Analytical Data
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Gene name
STRAP
- Application
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Alternative Names
MAP activator with WD repeats UNR-interacting protein WD-40 repeat protein PT-WD
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y3F4
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Expression Region
1-350aa
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Molecular Weight
65.4 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
STRAP (Serine/Threonine-Protein Kinase and RNA-Binding Protein) is an important regulator of various cellular processes, including cell growth, differentiation, and stress response. Its role as a cofactor in signaling pathways, particularly those mediated by transforming growth factor-beta (TGF-β), highlights its significance in cellular communication and development. Research into STRAP has gained momentum due to its potential implications in various diseases, including cancer and fibrotic disorders. The protein's multifunctionality, which involves both protein kinase activity and RNA-binding capabilities, underpins its involvement in post-transcriptional regulation and signal transduction. Moreover, STRAP's interaction with other signaling molecules and its influence on gene expression make it a critical subject of study for understanding the molecular mechanisms underlying pathophysiological conditions. Current investigations are focused on elucidating the structural basis of STRAP's interactions and determining its precise role in cellular contexts, which may open new avenues for therapeutic interventions targeting dysregulated signaling pathways associated with diseases. This research is essential not only for gaining insights into fundamental biological processes but also for translating findings into clinical applications that can improve disease management and treatment strategies.
