Analytical Data
-
Gene name
TTL
- Application
-
Species
Human
-
Source
E. coli
-
Tag
Two N- s, His- & SUMO-
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8NG68
-
Expression Region
Met1~Leu377
-
Molecular Weight
57kDa
-
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 research on TTL (tubulin tyrosine ligase) recombinant proteins has gained momentum due to the pivotal role of tubulin post-translational modifications in cellular functions and the dynamics of the cytoskeleton. Tubulin, a fundamental protein that forms microtubules, undergoes various modifications that influence its stability, interactions, and cellular processes, including cell division, intracellular transport, and signaling pathways. TTL specifically catalyzes the attachment of a tyrosine residue to the C-terminal of alpha-tubulin, a modification crucial for proper microtubule dynamics and function. Understanding the mechanisms by which TTL and other tubulin-modifying enzymes operate has significant implications for elucidating cellular behavior in both normal and disease states, particularly in cancer, where microtubule dynamics are often dysregulated. Through the generation and study of recombinant TTL proteins, researchers can investigate its enzymatic activity, interaction with tubulin, and the effects of specific mutations on its function. This research not only contributes to a deeper understanding of microtubule biology but also holds potential therapeutic significance, as modulation of tubulin modifications may offer novel strategies for targeting impaired cellular processes in diseases.
