Analytical Data
-
Gene name
GNB5
- Application
-
Alternative Names
Gbeta5Transducin beta chain 5
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O14775
-
Expression Region
1-353aa
-
Molecular Weight
54.8 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
GNB5 is a member of the G-protein β subunit family, playing a crucial role in various signal transduction pathways by forming heterotrimeric G proteins with α and γ subunits. Its involvement in neuronal signaling, modulation of ion channels, and influence on neurotransmitter release highlights its significance in both physiological and pathological processes. Recent studies suggest that GNB5 is implicated in certain neurological disorders, making it a potential target for therapeutic interventions. The research surrounding the recombinant production of GNB5 protein aims to facilitate a deeper understanding of its structural and functional properties. By employing techniques such as recombinant DNA technology, researchers can produce GNB5 in various expression systems, allowing for detailed investigations into its interactions with G-protein coupled receptors (GPCRs) and other cellular components. This knowledge is essential for deciphering the complex roles of GNB5 in cellular signaling and its implications in health and disease. Furthermore, the availability of purified GNB5 protein can enable high-throughput screening for novel compounds that may modulate its activity, providing insights into new therapeutic strategies for conditions linked to G-protein signaling dysfunction. Overall, research on GNB5 recombinant protein not only enhances our understanding of its molecular mechanisms but also paves the way for potential clinical applications in the realms of neurology and pharmacology.
