Analytical Data
-
Gene name
TSEN15
- Application
-
Alternative Names
TSEN15；C1orf19；tRNA-splicing endonuclease subunit Sen15
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q8WW01
-
Expression Region
1-171aa
-
AA Sequence
MEERGDSEPT PGCSGLGPGG VRGFGDGGGA PSWAPEDAWM GTHPKYLEMM ELDIGDATQV YVAFLVYLDL MESKSWHEVN CVGLPELQLI CLVGTEIEGE GLQTVVPTPI TASLSHNRIR EILKASRKLQ GDPDLPMSFT LAIVESDSTI VYYKLTDGFM LPDPQNISLR R
-
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
TSEN15, a component of the tRNA splicing endonuclease complex, plays a vital role in the maturation of tRNA molecules by facilitating the removal of intronic sequences through a precise splicing mechanism. Mutations in the TSEN15 gene have been associated with neurodegenerative disorders, particularly with pontocerebellar hypoplasia (PCH), which is characterized by developmental delays and neurological deficits. Research into TSEN15 recombinant proteins aims to elucidate its functional mechanisms and interactions within the tRNA splicing pathway, ultimately contributing to a better understanding of the pathogenesis of related diseases. By producing and characterizing recombinant TSEN15, scientists can investigate its structural properties, enzymatic activity, and the impact of various mutations, thereby facilitating the development of potential therapeutic strategies. These studies are significant not only for basic science but also for clinical applications, as they may lead to insights into targeted treatments for the patients affected by TSEN15-related disorders. The ongoing research into TSEN15 underscores the importance of unraveling the complexities of tRNA biogenesis and its implications in human health.
