Analytical Data
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Gene name
SUS1
- Application
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Alternative Names
Sucrose-UDP glucosyltransferase
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Species
Saccharum officinarum
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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
P31925
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Expression Region
1-218aa
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Molecular Weight
41.3 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
SUS1, a key component of the transcription and splicing machinery, plays a crucial role in the regulation of gene expression and RNA processing in eukaryotic cells. It is involved in the assembly of spliceosomal complexes and is known to interact with various RNA-binding proteins and transcription factors. The research on SUS1 recombinant proteins has gained significant attention due to its potential implications in understanding cellular processes related to gene regulation, alternative splicing, and the overall mechanisms of mRNA maturation. Studying SUS1 in a recombinant form allows researchers to elucidate its structure-function relationships, explore specific protein interactions, and assess its functional roles in various biological contexts. Moreover, investigating SUS1 may provide insights into the molecular basis of certain diseases associated with splicing defects and dysregulated transcription, thereby highlighting its significance as a target for therapeutic interventions. Furthermore, advancements in protein expression systems have made it increasingly feasible to produce and characterize SUS1 as a purified recombinant protein, paving the way for detailed biochemical and biophysical analyses. Such studies are vital for understanding how SUS1 integrates into the larger network of gene expression regulation and may offer novel perspectives on cellular homeostasis and pathology.
