Analytical Data
-
Gene name
INSL6
- Application
-
Alternative Names
RIF1; Relaxin/Insulin-Like Factor 1
-
Species
Human
-
Source
E. coli
-
Tag
N-His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y581
-
Expression Region
Arg21~Phe198
-
Molecular Weight
25kDa
-
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 6 (INSL6) is a member of the insulin superfamily, characterized by its unique structural features and expression profile. It has garnered interest due to its potential roles in metabolic regulation, reproductive biology, and its emerging association with certain pathological conditions. INSL6 is predominantly expressed in tissues such as the testis and placenta, suggesting functions related to reproduction and embryonic development. Research has also indicated its involvement in insulin signaling pathways, implying a possible link to metabolic diseases like obesity and diabetes. Furthermore, INSL6’s expression patterns and functional properties have made it a candidate for exploring novel therapeutic avenues. Recent studies have highlighted the need for recombinant INSL6 protein to investigate its biological functions and mechanisms in vitro and in vivo. This demand has driven the development of techniques for the production and purification of recombinant INSL6, allowing researchers to explore its interactions with receptors and other cellular components. Understanding INSL6 at the molecular level can provide insights into its physiological roles and potential implications for human health, thus underscoring the importance of harnessing recombinant technology for functional analyses in this field.











