Analytical Data
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Gene name
GLUB4
- Application
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Species
Oryza sativa subsp. japonica
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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
P14614
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Expression Region
25-303aa
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Molecular Weight
39.5 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
GLUB4, or glutamate-binding protein 4, is a member of a family of proteins that play crucial roles in various physiological processes, including synaptic transmission and glutamate homeostasis in the central nervous system. Research into GLUB4 is driven by its implication in neurological disorders, given that dysregulation of glutamate signaling can lead to conditions such as epilepsy, schizophrenia, and neurodegenerative diseases. The recombinant expression of GLUB4 offers a valuable tool for studying its structure-function relationships, interaction with ligands, and role in neurotransmission. Through the production of GLUB4 as a recombinant protein, researchers can investigate its binding properties, conformational dynamics, and potential therapeutic targets. The elucidation of GLUB4's mechanisms may provide insights into novel treatments for glutamate-related pathologies, making it an important focus within neurobiology and pharmacology research. By employing techniques such as X-ray crystallography and nuclear magnetic resonance (NMR) spectroscopy, scientists aim to characterize the protein's active sites and interactions, furthering our understanding of its functional implications in the brain. As our knowledge of GLUB4 expands, it could pave the way for innovative interventions in the management of glutamate-associated disorders.
