Analytical Data
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Gene name
DLG5
- Application
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Alternative Names
DLG5；KIAA0583；PDLG；Disks large homolog 5
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8TDM6
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Expression Region
全长
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AA Sequence
full
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Molecular Weight
213.8 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
Related Products
Protein Description
DLG5 (Discs Large Homolog 5) is a member of the DLG protein family, which plays a crucial role in maintaining cell polarity, synaptic development, and signal transduction in neurons. The significance of DLG5 has grown in recent years due to its involvement in various neurodegenerative diseases and its potential as a biomarker for psychiatric disorders. Research has shown that DLG5 is associated with synaptic functions and cellular signaling pathways, particularly in the context of glutamate receptors, which are essential for synaptic plasticity and cognitive processes. Advances in recombinant protein technology have facilitated the production of DLG5 in sufficient quantities, enabling in-depth studies of its structure and function. Investigating the recombinant form of DLG5 can provide insights into its role in neurotransmission, cellular architecture, and potential interactions with other synaptic proteins. Additionally, understanding how mutations or dysregulation of DLG5 may contribute to neurodevelopmental disorders holds promise for developing therapeutic strategies. This research underscores the importance of DLG5 not only as a structural protein but also as a pivotal player in cellular communication within the nervous system.
