Analytical Data
-
Gene name
CYTH4
- Application
-
Alternative Names
PSCD4; CYT4; Pleckstrin Homology,Sec7 And Coiled-Coil Domains 4
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9UIA0
-
Expression Region
Met1~Phe379
-
Molecular Weight
48kDa
-
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
CYTH4 (CYT homology domain-containing protein 4) is a member of a larger family of proteins known for their involvement in cellular signaling and cytoskeletal organization. Research on CYTH4 has gained attention due to its potential roles in various physiological processes, including cell polarity, migration, and morphology. Notably, CYTH4 has been implicated in different diseases, including cancer and neurological disorders, where its expression levels and functional alterations could contribute to disease progression. The characterization of CYTH4 recombinant proteins is essential for understanding its biological functions and mechanisms of action. By producing these proteins through recombinant DNA technology, researchers can investigate their interactions with other cellular molecules, elucidating their pathways in both normal and pathological conditions. Additionally, studying CYTH4’s structural features and functional domains can provide insights into the therapeutic potential of targeting this protein. Given the complexities of its regulatory mechanisms, ongoing research aims to clarify the diverse roles of CYTH4 in cellular processes and its potential as a biomarker or therapeutic target in various diseases. As such, the study of CYTH4 recombinant proteins offers significant promise in advancing our understanding of cellular dynamics and developing new therapeutic strategies.
