQVHEYLRSKLCSLYENDCIFDKFECCWNGSDSVVMTGSYNNFFRMFDRNTKRDITLEASRENNKPRTVLKPRKVCASGKRKKDEISVDSLDFNKKILHTAWHPKENIIAVATTNNLYIFQDKVN
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Molecular Weight
51.6 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
ABA (Abscisic Acid) is a critical plant hormone that plays a significant role in regulating various physiological processes, including stomatal closure, seed development, and stress responses. In recent years, the study of ABA-responsive proteins has gained momentum, particularly in the context of plant adaptation to environmental stresses such as drought and salinity. These proteins, often referred to as ABA-repressed proteins (ABAs), contribute to the intricate signaling pathways activated by ABA. Research has shown that ABA signaling is essential for enhancing plant resilience and productivity, especially in changing climate conditions. The identification and characterization of ABA-responsive proteins can provide insights into their roles in mediating the plant's adaptive responses. Moreover, understanding the molecular mechanisms underlying ABA signal transduction is crucial for developing crop varieties with improved stress tolerance. As a result, the exploration of ABA and its associated proteins has emerged as a promising area in plant biotechnology and agricultural research, aiming to optimize plant growth and yield under adverse environmental conditions. This line of research not only contributes to basic plant biology but also holds significant implications for food security and sustainable agriculture in the face of global climate challenges.
