Analytical Data
-
Gene name
OPRk1
- Application
-
Alternative Names
OPR-K; KOR
-
Species
Mouse
-
Source
E. coli
-
Tag
N- His & GST
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P33534
-
Expression Region
Met1~Ala57
-
Molecular Weight
36kDa
-
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
OPRk1 (octopamine/tyramine receptor kinase 1) is a member of the protein kinase family that plays a crucial role in various physiological processes, including signal transduction, cellular response, and metabolic regulation. The research surrounding OPRk1 has gained momentum due to its potential implications in neurobiology and pharmacology, particularly in the modulation of neurotransmitter systems. Octopamine, a biogenic amine, and its receptor pathways are known to influence behaviors such as arousal, motivation, and stress response in both invertebrates and vertebrates. Recent studies have indicated that OPRk1 may be involved in the regulation of metabolic pathways and could serve as a target for therapeutic interventions in metabolic disorders. Furthermore, the exploration of OPRk1 has opened new avenues for understanding the molecular mechanisms underlying neurodegenerative diseases and anxiety-related disorders. Given the intricate relationship between OPRk1 signaling and various signaling cascades, further investigation into its structure-function relationship, spatiotemporal expression patterns, and interaction with other cellular components is warranted. The development of recombinant OPRk1 proteins allows for detailed biochemical analyses and structure elucidation, facilitating the identification of small molecules that may modulate OPRk1 activity. This research has the potential to enhance our understanding of the role of OPRk1 in health and disease, paving the way for novel therapeutic strategies targeting disorders associated with dysregulated octopamine signaling. Overall, the study of OPRk1 recombinant proteins represents a promising area of research with significant implications for both basic science and clinical applications.











