Analytical Data
-
Gene name
LSM3
- Application
-
Alternative Names
LSM3;U6 snRNA-associated Sm-like Protein LSm3
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P62310
-
Expression Region
1-102aa
-
AA Sequence
MGSSHHHHHHSSGLVPRGSHMGSMADDVDQQQTTNTVEEPLDLIRLSLDE RIYVKMRNDRELRGRLHAYDQHLNMILGDVEETVTTIEIDEETYEEIYKS TKRNIPMLFVRGDGVVLVAPPLRVG
-
Molecular Weight
14 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 LSM3 protein, a member of the LSM (Like-Sm) family, plays a crucial role in RNA processing and regulation, particularly in the context of mRNA stability and decay. This protein is known to form part of the LSM complex, which is essential for the splicing and degradation of RNA transcripts in eukaryotic cells. Research into LSM3 has gained prominence due to its involvement in various cellular processes, including the regulation of gene expression and the response to stress conditions. Abnormalities in LSM3 function can lead to dysregulation of RNA metabolism, which is associated with several diseases, including cancer and neurodegenerative disorders. Understanding the structure and function of LSM3, particularly its interactions with other RNA-binding proteins and its role in RNA surveillance mechanisms, has significant implications for both basic biological research and therapeutic applications. The reconstitution of LSM3 and its complexes has become a focal point of study, allowing researchers to explore its specific interactions and biochemical pathways in a controlled environment, ultimately providing insights into its contribution to cellular homeostasis and potential targets for therapeutic intervention.
