Analytical Data
-
Gene name
YNK1
- Application
-
Alternative Names
YNK1;pqn-58;Apoptosis-linked gene 2-interacting Protein X 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P36010
-
Expression Region
1-153aa
-
AA Sequence
MSSQTERTFIAVKPDGVQRGLVSQILSRFEKKGYKLVAIKLVKADDKLLEQHYAEHVGKPFFPKMVSFMKSGPILATVWEGKDVVRQGRTILGATNPLGSAPGTIRGDFGIDLGRNVCHGSDSVDSAEREINLWFKKEELVDWESNQAKWIYE
-
Molecular Weight
37.2 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
YNK1, or YlqG-like kinase 1, is a serine/threonine kinase implicated in various cellular processes, including cell cycle regulation and stress responses. Research into YNK1 has gained momentum due to its potential role in cancer biology and neurodegenerative diseases, where dysregulation of kinase activities can lead to aberrant signaling pathways. The study of recombinant YNK1 proteins allows researchers to explore their enzymatic functions, substrate specificity, and interactions with other cellular molecules. Recent investigations have focused on the crystallization and structural characterization of YNK1 to understand its catalytic mechanism and regulation. Additionally, understanding the post-translational modifications of YNK1 can provide insights into its functional versatility and involvement in disease states. Overall, the exploration of YNK1 as a therapeutic target has become a compelling area of study in the broader context of kinase research, highlighting its significance in developing novel treatments for various pathologies.











