Analytical Data
-
Gene name
ETRB
- Application
-
Alternative Names
ETRB；ETRB；Endothelin receptor type B
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P24530
-
Expression Region
27-442aa
-
AA Sequence
EERGFPPDRATPLLQTAEIMTPPTKTLWPKGSNASLARSLAPAEVPKGDRTAGSPPRTISPPPCQGPIEIKETFKYINTVVSCLVFVLGIIGNSTLLRIIYKNKCMRNGPNILIASLALGDLLHIVIDIPINVYKLLAEDWPFGAEMCKLVPFIQKASVGITVLSLCALSIDRYRAVASWSRIKGIGVPKWTAVEIVLIWVVSVVLAVPEAIGFDIITMDYKGSYLRICLLHPVQKTAFMQFYKTAKDWWLFSFYFCLPLAITAFFYTLMTCEMLRKKSGMQIALNDHLKQRREVAKTVFCLVLVFALCWLPLHLSRILKLTLYNQNDPNRCELLSFLLVLDYIGINMASLNSCINPIALYLVSKRFKNCFKSCLCCWCQSFEEKQSLEEKQSCLKFKANDHGYDNFRSSNKYSSS
-
Molecular Weight
50.3kDa
-
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 study of ETRB (Ethanolamine-Transporting Receptor Protein B) recombinant proteins has gained significant attention in recent years due to their potential applications in various biomedical fields. ETRB is known to play a crucial role in cellular signaling and homeostasis, particularly in the context of membrane transport and nutrient sensing. Recombinant protein technology allows for the production of large quantities of ETRB with controlled purity and activity, enabling detailed studies of its structure-function relationships. Researchers are particularly interested in understanding how ETRB interacts with other cellular components, including ligands and downstream signaling molecules, which may ultimately reveal novel therapeutic targets for diseases linked to dysfunction in these pathways, such as metabolic disorders and cancer. Moreover, advancements in protein engineering techniques have improved the ability to modify ETRB for enhanced stability and activity, paving the way for its use in drug delivery systems and diagnostic tools. Overall, the investigation of ETRB recombinant proteins represents a promising area of research that could provide valuable insights into cellular mechanisms and lead to innovative approaches for treating various health issues.
