Analytical Data
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Gene name
Sharpin
- Application
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Alternative Names
(Shank-associated RH domain-interacting protein)
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Species
Rat
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9EQL9
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Expression Region
1-381aa
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Molecular Weight
47.7 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
The study of Sharpin recombinant protein is rooted in its significant role in immune response regulation and cell signaling pathways. Sharpin, or SHANK-associated protein interacting protein, is crucial for maintaining the integrity of the skin and mucosal barriers by influencing the formation of tight junctions and epithelial cell differentiation. Research indicates that mutations in the Sharpin gene can lead to severe inflammatory conditions, exemplifying its importance in the immune system's functionality. In the context of autoimmune diseases, understanding Sharpin's mechanisms can shed light on potential therapeutic targets, as aberrant signaling linked to Sharpin has been associated with disorders such as chronic inflammation and different skin pathologies. Additionally, the expression and purification of Sharpin as a recombinant protein provide a valuable tool for further investigations into its structure-function relationships, paving the way for innovative treatments tailored to manipulate its pathways in disease contexts. As researchers continue to explore the nuances of Sharpin's role in cellular processes, the insights gained could significantly advance our understanding of immune-related disorders and foster the development of targeted interventions.
