Analytical Data
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Gene name
Syntenin-1
- Application
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Alternative Names
(Melanoma differentiation-associated protein 9)(MDA-9)(Pro-TGF-alpha cytoplasmic domain-interacting protein 18)(TACIP18)(Scaffold protein Pbp1)(Syndecan-binding protein 1)
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Species
Human
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Source
E. coli
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Tag
N- His-GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O00560
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Expression Region
2-298aa
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Molecular Weight
63.8 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
Syntenin-1 is a multifunctional protein that plays a pivotal role in various cellular processes, including signal transduction, endosomal sorting, and cytoskeletal dynamics. It functions as an adaptor protein, linking various signaling pathways to the endosomal compartments and facilitating the transport of cargo within the cell. Research has shown that Syntenin-1 interacts with multiple binding partners, which suggests its involvement in diverse biological processes such as cancer progression, cell migration, and immune responses. The interest in Syntenin-1 has been fueled by its potential as a therapeutic target, particularly in cancers where its expression levels are altered. The recombinant production of Syntenin-1 allows for in-depth studies on its structural and functional properties, enabling researchers to explore its role in pathophysiological conditions. By generating Syntenin-1 as a recombinant protein, scientists can investigate its interactions with other proteins and its downstream effects on cellular functions, thereby shedding light on its contributions to disease mechanisms. Moreover, understanding the biophysical characteristics of Syntenin-1 can inform drug design strategies aimed at modulating its activity. Overall, the study of recombinant Syntenin-1 represents a promising avenue for elucidating its biological roles and identifying potential interventions in diseases associated with its dysregulation.
