Analytical Data
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Gene name
SMO Protein-VLP
- Application
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Alternative Names
SMOH
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Species
Human
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Source
HEK293
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99835
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Expression Region
R28-F787
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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
SMO Protein-VLP (Virus-Like Particles) recombinant proteins have emerged as a significant area of research, particularly in the fields of vaccine development and targeted drug delivery. The Smoothened (SMO) protein, a critical component of the Hedgehog signaling pathway, plays vital roles in various developmental processes and has been implicated in several cancers, notably medulloblastoma. The use of VLPs, which mimic the structure of viruses without containing viral genetic material, presents an innovative strategy for presenting antigens in a manner that elicits strong immune responses. Research into SMO Protein-VLPs focuses on their potential to serve as effective immunogens, stimulating an immune reaction that could lead to both preventive and therapeutic vaccines against SMO-related cancers. Additionally, these VLPs can be engineered to enhance stability and delivery of therapeutic agents, making them versatile tools in biomedicine. The ongoing exploration of SMO Protein-VLPs could pave the way for novel approaches in cancer therapy and immunization strategies, addressing the pressing need for effective treatments in oncology.
