Analytical Data
-
Gene name
KNSTRN
- Application
-
Alternative Names
Kinetochore-localized astrin-binding protein (Kinastrin) (Kinetochore-localized astrin/SPAG5-binding protein) (TRAF4-associated factor 1)
-
Species
Human
-
Source
E. coli
-
Tag
N- His
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q9Y448
-
Expression Region
1-316aa
-
Molecular Weight
39.5 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
KNSTRN (Kinesin-13-Associated Protein) is a crucial protein that plays an essential role in cell division and mitotic progression by regulating microtubule dynamics. Its involvement in the proper formation of the spindle apparatus is critical for accurate chromosome segregation. Dysregulation or mutations in KNSTRN have been associated with various malignancies, emphasizing its importance as a potential biomarker and therapeutic target in cancer research. Recent studies have focused on the structural characterization and cellular mechanisms of KNSTRN, revealing its interactions with kinesin motor proteins and other microtubule-associated factors. This research aims to elucidate the precise roles and regulatory pathways of KNSTRN within the mitotic framework. Understanding the dynamics of KNSTRN could provide insights into the fundamental processes of cell division and highlight new avenues for cancer therapies that exploit the vulnerabilities of tumor cells. The ongoing investigation into KNSTRN's structure and function represents a promising frontier in cellular biology and cancer therapeutics.
