Analytical Data
-
Gene name
Ins2
- Application
-
Alternative Names
Ins-2
-
Species
Mouse
-
Source
E. coli
-
Tag
N- His & C- Myc
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P01326
-
Expression Region
25-110aa
-
Molecular Weight
16.9 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
Insulin-like growth factor 2 (IGF2) is a crucial protein involved in growth and development, mainly during fetal growth and postnatal development, acting through the IGF signaling pathway. Research on recombinant IGF2 (Ins2) has gained attention in recent years due to its potential therapeutic applications in regenerative medicine and cancer treatment. IGF2 is known to influence cellular processes such as proliferation, differentiation, and apoptosis, making it a significant target for understanding various diseases, including metabolic disorders and cancers. Recombinant production of IGF2 allows for detailed studies of its structure-function relationships, mechanism of action, and interactions with its receptors. Additionally, the ability to produce Ins2 in a controlled and scalable manner opens avenues for exploring its role in tissue engineering and stem cell biology. Given the increasing incidence of conditions linked to IGF signaling dysregulation, such as obesity and type 2 diabetes, research into Ins2 holds promise for developing targeted therapies. Overall, the study of recombinant Ins2 not only deepens our understanding of fundamental biological processes but also paves the way for innovative approaches to treat diseases associated with growth factor signaling pathways.
