Analytical Data
-
Gene name
talB
- Application
-
Alternative Names
talB；Talin-B
-
Species
E.coli
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P0A870
-
Expression Region
2-317aa
-
AA Sequence
TDKLTSLRQYTTVVADTGDIAAMKLYQPQDATTNPSLILNAAQIPEYRKLIDDAVAWAKQQSNDRAQQIVDATDKLAVNIGLEILKLVPGRISTEVDARLSYDTEASIAKAKRLIKLYNDAGISNDRILIKLASTWQGIRAAEQLEKEGINCNLTLLFSFAQARACAEAGVFLISPFVGRILDWYKANTDKKEYAPAEDPGVVSVSEIYQYYKEHGYETVVMGASFRNIGEILELAGCDRLTIAPALLKELAESEGAIERKLSYTGEVKARPARITESEFLWQHNQDPMAVDKLAEGIRKFAIDQEKLEKMIGDLL
-
Molecular Weight
42.5 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
TalB is a type of protein known as a transcription activator-like (TAL) effector, which is derived from certain plant pathogenic bacteria, particularly from the genus Xanthomonas. These proteins have evolved the capability to specifically bind to host plant genomes, leading to the activation of specific host genes and the subsequent manipulation of plant susceptibility to infection. The study of TalB and similar TAL effectors has garnered significant interest due to their potential applications in biotechnology and plant protection. Researchers aim to harness these proteins for creating genetically modified crops with enhanced resistance to diseases and environmental stressors. Additionally, the precision with which TalB can target specific DNA sequences makes it a valuable tool in genome editing technologies, akin to CRISPR-Cas systems. Understanding the mechanisms underlying TalB function and interaction with host plant DNA not only provides insights into plant-pathogen interactions but also contributes to the development of innovative agricultural practices aimed at improving crop yield and sustainability. The ongoing research into TalB reconstitutes an essential part of the broader field of synthetic biology, where natural protein functionalities are repurposed for human benefit, highlighting both the complexity of plant immune responses and the ingenuity of nature's evolutionary adaptations.
