Analytical Data
-
Gene name
IRS1
- Application
-
Alternative Names
HIRS1
-
Species
Mouse
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 95% as determined by SDS-PAGE.
-
Uniprot
P35569
-
Expression Region
Pro837~Gln1089
-
Molecular Weight
30kDa
-
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
IRS1 (Insulin Receptor Substrate 1) is a pivotal adaptor protein that plays a crucial role in insulin signaling pathways and metabolic regulation. Alterations in IRS1 function or expression have been implicated in various metabolic disorders, including obesity, insulin resistance, and type 2 diabetes. The study of IRS1 recombinant protein offers significant insights into its structural and functional properties, enabling researchers to explore its interactions with insulin receptors and downstream signaling molecules such as PI3K and Akt. Recombinant IRS1 serves as a valuable tool for elucidating the mechanisms by which insulin signaling is impaired in metabolic diseases. Furthermore, understanding the phosphorylation dynamics and the impact of post-translational modifications on IRS1 activity can aid in identifying potential therapeutic targets for enhancing insulin sensitivity. Recent advances in molecular biology techniques have facilitated the production and characterization of IRS1 as a recombinant protein, allowing for detailed functional assays and structural analyses. This research is essential for developing novel strategies to combat the rising prevalence of metabolic disorders and improving our understanding of insulin signaling pathways.
