Analytical Data
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Gene name
JUP
- Application
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Alternative Names
DP3; gCat; G-Cat; CTNNG; DPIII; PDGB; PKGB; Gamma Catenin; Desmoplakin III; Desmoplakin-3
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P14923
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Expression Region
Pro574~Ala745
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Molecular Weight
23kDa
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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 JUP (Junctional Plakoglobin) recombinant proteins has gained considerable attention due to its critical role in cell adhesion and signaling pathways. JUP, a member of the plakoglobin family, is a vital cytoplasmic protein that connects cadherins to the actin cytoskeleton, thereby playing a crucial role in maintaining the integrity of epithelial tissues. Its dysfunction has been implicated in various pathological conditions, including cancers and hereditary heart diseases. Researchers are particularly interested in understanding the structure-function relationship of JUP to elucidate its mechanism in intercellular communication and its influence on cell motility and proliferation. The production of recombinant JUP proteins allows for detailed biochemical characterization and functional assays, facilitating the exploration of its interactions with other molecular partners. Furthermore, this research aids in the development of potential therapeutic strategies targeting diseases associated with JUP dysregulation. By employing techniques such as recombinant DNA technology and protein expression systems, scientists have made significant strides in harnessing JUP proteins for both basic research and clinical applications. Overall, the investigation of JUP recombinant proteins stands at the intersection of cellular biology and medical research, promising insights that could lead to innovative approaches in treating related diseases.
