Analytical Data
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Gene name
DLG4
- Application
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Alternative Names
PSD95
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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
P78352-1
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Expression Region
D2-L724
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Protein Length
Partial
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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
DLG4, also known as PSD-95, is a scaffolding protein predominantly expressed in the postsynaptic density of neurons, playing a critical role in synaptic signaling and plasticity. Its structure comprises multiple PDZ (PSD-95/Dlg/ZO-1) domains, which facilitate the clustering of neurotransmitter receptors, such as NMDA and AMPA receptors, as well as various signaling molecules. Research into DLG4 has gained momentum due to its implication in several neurodevelopmental and neuropsychiatric disorders, including schizophrenia, autism, and bipolar disorder, where alterations in synaptic function are evident. Furthermore, DLG4's interaction with other proteins and its role in anchoring signaling pathways make it a valuable target for understanding the molecular mechanisms underlying synaptic dysfunction. The study of DLG4 and its recombinant forms provides essential insights into the modulation of synaptic strength and the development of potential therapeutic strategies for synaptic-related diseases. Advances in recombinant protein technology have enabled the production of DLG4 variants, facilitating detailed investigations into its functional properties and interactions. Overall, research on DLG4 recombinant proteins not only enhances our comprehension of synaptic biology but also holds promise for identifying novel biomarkers and therapeutic targets in the realm of neuropsychiatric disorders.
