Analytical Data
-
Gene name
G16R,E27Q
- Application
-
Alternative Names
Beta-2 adrenoreceptor Short name: Beta-2 adrenoceptor
-
Species
Human
-
Source
E. coli
-
Tag
N- His-SUMO
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P07550
-
Expression Region
1-413aa(G16R&E27Q)
-
Molecular Weight
62.5 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
The G16R and E27Q mutations in the G protein-coupled receptor (GPCR) family, particularly the serotonin 5-HT2A receptor, have garnered significant attention due to their implications in neuropsychiatric disorders and cellular signaling pathways. These mutations are primarily studied in the context of altered receptor activity and pharmacological responses. The G16R mutation, resulting in a glycine to arginine substitution at position 16, has been linked to enhanced receptor signaling and increased affinity for certain ligands, potentially leading to altered serotoninergic transmission. Conversely, the E27Q mutation, which replaces glutamic acid with glutamine at position 27, often modifies the receptor's interaction with G proteins and downstream signaling mechanisms. Research into these recombinant proteins aims to elucidate the structural and functional consequences of these mutations, allowing for a deeper understanding of GPCR dynamics, receptor-ligand interactions, and their roles in disease mechanisms. Moreover, studying G16R and E27Q variants provides insights into the development of targeted pharmacological therapies, as abnormalities in GPCR signaling are frequently implicated in conditions such as schizophrenia and depression. As such, the investigation of these mutations not only advances the fundamental understanding of receptor biology but also holds promise for therapeutic innovations in psychotropic drug development.
