Analytical Data
-
Gene name
RAN
- Application
-
Alternative Names
RAN;ARA24;GTP-binding nuclear Protein Ran
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
P62826
-
Expression Region
1-216aa
-
AA Sequence
AAQGEPQVQFKLVLVGDGGTGKTTFVKRHLTGEFEKKYVATLGVEVHPLVFHTNRGPIKFNVWDTAGQEKFGGLRDGYYIQAQCAIIMFDVTSRVTYKNVPNWHRDLVRVCENIPIVLCGNKVDIKDRKVKAKSIVFHRKKNLQYYDISAKSNYNFEKPFLWLARKLIGDPNLEFVAMPALAPPEVVMDPALAAQYEHDLEVAQTTALPDEDDDL
-
Molecular Weight
51.3kDa
-
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
RAN (Ras-related nuclear protein) is a small GTPase that plays a critical role in various cellular processes, particularly in nucleocytoplasmic transport and cell division. It functions as a molecular switch, existing in active (GTP-bound) and inactive (GDP-bound) states, and regulates the movement of proteins and RNA across the nuclear envelope. Research on RAN and its associated proteins has gained momentum due to its implications in fundamental cellular functions, as well as its involvement in various diseases, including cancer. Abnormalities in RAN signaling pathways have been linked to tumorigenesis and cellular proliferation, making it a potential target for therapeutic intervention. The study of RAN’s structure, function, and interactions with other molecules has provided insights into its role in maintaining cellular homeostasis and its impact on disease mechanisms. Furthermore, RAN has been associated with the regulation of the mitotic spindle and chromosome organization during cell division, underscoring its importance in ensuring accurate genome segregation. Understanding RAN dynamics at the molecular level may facilitate the development of novel strategies to manipulate its activity, which could lead to innovative treatments for disorders marked by defective cellular transport and proliferation. As research progresses, the potential of RAN as a biomarker and a target for drug design remains a compelling avenue in molecular biology and cancer research.
