Analytical Data
-
Gene name
TTK
- Application
-
Alternative Names
MPS1; MPS1L1; CT96; PYT; Cancer/Testis Antigen 96; Phosphotyrosine picked threonine-protein kinase; Dual specificity protein kinase TTK
-
Species
Rat
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
D4A4S7
-
Expression Region
Glu570~Met787
-
Molecular Weight
30kDa
-
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
TTK, also known as dual-specificity tyrosine phosphorylation-regulated kinase 1A (DYRK1A), is a crucial protein involved in various cellular processes, including cell cycle regulation, neuronal differentiation, and response to DNA damage. Research has increasingly focused on TTK due to its significant role in cancer biology—particularly in the progression of several tumor types—where it has been linked to the regulation of mitotic entry and spindle assembly checkpoint. Recent studies have demonstrated that TTK is often overexpressed in various cancers, making it a potential biomarker for malignancy and a candidate for targeted therapy. Furthermore, the elucidation of TTK's structure and function has paved the way for the development of small-molecule inhibitors that could selectively modulate its activity, thereby offering a promising avenue for therapeutic interventions. The incorporation of recombinant protein technologies has facilitated the production of functional TTK proteins, allowing for in-depth studies of its enzymatic activity, substrate interactions, and downstream signaling pathways. By generating and characterizing TTK recombinant proteins, researchers aim to uncover the intricate mechanisms governing TTK's role in oncogenesis and explore its potential as a therapeutic target, making it a significant focus in the field of cancer research and drug development.
