Analytical Data
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Gene name
SBEM
- Application
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Alternative Names
SBEM；SBEM；Mucin-like Protein 1
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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
Q96DR8
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Expression Region
21-90aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSNPTTAAPADTYPATGPADDEAPDAETT AAATTATTAAPTTATTAASTTARKDIPVLPKWVGDLPNGRVCP
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Molecular Weight
9 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
SBEM (Spindlin-1 Binding and Exporting Module) is a significant focus in the field of protein research due to its potential implications in various biological processes and diseases. This modular protein, originally identified for its role in binding specific RNA sequences, has garnered attention for its involvement in gene regulation and cellular signaling pathways. SBEM is believed to play a crucial role in the nuclear export of RNA and proteins, making it essential for maintaining cellular homeostasis. Researchers are increasingly interested in understanding the molecular mechanisms underlying SBEM's function, particularly its interactions with other proteins and nucleic acids. Given its implications in cancer biology and developmental processes, SBEM offers a promising target for therapeutic interventions. The ongoing studies aim to elucidate the structural and functional characteristics of SBEM, paving the way for innovative strategies in drug design and molecular therapies that could address diseases linked to dysregulation of its pathways. Through advanced techniques such as X-ray crystallography and cryo-electron microscopy, scientists are working to characterize the protein's structure in detail, facilitating the development of specific inhibitors or modulators that could provide new avenues for treatment. As research progresses, SBEM stands out as a critical protein that not only deepens our understanding of fundamental cellular processes but also presents opportunities for impactful medical advancements.
