Analytical Data
-
Gene name
ELOC
- Application
-
Alternative Names
ELOC;TCEB1;Elongin-C
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q15369
-
Expression Region
1-112aa
-
AA Sequence
MGSSHHHHHHSSGLVPRGSHMDGEEKTYGGCEGPDAMYVKLISSDGHEFI VKREHALTSGTIKAMLSGPGQFAENETNEVNFREIPSHVLSKVCMYFTYK VRYTNSSTEIPEFPIAPEIALELLMAANFLDC
-
Molecular Weight
15 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
The research on ELOC (Elongator complex protein 1) recombinant proteins stems from the growing interest in understanding the role of the Elongator complex in transcriptional regulation and cell proliferation. ELOC, as a component of the Elongator complex, is implicated in the modification of tRNA and has been linked to various cellular processes, including RNA polymerase II elongation and gene expression. Dysregulation of ELOC has been associated with several diseases, including cancer and neurological disorders, highlighting its potential as a therapeutic target. The production and characterization of ELOC recombinant proteins not only facilitate the exploration of its biochemical properties but also enable functional studies that can elucidate the complex interactions within the cell. By employing techniques such as site-directed mutagenesis and protein assays, researchers aim to probe the mechanisms by which ELOC influences cellular functions and its role in disease pathology. Overall, the study of ELOC recombinant proteins is crucial for advancing our understanding of cellular dynamics and developing novel therapeutic approaches.











