Analytical Data
-
Gene name
EphA4
- Application
-
Alternative Names
HEK8; SEK; TYRO1; EPH-like kinase 8; Tyrosine-protein kinase receptor SEK
-
Species
Human
-
Source
E. coli
-
Tag
N- His & GST
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
P54764
-
Expression Region
Ile621~Ile882
-
Protein Length
Partial
-
Molecular Weight
60kDa
-
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
EphA4, a member of the ephrin receptor family, plays a crucial role in various biological processes, including cell adhesion, migration, and neural development. Its interaction with ephrin ligands is significant in mediating bidirectional signaling pathways that influence cellular behaviors in different tissues. Dysregulation of EphA4 has been implicated in several pathologies, including cancer, neurological disorders, and cardiovascular diseases, making it an important target for therapeutic interventions. Research on recombinant EphA4 protein has gained momentum due to the potential of modulating its signaling pathways for clinical applications. By generating and studying recombinant EphA4, scientists aim to better understand its functional mechanisms and explore its role in disease progression and treatment. Techniques such as protein engineering and expression in various systems facilitate the production of functional EphA4 proteins, which can be used for binding assays, structural studies, and potential drug development. Moreover, understanding EphA4's molecular structure and its interactions with ligands could lead to the design of selective inhibitors or agonists, providing new strategies for combating diseases associated with EphA4 dysregulation. Overall, the study of recombinant EphA4 protein is pivotal in unveiling its biological significance and advancing therapeutic approaches targeting EphA4-related pathways.
